Assay
≥95% (SDS-PAGE)
Quality Level
form
solid
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
impurities
≤100 pg/μg Endotoxins (pg/μg Angiogenin)
shipped in
dry ice
storage temp.
−70°C
General description
Recombinant, human angiogenin expressed in E. coli. Exhibits angiogenic and ribonucleolytic activities. Enhances the ability of endothelial cells to digest extracellular matrix components and degrade basement membrane. Has been shown to stimulate capillary and umbilical vein endothelial cells to produce DAG and secrete prostacyclin by phospholipase activation. Biological activity: 1.0 µg protein produces an absorbance change at 260 nm of approximately 2.0 - 3.0 as measured by yeast tRNA ribonucleolytic activity.
Biochem/physiol Actions
≥1.0 µg protein produces an absorbance change at 260 nm of ~2.0-3.0 as measured based upon its ribonucleolytic activity toward Yeast tRNA.
Physical form
Lyophilized from sterile-filtered PBS containing 50 µg BSA/µg Angiogenin.
Preparation Note
Following reconstitution, aliquot and freeze (-70°C). Stock solutions are stable for up to months at -70°C. Avoid freeze/thaw cycles of solutions.
Reconstitute to a concentration ≥1 µg/ml with sterile PBS containing ≥0.1% HSA or BSA.
Other Notes
Leland, P.A., et al. 2002. Biochemistry41, 1343.
Hatzi, E., et al. 2000. Biochem. Biophys. Res. Commun. 267, 719.
Hu, G., et al. 1994. Proc. Natl. Acad. Sci. USA91, 12096.
Lee, F.S., and Vallee, B.L. 1989. Biochem. Biophys. Res. Commun.161, 121.
Kurachi, R., et al. 1985. Biochemistry24, 5494.
Hatzi, E., et al. 2000. Biochem. Biophys. Res. Commun. 267, 719.
Hu, G., et al. 1994. Proc. Natl. Acad. Sci. USA91, 12096.
Lee, F.S., and Vallee, B.L. 1989. Biochem. Biophys. Res. Commun.161, 121.
Kurachi, R., et al. 1985. Biochemistry24, 5494.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Toxicity: Standard Handling (A)
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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