Distribution

NUDC (Nuclear Distribution C, Dynein Complex Regulator) is a Protein Coding gene. NUDC consists of at least 9 exons ranging from 66 bp to 266 bp in size and 8 introns from 92 bp to 2.0 kb in length, and the total genomic region spans about 8 kb. NUDC was mapped to 1p34-p35 by fluorescence in situ hybridization. This gene encodes a nuclear distribution protein that plays an essential role in mitosis and cytokinesis. Nuclear migration is essential for the growth, development, and cellular function of eukaryotes. NUDC protein plays an important role in nuclear migration. It is widely expressed in the testis, adrenal, and other tissues. NUDC protein is expressed highly in CNE-2 and HNE-2 cells. Anti-NUDC antibody could inhibit the growth of CNE-2 and HNE-2 cells.

Coronin 6, a newly identified member of the coronin family, is highly enriched at adult NMJs and regulates AChR clustering via modulating the interaction between receptors and the actin cytoskeletal network. Coronins are a family of conserved actin-binding proteins originally identified in the actin-rich structure of the amoeba Dictyostelium discoideum . To date, seven members of coronins have been identified in mammals, and most exhibit tissue-specific distribution patterns. Coronin 6 is prominently expressed in adult muscle and enriched at the NMJ. Studies with cultured myotubes reveal that Coronin 6 regulates both agrin- and laminin-induced AChR clustering and is important for anchoring AChRs onto the actin cytoskeleton. Also, both the C-terminal region and a conserved Arg29 residue at the N terminus of Coronin 6 are essential for its actin-binding activity and stabilization of AChR–cytoskeleton linkage. Importantly, in vivo knockdown of Coronin 6 in mouse skeletal muscle fibers leads to destabilization of AChR clusters, which demonstrates that Coronin 6 is a critical regulator of AChR clustering at the postsynaptic region of the NMJs through modulating the receptor-anchored actin cytoskeleton. The human Coronin 6 has five isoforms produced by alternative splicing, and tissue-specific expression of these isoforms are unclear.

Ephrin-B2 controls platelet-derived growth factor receptor β (PDGFRβ) distribution in the VSMC plasma membrane, endocytosis, and signaling in a fashion that is highly distinct from its role in the endothelium. Ephrin-B2 is an important regulator of PDGFRβ endocytosis and thereby acts as a molecular switch controlling the downstream signaling activity of this receptor in mural cells.

Chimeric antigen receptor (CAR) T cells, a type of cell-based immunotherapy, have shown some promising results in multiple myeloma, a bone marrow cancer.The orphan G protein–coupled receptor, class C group 5 member D (GPRC5D), normally expressed only in the hair follicle, Using quantitative immunofluorescence, we determined that GPRC5D protein is expressed on CD138 MM cells from primary marrow samples with a distribution that was similar to, but independent of, BCMA. GPRC5D Protein-VLP, Mouse, Recombinant is expressed in HEK293 mammalian cells. The predicted molecular weight is 39.90 kDa and the accession number is Q9JIL6-1.

Macrophages play key roles during cardiovascular diseases (CVD) and their related complications.Apelin (APLN) is a key molecule, whose roles during CVD have been documented previously. Therefore, it has been hypothesized that APLN may perform its roles via modulation of macrophages. Additionally, due to the widespread distribution of the CVD, more effective therapeutic strategies need to be developed to overcome the related complications. APLN Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with C-hFc tag. The predicted molecular weight is 32.9 kDa and the accession number is Q9ULZ1.

Cystatins are natural inhibitors of papain-like (family C1) and legumain-related (family C13) cysteine peptidases. The mammalian cystatin superfamily members are of three major types, including the type 1 cystatins (stefins), type 2 cystatins and the kininogens. As a member of type 2 cystatin, cystatin D is a single-domain protein and also has cysteine residues that form disulfide bridges. In contrast with the wider distribution of all the other family 2 cystatins, cystatin D is tissue-restricted expressed and has been found only in saliva and tears. and meanwhile, it displays an inhibition profile with a preferential inhibition on cathepsin S, H, L. Although the exact functions are largely unknown, it has reported that cystatin D is involved in the inhibition of virus replication and apoptosis.

