7,8-diaminononanoate synthase (dans)

Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only animotransferase known to utilize SAM as an amino donor. Complements a bioU deletion in Synechocystis PCC 6803.

KIR2DL2 (2DL2, formerly NKAT6, designated CD158b) is a 348 amino acid (aa) type I transmembrane glycoprotein that belongs to the human killer cell Ig‑like receptor (KIR) family. KIRs are expressed on human CD56dim NK cells and T cell subsets, and regulate effector functions in the innate immune system.KIR2DL2 is receptor on natural killer (NK) cells for HLA-Cw1, 3, 7, and 8 allotypes. Inhibits the activity of NK cells thus preventing cell lysis. KIR2DL2 Protein, Human, Recombinant (His & Avi) is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 27.4 kDa and the accession number is P43627.

KIR2DL2 (2DL2, formerly NKAT6, designated CD158b) is a 348 amino acid (aa) type I transmembrane glycoprotein that belongs to the human killer cell Ig‑like receptor (KIR) family. KIRs are expressed on human CD56dim NK cells and T cell subsets, and regulate effector functions in the innate immune system.KIR2DL2 is receptor on natural killer (NK) cells for HLA-Cw1, 3, 7, and 8 allotypes. Inhibits the activity of NK cells thus preventing cell lysis. KIR2DL2 Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 27.4 kDa and the accession number is P43627.

X-ray repair cross-complementing protein 5, also known as 86 kDa subunit of Ku antigen, ATP-dependent DNA helicase 2 subunit 2, ATP-dependent DNA helicase II 8 kDa subunit, CTC box-binding factor 85 kDa subunit, DNA repair protein XRCC5, Lupus Ku autoantigen protein p86, TLAA and XRCC5, is a nucleus and chromosome which belongs to the ku8 family. XRCC5 is a single-stranded DNA-dependent ATP-dependent helicase. XRCC5 has a role in chromosome translocation. X-ray repair cross-complementing protein 6, also known as 5'-deoxyribose-5-phosphate lyase Ku7, ATP-dependent DNA helicase 2 subunit 1, ATP-dependent DNA helicase II 7 kDa subunit, 7 kDa subunit of Ku antigen, ATP-dependent DNA helicase 2 subunit 1, CTC box-binding factor 75 kDa subunit, Lupus Ku autoantigen protein p7, Thyroid-lupus autoantigen and XRCC6, is a nucleus and chromosome which belongs to the ku7 family. Heterodimer of a XRCC6 and a XRCC5 subunit associates in a DNA-dependent manner with PRKDC to form the DNA-dependent protein kinase complex DNA-PK, and with the LIG4-XRCC4 complex. The dimer also associates with NAA15, and this complex binds to the osteocalcin promoter and activates osteocalcin expression.

PDCD2 Protein, Human, Recombinant (His) is expressed in E. coli.

Caspase 7, also known as caspase-7 and MCH3, belongs to the cysteine-aspartic acid protease (caspase) family. Caspases play a role in the signal transduction pathways of apoptosis, necrosis and inflammation. There are two major classes of caspases: initiators and effectors. The initiator isoforms (caspases-1,-4,-5,-8,-9,-10,-11,-12) are activated by, and interact with, upstream adaptor molecules through protein-protein interaction domains known as CARD and DED. Effector caspases (-3,-6,-7) are responsible for cleaving downstream substrates and are sometimes referred to as the executioner caspases. Caspase 7 exists in lung, skeletal muscle, liver, kidney, spleen, heart, and moderately in testis. Caspase 7 cannot be detected in the brain. Caspase 7 functions in the activation cascade of caspases responsible for apoptosis execution. It cleaves and activates sterol regulatory element binding proteins (SREBPs). It proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp- -Gly-217' bond. Overexpression promotes programmed cell death.

