forms

Expression system: E. coli
Length: 2-160, Full Length of Mature Protein
Activity: Not Tested

G protein-coupled receptor kinase 6, also known as G protein-coupled receptor kinase GRK6, GRK6, and GPRK6, is a lipid-anchor protein that belongs to the protein kinase superfamily, AGC Ser Thr protein kinase family, and GPRK subfamily. GRK6 GPRK6 contains one AGC-kinase C-terminal domain, one protein kinase domain, and one RGS domain. This protein phosphorylates the activated forms of G protein-coupled receptors thus initiating their deactivation. Several transcript variants encoding different isoforms have been described. GRK6 GPRK6 is widely expressed. GRK6 GPRK6 silencing causes suppression of signal transducer and activator of transcription 3 (STAT3) phosphorylation associated with a reduction in MCL1 levels and phosphorylation, illustrating a potent mechanism for the cytotoxicity of GRK6 inhibition in multiple myeloma (MM) tumor cells. GRK6 also appears to be involved in responses to morphine. Inhibition of GRK6 represents a uniquely targeted novel therapeutic strategy in human multiple myeloma.

GOT1 (Glutamic-Oxaloacetic Transaminase 1) is a Protein Coding gene. GOT1 belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Glutamic-oxaloacetic transaminase is a pyridoxal phosphate-dependent enzyme that exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, respectively. GOT plays a role in amino acid metabolism and the urea and tricarboxylic acid cycles. The two enzymes are homodimeric and show close homology. GOT1 is an important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. GOT1 is broadly expressed in the heart, liver, and other tissues. Diseases associated with GOT1 include Aspartate Aminotransferase, Serum Level Of, Quantitative Trait Locus 1, and Lujo Hemorrhagic Fever.

Dog dander is an important cause of respiratory allergy but its content of allergenic components is still incompletely known. The size and the amino acid composition of the ligand-binding pocket indicate that Can f 4 is capable of binding only relatively small hydrophobic molecules which are different from those that Can f 2 is able to bind. The crystal structure of Can f 4 contained both monomeric and dimeric forms of the allergen, suggesting that Can f 4 is able to form transient (weak) dimers. The existence of transient dimers in solution was confirmed by use of native mass spectrometry. The dimeric structure of Can f 4 is formed when the ends of four β-strands are packed against the same strands from the second monomer.

BDNF is a member of thenerve growth factorfamily. It is highly expressed in hippocampus, amygdala, cerebral cortex and cerebellum. It also can be detected in heart, lung, skeletal muscle, testis, prostate and placenta. BDNF is induced by cortical neurons, and is necessary for survival of striatal neurons in the brain. During development, BDNF promotes the survival and differentiation of selected neuronal populations of the peripheral and central nervous systems. It participates in axonal growth, pathfinding and in the modulation of dendritic growth and morphology. It functions as the major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (LTP), long-term depression (LTD), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.

Myelin P2 protein, also known as PMP2, is a cytosolic protein found primarily in peripheral nerves. It Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family. PMP2 is a small, basic, and cytoplasmic lipid binding protein of peripheral myelin. It is similar in amino acid sequence and tertiary structure to fatty acid binding proteins found in the liver, adipocytes, and intestine, its expression is limited to the nervous system. PMP2 is detected only in myelin-producing cells of the central and peripheral nervous systems, the oligodendrocytes and Schwann cells, respectively. PMP2 may play a role in lipid transport protein in Schwann cells. It forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.

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. Carbonic anhydrases (CAs) form a family of enzymes that catalyze the rapid conversion of carbon dioxide and water to bicarbonate and protons, a reaction that occurs rather slowly in the absence of a catalyst. The active site of most carbonic anhydrases contains a zinc ion, they are therefore classified as metalloenzymes. Several forms of carbonic anhydrase occur in nature. The primary function of the enzyme in animals is to interconvert carbon dioxide and bicarbonate to maintain acid-base balance in blood and other tissues, and to help transport carbon dioxide out of tissues. Plants contain a different form called β-carbonic anhydrase, which, from an evolutionary standpoint, is a distinct enzyme, but participates in the same reaction and also uses a zinc ion in its active site. Carbonic anhydrase 3, also known as Carbonate dehydratase III, CA-III and CA3, is a cytoplasm protein which belongs to thealpha-carbonic anhydrase family. CA3 is activated by proton donors such as imidazole and the dipeptide histidylhistidine. It is inhibited by coumarins and sulfonamide derivatives such as acetazolamide. At 6 weeks gestation, transcripts accumulate at low levels in the somites and at high levels throughout the notochord. As gestation continues, CA3 becomes abundant in all developing muscle masses and continues at high to moderate levels in the notochord.