CCL28 chemokine is expressed by epithelial cells of various mucosal tissues. This chemokine binds to CCR3 and CCR10 receptors and plays an essential role in the IgA antibody secreting cells (IgA-ASC) homing to mucosal surfaces and lactating mammary gland as well. Besides, CCL28 has been shown to exert a potent antimicrobial activity against both Gram-negative and Gram-positive bacteria and fungi. The potent antimicrobial function of CCL28 combined with its wide distribution in mucosal tissues and secretions suggest that this protein plays an important role in innate immune protection of the epithelial surfaces. CCL28 is a human chemokine constitutively expressed by epithelial cells in diverse mucosal tissues and is known to attract a variety of immune cell types including T-cell subsets and eosinophils. Elevated levels of CCL28 have been found in the airways of individuals with asthma, and previous studies have indicated that CCL28 plays a vital role in the acute development of post-viral asthma. CCL28 presents a novel target for the development of alternative asthma therapeutics. The dental decay of children leads to the secretion of chemokine CCL28, which promotes the secretion of sIgA in saliva. CC chemokine ligand28 (CCL28) has been reported as a severity marker in atopic dermatitis.

Acyl-coenzyme A: cholesterol acyltransferase (ACAT) is an intracellular enzyme that produces cholesteryl esters in various tissues. In mammals, two ACAT genes (ACAT1 and ACAT2) have been identified. Together, these two enzymes are involved in storing cholesteryl esters as lipid droplets, in macrophage foam-cell formation, in absorbing dietary cholesterol, and in supplying cholesteryl esters as part of the core lipid for lipoprotein synthesis and assembly. The key difference in tissue distribution of ACAT1 and ACAT2 between humans, mice and monkeys is that, in adult human liver (including hepatocytes and bile duct cells), the major enzyme is ACAT1, rather than ACAT2. There is compelling evidence implicating a role for ACAT1 in macrophage foam-cell formation, and for ACAT2 in intestinal cholesterol absorption.Ubiquitin linkage to cysteine is an unconventional modification targeting protein for degradation. However, the physiological regulation of cysteine ubiquitylation is still mysterious. Here we found that ACAT2, a cellular enzyme converting cholesterol and fatty acid to cholesteryl esters, was ubiquitylated on Cys277 for degradation when the lipid level was low. gp78-Insigs catalysed Lys48-linked polyubiquitylation on this Cys277. A high concentration of cholesterol and fatty acid, however, induced cellular reactive oxygen species (ROS) that oxidized Cys277, resulting in ACAT2 stabilization and subsequently elevated cholesteryl esters. Furthermore, ACAT2 knockout mice were more susceptible to high-fat diet-associated insulin resistance. By contrast, expression of a constitutively stable form of ACAT2 (C277A) resulted in higher insulin sensitivity. ACAT2 is an appealing target for therapy to reduce coronary heart disease.

IP6K1 (Inositol Hexakisphosphate Kinase 1) is a Protein Coding gene. 2 alternatively spliced human isoforms have been reported. IHPK1 is an inositol hexaphosphate kinase (IHPK) protein that belongs to the inositol phosphokinase (IPK) family. IHPK proteins are likely responsible for the conversion of inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7 PP-InsP5). IHPK1 may also convert 1,3,4,5,6-pentakisphosphate (InsP5) to PP-InsP4 and affect the growth-suppressive and apoptotic activities of interferon-beta in some ovarian cancers. During cell death, IHPK1 activity is enhanced, and the intracellular InsP7 level is augmented. The distribution of IHPK1 or another predisposing gene affected by the position effect of translocation may explain the T2DM phenotype at least in this family.

ZW10 Interactor is localized to the kinetochores from late Prophase to Anaphase and has a uniform distribution in the cytoplasm of Interphase cells. ZWINT interacts ZW10, MIS12 and NDC80 subunit of the NDC80 complex specifically during mitosis. ZWINT is a part of the MIS12 complex which is required for kinetochore formation and spindle checkpoint activity. In addition, ZWINT is required to target ZW10 to the kinetochore at prometaphase.

Sperm Equatorial Segment Protein 1 (SPESP1) is a member of the SPESP1 family. SPESP1 is highly expressed in the testis, where it is localized to the acrosome of postmeiotic stages of spermiogenesis; it is expressed at lower levels in the placenta and fetal lung. SPESP1 is involved in the multicellular organisimal development. Disruption of SPESP1 leads to abnormal distribution of sperm proteins resulting in a detached membrane from the equatorial segment and less fertile sperm. SPESP1 may interact with IZUMO1 and MN9 antigen and it contains an N-glycosylation site as well as several cAMP-dependent kinase, protein kinase C, and casein kinase II consensus phosphorylation sites.

Interleukin 17 (also known as CTLA‑8) is a T cell‑expressed pleotropic cytokine. IL‑17 binds to IL‑17 receptor (IL‑17 R) which shares no homology with any known family of receptors. While the expression of IL‑17 is restricted to activated T cells, the IL‑17 R mRNA exhibits a broad tissue distribution, and has been detected in virtually all cells and tissues tested. The human IL‑17 R gene was localized to chromosome 22.

