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Recombinant Human COL18A1 protein (His Tag)

Species

Human

Purity

>90 %, SDS-PAGE

Tag

C-His

Activity

not tested

Cat no : Eg0254

Validation Data Gallery

  • Purity of Recombinant Human COL18A1 was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

    Purity of Recombinant Human COL18A1 was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

Product Information

Purity >90 %, SDS-PAGE
Endotoxin <0.1 EU/μg protein, LAL method
Activity 
Not tested
Expression HEK293-derived Human COL18A1 protein His1572-Lys1754 (Accession# P39060-3) with a His tag at the C-terminus.
GeneID 80781
Accession P39060-3
PredictedSize 23.9 kDa
SDS-PAGE 25-28 kDa, reducing (R) condition
Formulation Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
Reconstitution Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
Storage Conditions
It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

Background

Endostatin, a 20-kDa C-terminal fragment derived from collagen alpha-1(XVIII) chain (COL18A1), is an endogenously produced inhibitor of angiogenesis. Many different proteases are able to cleave the NC1 domain of collagen alpha-1(XVIII) chain to produce endostatin including cathepsins L, B, and K, elastase. Endostatin inhibits proliferation and migration of endothelial cells, angiogenesis, and tumor growth. It may interfere with the pro-angiogenic action of growth factors such as basic fibroblast growth factor (bFGF/FGF-2) and vascular endothelial growth factor (VEGF).

References:

1. M S O'Reilly, et al. (1997) Cell. 88(2):277-85
2. M Ferreras, et al. (2000) FEBS Lett. 486(3):247-51. 
3. Judah Folkman. (2006) Exp Cell Res. 312(5):594-607.
4. Amit Walia, et al. (2015) Biochim Biophys Acta. 1850(12):2422-38.