Fatty acid-binding protein, liver, also known as Fatty acid-binding protein 1, Liver-type fatty acid-binding protein, FABP1 and FABPL,is a cytoplasm protein which belongs to thecalycin superfamily and Fatty-acid binding protein (FABP) family. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABP1 and FABP6 (the ileal fatty acid binding protein) are also able to bind bile acids. It is thought that FABPs roles include fatty acid uptake, transport, and metabolism. FABP1 FABPL binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. It forms a beta-barrel structure that accommodates hydrophobic ligands in its interior. FABP1 FABPL may be involved in intracellular lipid transport.

Superoxide dismutases (SOD) are important anti-oxidant enzymes that guard against superoxide toxicity. In humans, as in all mammals and most chordates, three forms of superoxide dismutase (SOD) are present: SOD1 is located in the cytoplasm, SOD2 in the mitochondria, and SOD3 is extracellular. Mitochondrial superoxide dismutase [SOD; manganese SOD (MnSOD) or SOD2] neutralizes highly reactive superoxide radical (O•-2), the first member in the plethora of mitochondrial reactive oxygen species.

Aldehyde dehydrogenase 3A1 (ALDH3A1) is a metabolic enzyme that catalyzes the oxidation of various aldehydes. Certain types of epithelial tissues in mammals, especially those continually exposed to environmental stress (e.g., corneal epithelium), express ALDH3A1 at high levels and its abundance in such tissues is perceived to help to maintain cellular homeostasis under conditions of oxidative stress. Metabolic as well as non-metabolic roles for ALDH3A1 have been associated with its mediated resistance to cellular oxidative stress. Aldehyde dehydrogenase 1A1 (ALDH1A1) and ALDH3A1 are corneal crystallins. They protect inner ocular tissues from ultraviolet radiation (UVR)-induced oxidative damage through catalytic and non-catalytic mechanisms. Additionally, ALDH3A1 has been postulated to play a regulatory role in the corneal epithelium based on several studies that report an inverse association between ALDH3A1 expression and corneal cell proliferation. Aldehyde dehydrogenase 3A1 (ALDH3A1) plays an important role in many cellular oxidative processes, including cancer chemoresistance, by metabolizing activated forms of oxazaphosphorine drugs such as cyclophosphamide (CP) and its analogues, such as mafosfamide (MF), ifosfamide (IFM), and 4-hydroperoxycyclophosphamide (4-HPCP). Compounds that can selectively target ALDH3A1 could permit delineation of its roles in these processes and could restore chemosensitivity in cancer cells that express this isoenzyme. ALDH3A1 may act to protect corneal cells against cellular oxidative damage by metabolizing toxic lipid peroxidation products (e.g., 4-HNE), maintaining cellular GSH levels and redox balance, and operating as an antioxidant.

Acyl-Protein Thioesterase 1 (APT-1) is lysophospholipase that belongs to the AB hydrolase 2 family. Lysophospholipases are enzymes that act on biological membranes to regulate the multifunctional lysophospholipids. APT-1 performs on biological membranes to regulate the multifunctional lysophospholipids. It hydrolyzes lysophosphatidylcholine in both monomeric and micellar forms. It hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS; in addition, it also has depalmitoylating activity and low lysophospholipase activity.

Cathepsin L is an enzyme. Cathepsin L, a lysosomal endopeptidase expressed in most eukaryotic cells, is a member of the papain-like family of cysteine proteinases. Cathepsin L plays a major role in antigen processing, tumor invasion and metastasis, bone resorption, and turnover of intracellular and secreted proteins involved in growth regulation. Unlike the precursor forms of other papain family members, the 43 kDa pro-cathepsin L itself is secreted from various cells. Pro-cathepsin L is the major excreted protein of malignantly transformed mouse fibroblasts and is also one of the major acidic cysteine proteases in mammalian cells.

The ADAMs (a disintegrin and metalloprotease) comprise a family of multidomain proteins with metalloprotease, cell adhesion, and signaling activities. Human ADAM12, which is implicated in diseases such as cancer, is expressed in two splice forms, the transmembrane ADAM12-L and the shorter and soluble ADAM12-S. ADAM12, also known as and Meltrin alpha, is a member of the ADAM protein family, which contains one disintegrin domain, one EGF-like domain and one peptidase M12B domain. ADAM12 is synthesized as a zymogen with the prodomain keeping the metalloprotease inactive through a cysteine-switch mechanism. Maturation and activation of the protease involves the cleavage of the prodomain in the trans-Golgi or possibly at the cell surface by a furin-peptidase. It is a membrane-anchored metalloprotease, which has been implicated in activation-inactivation of growth factors that play an important role in wound healing, including heparin-binding epidermal growth factor (EGF)-like growth factor (HB-EGF) and IGF binding proteins. ADAM12 may also regulate cell-cell and cell-extracellular matrix contacts through interactions with cell surface receptors - integrins and syndecans - potentially influencing the actin cytoskeleton. Moreover, ADAM12 interacts with several cytoplasmic signaling and adaptor molecules through its intracellular domain, thereby directly transmitting signals to or from the cell interior. These ADAM12-mediated cellular effects appear to be critical events in both biological and pathological processes. In addition to protease activity, ADAM12 possesses cell binding and cell signaling properties. In many studies, ADAM12 overexpression has been correlated with disease, and ADAM12 has been shown to promote tumor growth and progression in cancer. On the other hand, protective effects of ADAM12 in disease have also been reported.