Like parvalbumins, SCP's seem to be more abundant in fast contracting muscles, but no functional relationship can be established from this distribution. SCP alpha chain Protein, Penaeus sp., Recombinant (His & Myc & SUMO) is expressed in E. coli expression system with N-10xHis-SUMO and C-Myc tag. The predicted molecular weight is 42.0 kDa and the accession number is P02636.

MEP1B (Meprin A Subunit Beta) is a Protein Coding gene. This gene encodes the beta subunit. Targeted disruption of this gene in mice affects embryonic viability, renal gene expression profiles, and distribution of the membrane-associated alpha subunit in the kidney and intestine. Meprins are cell membrane, oligomeric metalloendopeptidases composed of two distinct but evolutionarily related subunits, alpha, and beta. MEP1A is mapped to the short arm of chromosome 6 by the use of radiation and somatic cell hybrids. More specifically, it is localized between the centromere and GSTA2 in 6p11-p12. MEP1B mapped to chromosome 18, by the use of somatic cell hybrids, in 18q12.2-q12.3, proximal to the TTR PALB gene. Diseases associated with MEP1B include Powassan Encephalitis and Deafness, Autosomal Dominant 31.

LSP1 (Lymphocyte Specific Protein 1) is a Protein Coding gene. This gene encodes an intracellular F-actin binding protein. The protein is expressed in lymphocytes, neutrophils, macrophages, and endothelium and may regulate neutrophil motility, adhesion to fibrinogen matrix proteins, and transendothelial migration. LSP1 is a lymphocyte-specific intracellular Ca2(+)-binding protein. LSP1 localizes to nascent phagocytic cups during Fcgamma receptor-mediated phagocytosis, where it displays the same spatial and temporal distribution as the actin cytoskeleton. Down-regulation of LSP1 severely reduces the phagocytic activity of macrophages, clearly demonstrating a crucial role for this protein in Fcgamma receptor-mediated phagocytosis. LSP1, expressed in endothelial cells, plays a pivotal role in regulating subsequent recruitment steps following leukocyte adhesion.

Complexin-2 (CPLX2), a member of the complexin synaphin family, is a soluble pre-synaptic protein believed to regulate neurotransmitter release from pre-synaptic terminals. Complexins are soluble proteins that regulate the activity of soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes necessary for vesicle fusion. Complexins are unable to bind to monomeric SNARE proteins but bind with high affinity to ternary SNARE complexes and with lower affinity to target SNARE complexes. Complexin 1 (CX1) and complexin 2 (CX2) are presynaptic proteins that modulate neurotransmitter release and are used as markers of inhibitory and excitatory synapses, respectively. CPLX2 is localized in pre-synaptic terminals in mature brain. The G71-P89 region of CPLX2 is essential and sufficient for preferential axonal distribution. CPLX2 participates in the Ca(2+)-sensitive regulatory pathway for zymogen granule exocytosis. Complexin-2 is a key player in normal neurological function, and its downregulation could lead to changes in neurotransmitter release sufficient to cause significant behavioural abnormalities such as depression. It is involved in synaptogenesis and the modulation of neurotransmitter release.

PDE1C belongs to the cyclic nucleotide phosphodiesterase family, PDE1 subfamily. Phosphodiesterases (PDEs) are a family of related phosphohydrolyases that selectively catalyze the hydrolysis of 3' cyclic phosphate bonds in adenosine and or guanine 3',5' cyclic monophosphate (cAMP and or cGMP). They regulate the cellular levels, localization and duration of action of these second messengers by controlling the rate of their degradation. PDEs are expressed ubiquitously, with each subtype having a specific tissue distribution. These enzymes are involved in many signal transduction pathways and their functions include vascular smooth muscle proliferation and contraction, cardiac contractility, platelet aggregation, hormone secretion, immune cell activation, and they are involved in learning and memory. PDE1C has a high affinity for both cAMP and cGMP. It is expressed in several tissues, including brain and heart. As a cyclic nucleotide phosphodiesterase, PDE1C has a dual-specificity for the second messengers cAMP and cGMP.

SUSD4, also known as sushi domain-containing protein 4, is a hypothetical cell surface protein whose tissue distribution and function are completely unknown. SUSD4 is detectable in murine brains, eyes, spinal cords, and testis but not other tissues. In brains, SUSD4 is highly expressed in the white matter on oligodendrocytes axons, and in eyes, it is exclusively expressed on the photoreceptor outer segments. In in vitro complement assays, SUSD4 augments the alternative but not the classical pathway of complement activation at the C3 convertase step. SUSD4 deficiency may cause autism or Fryns syndrome, both of which are genetic diseases with severe abnormal neurological development and or functions.

