Recombinant Human Endostatin/COL18A1 protein (His tag)
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Recombinant Human Endostatin/COL18A1 protein (His tag) is a Human Fragment protein, in the 1578 to 1754 aa range, expressed in Yeast, with >90%, suitable for SDS-PAGE, Mass Spec.
View Alternative Names
Collagen alpha-1(XVIII) chain, COL18A1
- Mass Spec
Supplier Data
Mass Spectrometry - Recombinant Human Endostatin/COL18A1 protein (His tag) (AB240772)
Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS analysis result of ab240772 could indicate that this peptide derived from Yeast-expressed Homo sapiens (Human) COL18A1.
- Mass Spec
Supplier Data
Mass Spectrometry - Recombinant Human Endostatin/COL18A1 protein (His tag) (AB240772)
Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS analysis result of ab240772 could indicate that this peptide derived from Yeast-expressed Homo sapiens (Human) COL18A1.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human Endostatin/COL18A1 protein (His tag) (AB240772)
(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) analysis with 5% enrichment gel and 15% separation gel of ab240772.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Endostatin modulates cellular processes like migration proliferation and apoptosis. It is involved in the inhibition of endothelial cell proliferation which is an essential function in controlling angiogenesis. Endostatin does not typically form complexes but it has associations with heparan sulfate proteoglycans which facilitates its interaction with cells. Through these interactions endostatin plays a significant role in maintaining vascular homeostasis and tissue remodeling.
Pathways
Endostatin actively participates in the angiogenesis pathway and the regulation of the extracellular matrix pathway. Endostatin's inhibitory effects on angiogenesis involve interactions with pathways associated with key proteins like VEGF and FGF-2 blocking their pro-angiogenic signaling. Endostatin also influences other proteins like integrins which are important for cell adhesion and migration within angiogenesis and matrix remodeling processes.
Specifications
Form
Liquid
General info
Function
Probably plays a major role in determining the retinal structure as well as in the closure of the neural tube.. Non-collagenous domain 1. May regulate extracellular matrix-dependent motility and morphogenesis of endothelial and non-endothelial cells; the function requires homotrimerization and implicates MAPK signaling.. Endostatin. Potently inhibits endothelial cell proliferation and angiogenesis (PubMed : 9459295). May inhibit angiogenesis by binding to the heparan sulfate proteoglycans involved in growth factor signaling (By similarity). Inhibits VEGFA-induced endothelial cell proliferation and migration. Seems to inhibit VEGFA-mediated signaling by blocking the interaction of VEGFA to its receptor KDR/VEGFR2. Modulates endothelial cell migration in an integrin-dependent manner implicating integrin ITGA5 : ITGB1 and to a lesser extent ITGAV : ITGB3 and ITGAV : ITGB5 (By similarity). May negatively regulate the activity of homotrimeric non-collagenous domain 1 (PubMed : 11257123).
Sequence similarities
Belongs to the multiplexin collagen family.
Post-translational modifications
Prolines at the third position of the tripeptide repeating unit (G-X-Y) of the triple-helical regions are hydroxylated.. Circulating endostatins are found as sialoglycoprotein and asialoglycoprotein structures.. Undergoes proteolytic processing by CTSL/cathepsin-L and elastase-like proteases to generate both non-collagenous domain 1 trimers and endostatin monomers (PubMed:10626789). In tissue extracts (brain, skeletal muscle, heart, kidney, testis and liver) predominantly bands of approximately 38 kDa are detected; recombinant non-collagenous domain 1 shows similar mobility. In vitro, several proteolytic cleavage sites in the non-collagenous domain 1 hinge region generating different endostatin-like peptides are reported (By similarity).
Target data
Product promise
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