TEM-type are the most prevalent beta-lactamases in enterobacteria; they hydrolyze the beta-lactam bond in susceptible beta-lactam antibiotics, thus conferring resistance to penicillins and cephalosporins. TEM-3 and TEM-4 are capable of hydrolyzing cefotaxime and ceftazidime. TEM-5 is capable of hydrolyzing ceftazidime. TEM-6 is capable of hydrolyzing ceftazidime and aztreonam. TEM-8 CAZ-2, TEM-16 CAZ-7 and TEM-24 CAZ-6 are markedly active against ceftazidime. IRT-4 shows resistance to beta-lactamase inhibitors.

Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to utilize SAM as an amino donor. BIO3 Protein, S. cerevisiae, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 58.7 kDa and the accession number is P50277.

Growth Differentiation Factor 5(GDF-5, BMP-14) is a member of the BMP family of TGFβ superfamily proteins. Human GDF-5, -6, and -7 are a defined subgroup of the BMP family. GDF-5 is synthesized as a homodimeric precursor protein consisting of a 354 amino acid (aa) Nterminal proregion and a 120 aa C-terminal mature peptide. Mature human GDF-5 shares 99% aa sequence identity with both mature mouse and rat GDF-5. GDF-5 signaling is mediated by formation of a heterodimeric complex consisting of a type 1 (BMPR-IB) and a type II (BMPR-IIor Activin RII) serine threonine kinase receptor which results in the phosphorylation and activation of cytosolic Smad proteins (Smad1, 5, and 8). GDF-5 is involved in multiple developmental processes including limb generation, cartilage development, joint formation, bone morphogenesis, cell survival, and neuritogenesis. Inhibition of GDF-5 expression or alteration of its signaling can facilitate the development of osteoarthritis.

Caspase-10 (CASP10) is a 521 amino acid protein member of the Cysteine-Aspartic Acid Protease (Caspase) family. CASP10 contains two DED (Death Effector) domains and is detectable in most tissues. CASP10 cleavage by Granzyme B and autocatalytic activity generate the two active subunits: Caspase-10 subunit p23 17, Caspase-10 subunit p12. Caspases are a family of cytosolic aspartate-specific cysteine proteases involved in the execution-phase of cell apoptosis, the initiation and execution. Human caspases can be subdivided into three functional groups: cytokine activation (caspase-1, -4, -5, and -13), apoptosis initiation (caspase-2, -8, -9, -and -10), and apoptosis execution (caspase-3, -6, and -7). CASP10 cleaves and activates caspases 3 and 7, but itself is processed by caspase 8. Defects in CASP10 are associated with apoptosis defects seen in type II autoimmune lymphoproliferative syndrome.

Complement component C8 is a constituent of the membrane attack complex, C8 alpha, C8 beta and C8G. C8G is a secreted protein and comsists a disulfide-linked C8 alpha-gamma heterodimer and a non-covalently associated C8 beta chain. C8 alpha and C8 beta play an important role in complement-mediated bacterial killing together.C8 is involved in the formation of Membrane Attack Complex on bacterial cell membranes. C8 binds to the C5B-7 complex, forming the C5B-8 complex. C5-B8 binds C9 and acts as a catalyst in the polymerization of C9. The gamma subunit seems to be able to bind retinol. Patients lacking C8 are susceptible to certain bacterial infections.

STX8, also known as syntaxin 8, directly interacts with HECTd3. STX8 forms the SNARE complex with syntaxin 7, vti1b and endobrevin. STX8 belongs to the syntaxin family. Members of this family are key molecules implicated in diverse vesicle docking and membrane fusion events. STX8 physically interacts with cystic fibrosis transmembrane conductance regulator (CFTR): recombinant syntaxin 8 binds CFTR in vitro and both proteins co-immunoprecipitate in HT29 cells. Syntaxin 8 regulates CFTR-mediated currents in chinese hamster ovary (CHO) cells stably expressing CFTR and syntaxin 8. STX8 contributes to the regulation of CFTR trafficking and chloride channel activity by the SNARE machinery.

CYP2C9 Protein, Human, Recombinant (His & Myc) is expressed in E. coli.