Transglutaminases (TGase) are a family of calcium-dependent acyl-transfer enzymes ubiquitously expressed in mammalian cells and responsible for catalyzing covalent cross-links between proteins or peptides. Transglutaminase 3 (TGM3) is a member of a family of Ca2+-dependent enzymes that catalyze covalent cross-linking reactions between proteins or peptides. TGM3 isoform is widely expressed and is important for epithelial barrier formation. It is a zymogen, requiring proteolysis for activity. Calcium-activated TGM3 can bind, hydrolyze, and is inhibited by GTP, despite lacking structural homology with other GTP binding proteins. TGM3 displays a diffuse cytoplasmic distribution in vitro consistent with its proposed role in the early phase of cornified cell envelope assembly in the cytoplasm. TGM3-driven specific isopeptide bonds between intermediate filaments and KAPs participate to the progressive scaffolding of the hair shaft. Additionally, TGM3 may be a novel prognostic biomarker for esophageal squamous cell carcinoma (ESCC).

Carbonic anhydrase 5B, also known as carbonate dehydratase VB, carbonic anhydrase VB, CA-VB and CA5B, is amember of the alpha-carbonic anhydrase family. The strongest expression of CA5B CA-VB is in heart, pancreas, kidney, placenta, lung, and skeletal muscle. It is not expressed in liver. Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes first discovered in 1933 that catalyze the reversible hydration of carbon dioxide. CAs participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. CAs show extensive diversity in tissue distribution and in their subcellular localization. CA5B CA-VB is localized in the mitochondria and shows the highest sequence similarity to the other mitochondrial CA5A CA-VA. CA5B CA-VB has a wider tissue distribution than CA5A CA-VA, which is restricted to the liver. The differences in tissue distribution suggest that the two mitochondrial carbonic anhydrases evolved to assume different physiologic roles. CA5A CA-VA is activated by histamine, L-adrenaline, L- and D-histidine, and L- and D-phenylalanine. It is inhibited by coumarins, sulfonamide derivatives such as acetazolamide and Foscarnet (phosphonoformate trisodium salt). CA5B CA-VB is inhibited by coumarins, sulfonamide derivatives such as acetazolamide (AZA), saccharin and Foscarnet (phosphonoformate trisodium salt).

PTGS2, also known as COX-2, is s component of Prostaglandin-endoperoxide synthase (PTGS). PTGS, also known as cyclooxygenase, is the key enzyme in prostaglandin biosynthesis, and acts both as a dioxygenase and as a peroxidase. There are two isozymes of PTGS: a constitutive PTGS1 and an inducible PTGS2, which differ in their regulation of expression and tissue distribution. PTGS2 is overexpressed in many cancers. The overexpression of PTGS2 along with increased angiogenesis and GLUT-1 expression is significantly associated with gallbladder carcinomas. Furthermore the product of COX-2, PGH2 is converted by prostaglandin E2 synthase into PGE2, which in turn can stimulate cancer progression. Consequently inhibiting COX-2 may have benefit in the prevention and treatment of these types of cancer. PTGS2 is regulated by specific stimulatory events, suggesting that it is responsible for the prostanoid biosynthesis involved in inflammation and mitogenesis. It mediates the formation of prostaglandins from arachidonate and may have a role as a major mediator of inflammation and or a role for prostanoid signaling in activity-dependent plasticity.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy

Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS.

Required for brain and eye development. Promotes the disassembly of phosphorylated vimentin intermediate filaments (IF) during mitosis and may play a role in the trafficking and distribution of IF proteins and other cellular factors to daughter cells during progenitor cell division. Required for survival, renewal and mitogen-stimulated proliferation of neural progenitor cells. Nestin NES Protein, Human, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 27.8 kDa and the accession number is P48681.

Glypican-5 (GPC5), is a cell membrane protein that belongs to the glypican family. The glypicans compose a family of glycosylphosphatidylinositol-anchored heparan sulfate proteoglycans that may play a role in the control of cell division and growth regulation. So far, six members (Glypican-1 GPC1, Glypican-2 GPC2, Glypican-3 GPC3, Glypican-4 GPC4, Glypican-5 GPC5, Glypican-6 GPC6) of this family are known in the vertebrates. In the adult, Glypican-5 is primarily expressed in the brain. It is also detected in the fetal brain, lung, and liver. Glypican-5 enhances the intracellular signaling of FGF2 and HGF. It alters the cellular distribution of FGF2. The properties of Glypican-5 make it an attractive target for therapeutic intervention in rhabdomyosarcomas and other tumors that amplify and or overexpress its gene. Glypican-5 is overexpressed in lymphoma cell lines that had shown amplification. It is a likely target for amplification, and that over-expression of GPC5 may contribute to the development and or progression of lymphomas and other tumors.