Malate dehydrogenases 1(MDH1 MDHA) is a soluble form of malate dehydrogenases. Malate dehydrogenases (MDH) is a group of multimeric enzymes consisting of identical subunits usually organized as either dimer or tetramers with subunit molecular weights of 30-35 kDa. MDH has been isolated from different sources including archaea, eubacteria, fungi, plants, and mammals. MDH catalyzes the NAD NADH-dependent interconversion of the substrates malate and oxaloacetate. This reaction plays a key part in the malate aspartate shuttle across the mitochondrial membrane, and in the tricarboxylic acid cycle within the mitochondrial matrix. The enzymes share a common catalytic mechanism and their kinetic properties are similar, which demonstrates a high degree of structural similarity. The three-dimensional structures and elements essential for catalysis are conserved between mitochondrial and cytoplasmic forms of MDH in eukaryotic cells even though these isoenzymes are only marginally related at the level of the primary structure.

TREM-2 (Triggering Receptor Expressed on Myeloid cells-2) is a 35 kDa type I transmembrane member of the TREM family and Ig superfamily. Mature human TREM-2  consists of a 156 amino acid (aa) extracellular domain (ECD) with one V-type Ig-like domain, a 21 aa transmembrane (TM) domain, and a 35 aa cytoplasmic tail. TREM-2 forms a receptor signaling complex with TYROBP which mediates signaling and cell activation following ligand binding (PubMed:10799849). Acts as a receptor for amyloid-beta protein 42, a cleavage product of the amyloid-beta precursor protein APP, and mediates its uptake and degradation by microglia.

Thymopentin is a member of the LEM family. Thymopentin is expressed in many tissues, highly in the adult thymus and fetal liver. The N-terminal contains two structurally independent domains, LEM domain and LEM-like domain. The C-terminal domain forms a four-stranded coiled coil. Thymopentin may be involved in the structural organization of the nucleus and in the post-mitotic nuclear assembly. It is associated with T-cell development and function. Meantime, Thymopentin plays an important role, together with LMNA, in the nuclear anchorage of RB1. Thymopoietin is participated in the induction of CD90 in the thymus.

6-phosphofructo-2-kinase fructose-2,6-bisphosphatase 1 is an enzyme that in humans is encoded by the PFKFB1 gene. The enzyme forms a homodimer that catalyzes both the synthesis and degradation of fructose-2,6-biphosphate using independent catalytic domains. It belongs to the phosphoglycerate mutase family. Fructose-2,6-biphosphate is an activator of the glycolysis pathway and an inhibitor of the gluconeogenesis pathway. Consequently, regulating fructose-2,6-biphosphate levels through the activity of this enzyme is thought to regulate glucose homeostasis.

Collagen alpha-1(VIII) chain, also known as endothelial collagen, C3orf7 and COL8A1, can be cleaved into vastatin chain. COL8A1 is a short chain collagen and a major component of the basement membrane of the corneal endothelium. COL8A1 forms homotrimers, or heterotrimers in association with alpha 2(VIII) type collagens. Four homotrimers can form a tetrhedron stabilized by central interacting C-terminal NC1 trimers. COL8A1 contains one C1q domain and is primarily expressed in the subendothelium of large blood vessels. The expression level can be up-regulated during vascular injury, in atherosclerosis and in diabetes. COL8A1 may have a role in the maintenance of vessel wall integrity and structure, in particular in atherogenesis.

Pre-B cell colony enhancing factor (PBEF) was originally identified as a cytokine that potentiated the clonal expansion and differentiation of pre-B cells, but it is also acknowledged to be the ubiquitous intracellular enzyme nicotinamide phosphoribosyltranferase (NAMPT) and the adipokine visfatin . PBEF is constitutively expressed in the fetal membranes where its greatest expression is in the amnion. It has intracellular and extracellular forms. Most of the intracellular functions of PBEF are due to its role as a Nampt which can induce angiogenesis through upregulation of VEGF and VEGFR and secretion of MCP-1. Extracellular PBEF has been shown to increase inflammatory cytokines, such as TNF-α, IL-1β, IL-16, and TGF-β1. PBEF also increases the production of IL-6, TNF-α, and IL-1β in CD14+ monocyctes, macrophages, and dendritic cells, enhances the effectiveness of T cells.

FKBP4 act as a regulator of microtubule dynamics by inhibiting MAPT TAU ability to promote microtubule assembly. FKBP4 may play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments, it also may have a protective role against oxidative stress in mitochondria. The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening.

Expression system: HEK293 Cells
Length: 19-605, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 1-444, Full Length
Activity: Not Tested

Expression system: HEK293 Cells
Length: 19-244, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 21-442, Partial
Activity: Not Tested