Key features and details
- Expression system: Pichia pastoris
- Purity: > 95% SDS-PAGE
- Active: Yes
- Suitable for: Functional Studies, SDS-PAGE
Product nameRecombinant human Endostatin/COL18A1 protein
See all Endostatin/COL18A1 proteins and peptides
Purity> 95 % SDS-PAGE.
Greater than 98% as determined by SDS-PAGE and HPLC.
Expression systemPichia pastoris
Protein lengthProtein fragment
Our Abpromise guarantee covers the use of ab52022 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Additional notesFor long-term storage, aliquot and keep desiccated below –20degC. Avoid freeze-thaw cycles.
This product was previously labelled as Endostatin
Concentration information loading...
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.
Endotoxin level is less than 0.1 ng/mg of Endostatin
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- Alpha 1 collagen type 18 (XVIII)(COL18A1)
- Alpha 1 type XVIII collagen
- Antiangiogenic agent
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.
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.
- Information by UniProt
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab52022 has not yet been referenced specifically in any publications.