Latexin, also known as endogenous carboxypeptidase inhibitor, tissue carboxypeptidase inhibitor, TCI, ECI, and LXN, is a cytoplasm protein that belongs to the protease inhibitor I47 (latexin) family. It is highly expressed in the heart, prostate, ovary, kidney, pancreas, and colon. Latexin LXN is the only known endogenous specific inhibitor of zinc-dependent metallocarboxypeptidases (MCPs) present in mammalians so far. Latexin is originally identified as a molecular marker for the regional specification of the neocortex in development in rats. The 222 amino acid latexin in the human shows different expression distribution with high levels in heart, prostate, ovary, kidney, pancreas, and colon, but only moderate or low levels in other tissues including the brain. Latexin is also expressed at high levels and is inducible in macrophages in concert with other protease inhibitors and potential protease targets, and thus is suggested to play a role in inflammation and innate immunity pathways. Despite the non-detectable sequence similarity with plant and parasite inhibitors, Latexin is related to a human putative tumor suppressor protein, TIG1. Also, Latexin is implicated in Alzheimer's disease.

Carbonic anhydrase 7, also known as carbonate dehydratase VII, carbonic anhydrase VII, CA-VII and CA7, is a cytoplasm protein which belongs to thealpha-carbonic anhydrase family. Carbonic anhydrases are a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. They participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. Carbonic anhydrases show extensive diversity in tissue distribution and in their subcellular localization. CA7 CA-VII is predominantly expressed in the salivary glands. Alternative splicing in the coding region results in multiple transcript variants encoding different isoforms.

The carbonic anhydrases (or carbonate dehydratases) are classified as metalloenzyme for its zinc ion prosthetic group and form a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate and protons, a reversible reaction that takes part in maintaining acid-base balance in blood and other tissues. The carbonic anhydrasekl (CA) family consists of at least 11 enzymatically active members and a few inactive homologous proteins. The CAXIII is a member of the CA family, which owns a globular molecule with high structural similarity to cytosolic isozymes, CAI, II, and III. Recombinant mouse CAXIII showed catalytic activity similar to those of mitochondrial CAV and cytosolic CAI. In human tissues, CAXIII expression was identified in the thymus, small intestine, spleen, prostate, ovary, colon, and testis. In mouse, positive tissues included the spleen, lung, kidney, heart, brain, skeletal muscle, and testis. In conclusion, the predicted amino acid sequence, structural model, distribution, and activity data suggest that CAXIII represents a novel enzyme, which may play important physiological roles in several organs.

Lipocalin-1, also known as Von Ebner gland protein, VEG protein, Tear Prealbumin, VEGP, Tear lipocalin, and LCN1 is a secreted protein that belongs to the calycin superfamily and Lipocalin family. Human Lipocalin-1 VEGP was originally described as a major protein of human tear fluid, which was thought to be tear specific. Lipocalin-1 VEGP is identical to lingual von Ebner's gland protein and is also produced in the prostate, nasal mucosa, and tracheal mucosa. Homologous proteins have been found in the rat, pig, and probably dog and horse. Lipocalin-1 VEGP is an unusual lipocalin member, because of its high promiscuity for relative insoluble lipids and binding characteristics that differ from other members. Lipocalin-1 VEGP acts as the principal lipid-binding protein in tear fluid, a more general physiological function has to be proposed due to its wide distribution and properties. Lipocalin-1 VEGP would be ideally suited for scavenging of lipophilic, potentially harmful substances and thus might act as a general protection factor of epithelia. Lipocalin-1 LCN1 could play a role in taste reception. It could be necessary for the concentration and delivery of sapid molecules in the gustatory system. Lipocalin-1 LCN1 can bind various ligands, with chemical structures ranging from lipids and retinoids to the macrocyclic antibiotic rifampicin and even to microbial siderophores. It exhibits an extremely wide ligand pocket.

Proto-oncogene tyrosine-protein kinase Yes, also known as Proto-oncogene c-Yes, p61-Yes and YES1, is a cytoplasm protein that belongs to the protein kinase superfamily, Tyr protein kinase family and SRC subfamily. YES1 c-Yes contains one protein kinase domain, one SH2 domain and one SH3 domain. It is thought that the subcellular distribution of Src-family tyrosine kinases, including c-Yes binding to the cellular membrane, is membranous and or cytoplasmic. YES1 c-Yes protein tyrosine kinase is known to be related to malignant transformation. YES1 c-Yes and c-Src are the two most closely related members of the Src family of nonreceptor tyrosine kinases. Although there is much evidence to support redundancy in signaling between these two kinases. YES1 c-Yes promotes the formation of the tight junction by phosphorylating occludin, while c-Src signaling downregulates occludin formation in a Raf-1 dependent manner. YES1 c-Yes has tyrosine kinase activity. It promotes infectivity of Neisseria gonorrhoeae in epithelial cells by phosphorylating MCP CD46.

