SequenceTwo 14 amino acid synthetic peptides whose sequences are derived from amino acids 119-142 of mouse and human endostatin protein. The sequences of these peptides are (amino to carboxy terminus): R(129)RLM/TESYCETWRTE(142).
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
This peptide may be used for neutralization and control experiments with the polyclonal antibody that reacts with this product and mouse/human endostatin, catalog ab3453. Using a solution of peptide of equal volume and concentration to the corresponding antibody will yield a large molar excess of peptide (~ 70-fold) for competitive inhibition of antibody-protein binding reactions.
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Preparation and Storage
Stability and Storage
Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
Alpha 1 collagen type 18 (XVIII)(COL18A1)
Alpha 1 type XVIII collagen
Collagen alpha 1(XV) chain
Collagen alpha 1(XVIII) chain
Collagen alpha-1(XV) chain
Collagen type XV proteoglycan
Collagen type XVIII alpha 1
Collagen XV, alpha 1 polypeptide
Collagen, type XV, alpha 1
Multi functional protein MFP
FunctionCOLA18A probably plays a major role in determining the retinal structure as well as in the closure of the neural tube. Endostatin potently inhibits endothelial cell proliferation and angiogenesis. May inhibit angiogenesis by binding to the heparan sulfate proteoglycans involved in growth factor signaling.
Tissue specificityPresent in multiple organs with highest levels in liver, lung and kidney.
Involvement in diseaseDefects in COL18A1 are a cause of Knobloch syndrome (KNO) [MIM:267750]. KNO is an autosomal recessive disorder defined by the occurrence of high myopia, vitreoretinal degeneration with retinal detachment, macular abnormalities and occipital encephalocele.
Sequence similaritiesBelongs to the multiplexin collagen family. Contains 1 FZ (frizzled) domain. Contains 1 TSP N-terminal (TSPN) domain.
Post-translational modificationsProlines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Cellular localizationSecreted > extracellular space > extracellular matrix.