Human COL4A1 protein (Recombinant) (N-His) (STJP003584)
SPECIFICATIONS
HostE.coli
ImmunogenHomo sapiens (Human)
General Information
| Short Description | Recombinant-Human COL4A1-N-His protein was developed from e.coli for the region N-His. For use in research applications. |
| Applications | ELISA/Immunogen/SDS-PAGE/WB |
| Host | E.coli |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Dilution Range | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Formulation | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
| Storage Instruction | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at-20 to-80°C for twelve months from the date of receipt. |
Target Information
| Gene Symbol | COL4A1 |
| Gene ID | 1282 |
| Uniprot ID | CO4A1_HUMAN |
| Immunogen | Homo sapiens (Human) |
| Immunogen Region | His1444-Thr1669 |
Additional Info
| Post Translational Modifications | Lysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated. The modified lysines can be O-glycosylated. Contains 4-hydroxyproline (Probable). Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. Contains 3-hydroxyproline. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline. Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens. The trimeric structure of the NC1 domains is stabilized by covalent bonds (sulfilimine cross-links) between Lys and Met residues. These cross-links are important for the mechanical stability of the basement membrane. Sulfilimine cross-link is catalyzed by PXDN. Proteolytic processing produces the C-terminal NC1 peptide, arresten. |
| Function | Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen. Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation. |
| Protein Name | Collagen Alpha-1(Iv Chain Cleaved Into - Arresten |
| Database Links | Reactome: R-HSA-1442490Reactome: R-HSA-1474244Reactome: R-HSA-1650814Reactome: R-HSA-186797Reactome: R-HSA-2022090Reactome: R-HSA-216083Reactome: R-HSA-2214320Reactome: R-HSA-2243919Reactome: R-HSA-3000157Reactome: R-HSA-3000171Reactome: R-HSA-3000178Reactome: R-HSA-3000480Reactome: R-HSA-419037Reactome: R-HSA-8948216 |
| Cellular Localisation | SecretedExtracellular SpaceExtracellular MatrixBasement Membrane |
| Alternative Protein Names | Collagen Alpha-1(Iv Chain Cleaved Into - Arresten proteinCOL4A1 protein |
Information sourced from Uniprot.org