The Galectin family of proteins, with specificity for Nacetyllactosaminecontaining glycoproteins, consists of beta-galactoside binding lectins containing homologous carbohydrate recognition domains (CRDs). They also possess hemagglutination activity, which is attributable to their bivalent carbohydrate binding properties. Galectins are active both intracellularly and extracellularly. Although they are localized primarily in the cytoplasm and lack a classical signal peptide, galectins can also be secreted by one or more unidentified, non-classical, secretory pathways. They have diverse effects on many cellular functions including adhesion, migration, polarity, chemotaxis, proliferation, apoptosis, and differentiation. Galectins may therefore play a key role in many pathological states, including autoimmune diseases, allergic reactions, inflammation, tumor cell metastasis, atherosclerosis, and diabetic complications. The galectins have been classified into the prototype galectins(1, 2, 5, 7, 10, 11, 13, 14), which contain one CRD and exist either as a monomer or a noncovalent homodimer. The chimera galectins(Galectin3) containing one CRD linked to a nonlectin domain, and the tandemrepeat Galectins(4, 6, 8, 9, 12) consisting of two CRDs joined by a linker peptide.Galectins lack a classical signal peptide and can be localized to the cytosolic compartments where they have intracellular functions. However, via one or more as yet unidentified nonclassical secretory pathways, galectins can also be secreted to function extracellularly. Individual members of the galectin family have different tissue distribution profiles and exhibit subtle differences in their carbohydrate-binding specificities. Each family member may preferentially bind to a unique subset of cell surface glycoproteins.

The Atg8 LC3 GABARAP family of proteins, a group that has structural homology with ubiquitin, connects with a large set of binding partners to function in macroautophagy (hereafter autophagy). GABARAP in tumorigenesis in vivo by delaying cell death and its associated immune-related response. GABARAPs are uniquely required for antimicrobial host defense through cytosolic distribution of interferon-inducible GTPases. GABARAPs as the first known direct interaction partners of Nef that are essential for its plasma membrane localization.

Serpins are the largest and most diverse family of serine protease inhibitors which are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner.Mouse SerpinB8, also known as Cytoplasmic antiproteinase 2, Peptidase inhibitor 8, SerpinB8, PI-8, SERPINB8 and CAP2, is a member of the Serpin superfamily. SERPINB8 was broadly expressed. In normal neuroendocrine tissues, strongest SerpinB8 expression was detected in islets of Langerhans of the pancreas. Moderate SerpinB8 expression was observed in neuroendocrine cells of the thyroid, adrenal cortex, colon, and pituitary gland. In the pancreas, SerpinB8 is specifically expressed by insulin-producing beta cells, and can be used as an additional diagnostic immunohistochemical marker. Mouse SerpinB8 distribution alters during kidney regeneration, possibly to control a prohormone convertase involved in inflammation or tissue repair.

Aminopeptidase P (APP) is a hydrolase specific for N-terminal imido bonds, which are common to several collagen degradation products, neuropeptides, vasoactive peptides, and cytokines. A membrane-bound and soluble form of this enzyme (XPNPEP2) have been identified as products of two separate genes. XPNPEP2, the X-linked gene that encodes membranous aminopeptidase P (APP), has been reported to associate with APP activity. The membrane aminopeptidase P (XPNPEP2) is largely limited in distribution to endothelia and brush border epithelia. APP and XPNPEP2 contain homologous blocks of sequence common to members of the pita bread-fold protein family, of which Escherichia coli methionine aminopeptidase is the prototype. The C-2399A variant in XPNPEP2 is associated with reduced APP activity and a higher incidence of AE-ACEi. XPNPEP2 mRNA was detected in fibroblasts that carry the translocation, suggesting that this gene at least partially escapes X inactivation. XPNPEP2 is a candidate gene for premature ovarian failure (POF).

RAMP3 belongs to the RAMP family. Members of this family are single-transmembrane-domain proteins, called receptor (calcitonin) activity modifying proteins (RAMPs). RAMPs have a wide biological distribution; high concentrations are found in the brain, lung, liver, heart and spleen with lower expression levels present in the testes, gastrointestinal tract and thyroid. RAMPs are type I transmembrane proteins with an extracellular N terminus and a cytoplasmic C terminus. They are required to transport calcitonin-receptor-like receptor (CRLR) to the plasma membrane. CRLR, a receptor with seven transmembrane domains, can function as either a calcitonin gene-related peptide (CGRP) receptor or an adrenomedullin receptor, depending on which members of the RAMP family are expressed. In the presence of RAMP3 protein, CRLR functions as an adrenomedullin receptor.