C8 is a constituent of the membrane attack complex. C8 binds to the C5B-7 complex, forming the C5B-8 complex. C5-B8 binds C9 and acts as a catalyst in the polymerization of C9. The gamma subunit seems to be able to bind retinol. Complement C8g Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 26.4 kDa and the accession number is P07360.

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.

E3 Ubiquitin-Protein Ligase CHIP is a cytoplasmic protein. CHIP is highly expressed in skeletal muscle, heart, pancreas, brain and placenta. CHIP interacts with the molecular chaperones Hsc70-Hsp70 and Hsp90 through its TPR domain; lead to in client substrate ubiquitylation and degradation by the proteasome. CHIP targets misfolded chaperone substrates towards proteasomal degradation. CHIP mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. CHIP plays a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1 ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. It also may regulate the receptor stability and activity through proteasomal degradation.

Relaxin-1, also known as Prorelaxin H1 and RLN1, is a secreted protein that belongs to the insulin family. It is a peptide hormone that was first described in 1926 by Frederick Hisaw. Since its discovery as a reproductive hormone 8 years ago, relaxin has been implicated in a number of pregnancy-related functions involving extracellular matrix (ECM) turnover and collagen degradation. It is now becoming evident that relaxin's ability to reduce matrix synthesis and increase ECM degradation has important implications in several nonreproductive organs, including the heart, lung, kidney, liver and skin. The relaxin-like peptide family belongs in the insulin superfamily and consists of 7 peptides of high structural but low sequence similarity; relaxin-1 (RNL1), relaxin-2 (RNL2) and relaxin-3 ( RNL3), and the insulin-like (INSL) peptides, INSL3, INSL4, INSL5 and INSL6. The functions of relaxin-3, INSL4, INSL5, INSL6 remain uncharacterised. Relaxin-1 RLN1 is an ovarian hormone that acts with estrogen to produce dilatation of the birth canal in many mammals. Relaxin-1 RLN1 may be involved in remodeling of connective tissues during pregnancy, promoting growth of pubic ligaments and ripening of the cervix. Relaxin and estrogen appear to play protective roles against airway fibrosis, airway SM thickening, and cardiac hypertrophy. Relaxin may also provide a means to regulate excessive collagen deposition during kidney development and in diseased states characterized by renal fibrosis.

Catalyzes two activities which are involved in the biotine biosynthesis: the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism, and the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). BioAB Protein, Bacteroides fragilis, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 90.6 kDa and the accession number is Q5LEY1.

TEM-type are the most prevalent beta-lactamases in enterobacteria; they hydrolyze the beta-lactam bond in susceptible beta-lactam antibiotics, thus conferring resistance to penicillins and cephalosporins. TEM-3 and TEM-4 are capable of hydrolyzing cefotaxime and ceftazidime. TEM-5 is capable of hydrolyzing ceftazidime. TEM-6 is capable of hydrolyzing ceftazidime and aztreonam. TEM-8 CAZ-2, TEM-16 CAZ-7 and TEM-24 CAZ-6 are markedly active against ceftazidime. IRT-4 shows resistance to beta-lactamase inhibitors.

PSMB8 Protein, Human, Recombinant (His & Myc & SUMO) is expressed in E. coli.

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.

Human Chemokine (C-X-C motif) Ligand 7 (CXCL7), also known as neutrophil activating peptide 2 (NAP-2), is a member of the CXC chemokines containing an ELR domain (Glu-Leu-Arg tripeptide motif). Similar to other ELR domain containing CXC chemokines, such as IL-8 and the GRO proteins, CXCL7 binds CXCR2, chemoattracts and activates neutrophils. CXCL7, Connective Tissue Activating Protein III (CTAPIII) and βthrombogulin (βTG), are proteolytically processed carboxylterminal fragments of platelet basic protein (PBP) which is found in the alphagranules of human platelets. Although CTAPIII, βTG, and PBP represent amino-terminal extended variants of NAP2 and possess the same CXC chemokine domains, these proteins do not exhibit CXCL7 NAP2 activity. CXCL7 induces cell migration through the G-protein-linked receptor CXCR-2.