ORM2 belongs to the calycin superfamily, lipocalin family. Lipocalins share limited regions of sequence homology and a common tertiary structure architecture. They transport small hydrophobic molecules such as steroids, bilins, retinoids, and lipids. Lipocalins can be found in gram-negative bacteria, vertebrate cells, and invertebrate cells, and plants. They are associated with many biological processes. ORM2 functions as a transport protein in the bloodstream. It is expressed by the liver and secreted in plasma. It seems that ORM2 function in modulating the activity of the immune system during the acute-phase reaction. It binds various hydrophobic ligands in the interior of its beta-barrel domain. It also binds synthetic drugs and influences their distribution and availability.

VAMP3, also known as cellubrevin, is a member of the vesicle-associated membrane protein (VAMP) synaptobrevin family. Synaptobrevins VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein are the main components of a protein complex involved in the docking and or fusion of synaptic vesicles with the presynaptic membrane. Because of VAMP3 gene's high homology to other known VAMPs, its broad tissue distribution, and its subcellular localization, VAMP3 was shown to be the human equivalent of the rodent cellubrevin. In platelets VAMP3 resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation.

GOPC, also known as PIST, interacts specifically with TC1 (a Rho-family small GTPase)] as a binding partner for Rhotekin. Rhotekin associates with PIST in vitro and both polarized and non-polarized MDCK (Madin-Darby canine kidney) cells. The C-terminal SPV (Ser-Pro-Val) motif of Rhotekin binds to the PDZ domain of PIST. The co-localization of PIST and Rhotekin at the Golgi apparatus can be detected in non-polarized fibroblast-like MDCK cells and AJs (adherens junctions) in the fully polarized cells. PIST and Rhotekin are recruited from the cytosol to AJs as the cell becomes polarized. Expression of constitutively active Rho or prevention of Rhotekin-PIST interaction induced diffuse cytoplasmic distribution of Rhotekin in polarized MDCK cells. GOPC may regulate CFTR chloride currents and acid-induced ACCN3 currents by modulating cell surface expression of both channels. It may also regulate the intracellular trafficking of the ADR1B receptor. GOPC is ubiquitously expressed and its overexpression results in CFTR intracellular retention and degradation in the lysosomes.

Trefoil factor family (TFF) peptides are involved in the maintenance of epithelial integrity and epithelial restitution. Trefoil factor-3 (TFF3) is an estrogen-regulated gene associated with prognosis in different types of cancer. The presence and localization of TFF3 peptide was associated with the embryonic stage and tissue differentiation. TFF3 peptide distribution specific to the germ layers was not observed. The role of TFF3 peptide in cell migration and differentiation, immune response, and apoptosis might be associated with specific embryonic epithelial cells. TFF3 peptide may also be considered as a marker for mucosal maturation. Trefoil factor 3 (TFF3) serves an important role in intestinal mucosal damage and healing, and contributes to the pathogenesis and treatment of inflammatory bowel disease (IBD). The involvement of TFF3 in the pathogenesis of rhonchopathy and OSA and lead to the hypothesis that reduction of TFF3 production by the epithelium and subepithelial mucous glands of the uvula contributes to an increase in breathing resistance due to a change in mucus organization.

Copine-1(CPNE1) encodes a calcium-dependent protein which belongs to the copine family. CPNE1contains two N-terminal type II C2 domains and an integrin A domain-like sequence in the C-terminus. However, CPNE1 does not contain a predicted signal sequence or transmembrane domains. CPNE1 may regulate molecular events at the interface of the cell membrane and cytoplasm. CPNE1 has a broad tissue distribution and it may function in membrane trafficking.

Chimeric antigen receptor (CAR) T cells, a type of cell-based immunotherapy, have shown some promising results in multiple myeloma, a bone marrow cancer.The orphan G protein–coupled receptor, class C group 5 member D (GPRC5D), normally expressed only in the hair follicle, Using quantitative immunofluorescence, we determined that GPRC5D protein is expressed on CD138 MM cells from primary marrow samples with a distribution that was similar to, but independent of, BCMA. GPRC5D Protein-VLP, Cynomolgus, Recombinant is expressed in HEK293 mammalian cells. The predicted molecular weight is 35.10 kDa and the accession number is A0A2K5W6I7.

Modifies the subcellular distribution of heterogeneous nuclear ribonucleoprotein K (HNRNPK) and may contribute to modulate HNRNPK functions related to processing and export of mRNAs during ASFV infection.

Macrophages play key roles during cardiovascular diseases (CVD) and their related complications.Apelin (APLN) is a key molecule, whose roles during CVD have been documented previously. Therefore, it has been hypothesized that APLN may perform its roles via modulation of macrophages. Additionally, due to the widespread distribution of the CVD, more effective therapeutic strategies need to be developed to overcome the related complications. APLN Protein, Mouse, Recombinant (hFc) is expressed in HEK293 mammalian cells with C-hFc tag. The predicted molecular weight is 33 kDa and the accession number is Q9R0R4.

INSL4 (Insulin-Like 4) is a Protein Coding gene. An important paralog of this gene is RLN1. INSL4 encodes a precursor that undergoes post-translational cleavage to produce 3 polypeptide chains, A-C, that form tertiary structures composed of either all three chains or just the A and B chains. INSL4 is a member of the insulin family, which includes insulin, IGF-I, IGF-II, relaxin, and INSL3.INSL4 distribution was tissue- and cell-specific. Indeed, INSL4 mRNA was most abundant in syncytiotrophoblast cells. In fetal tissues, INSL4 mRNA was identified in the perichondrium of all four limbs, vertebrae, and ribs. Diseases associated with INSL4 include Placenta Accreta and Chromosome 9P Deletion Syndrome.

Lysophospholipase II (LYPLA2, LPL-II, or LysoPLA II), also known as Acyl-protein thioesterase 2 (APT-2), belongs to the AB hydrolase 2 family. This enzyme has lysophospholipase activity and may hydrolyze fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Acyl-protein thioesterase 1 (APT-1) and Acyl-protein thioesterase 2 (APT-2) are cytosolic lysophospholipids hydrolyzing enzymes. The serum activity of APT-1 may play an important role in the determination of the concentration of des-acyl ghrelin in circulation, especially under septic inflammation. APT-2 LYPLA2 is expressed both in CHO-K1 and HeLa cells and its overexpression increased the deacylation rate of single acylated GAP-43 and affected the steady-state localization of diacylated GAP-43 and H-Ras. Thus, the results demonstrate that APT-2 LYPLA2 is the protein thioesterase involved in the acylation deacylation cycle operating in GAP-43 subcellular distribution.

Abhydrolase domain containing 4 (ABHD4), also known as alpha beta-hydrolase 4 (ABH4) , or lyso-N-acylphosphatidylethanolamine lipase, which belongs to the ABHD4 ABHD5 subfamily of peptidase S33 family. Abhydrolase domain containing (ABHD) gene was a small group belongs to alpha beta hydrolase superfamily. Known members of this group are all found to be involved in important biochemical processes and related to various diseases. The alpha beta-hydrolase 4 (ABH4) is a lysophospholipase phospholipase B that selectively hydrolyzes N-acyl phosphatidylethanolamines (NAPEs) and lysoNAPEs. ABH4 accepts lysoNAPEs bearing both saturated and polyunsaturated N-acyl chains as substrates and displays a distribution that closely mirrors lysoNAPE-lipase activity in mouse tissues. The existence of an NAPE-PLD-independent route for NAE biosynthesis and suggest that ABH4 plays a role in this metabolic pathway by acting as a (lyso)NAPE-selective lipase.

SRFBP1 contains 7 WD repeats and belongs to the WD repeat STRAP family. SRFBP1 may play a role in the cellular distribution of the SMN complex. The SMN complex plays an essential role in spliceosomal snRNP assembly in the cytoplasm and is required for pre-mRNA splicing in the nucleus. SRFBP1 negatively regulates TGF-beta signaling but positively regulates the PDPK1 kinase activity by enhancing its autophosphorylation and by significantly reducing the association of PDPK1 with 14-3-3 protein. SRFBP1 may be involved in regulating transcriptional activation of cardiac genes during the aging process. It also may play a role in biosynthesis and or processing of SLC2A4 in adipose cells.

Serine threonine-protein kinase SRPK1, also known as SFRS protein kinase 1, Serine arginine-rich protein-specific kinase 1, SR-protein-specific kinase 1 and SRPK1, is a cytoplasm and nucleus protein that belongs to the protein kinase superfamily and CMGC Ser Thr protein kinase family. Isoform 2 of SRPK1 is predominantly expressed in the testis but is also present at lower levels in heart, ovary, small intestine, liver, kidney, pancreas and skeletal muscle. Isoform 1 of SRPK1 is only seen in the testis, at lower levels than isoform 2. SRPK1 hyperphosphorylates RS domain-containing proteins such as SFRS1, SFRS2 and ZRSR2 on serine residues during metaphase but at lower levels during interphase. SRPK1 plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. SRPK1 locks onto SFRS1 to form a stable complex and processively phosphorylates the RS domain. SRPK1 appears to mediate HBV core protein phosphorylation which is a prerequisite for pregenomic RNA encapsidation into viral capsids.