Description
Immunization Grade Bovine Amnion Type V Collagen, 1 mg, lyophilized - Cat Number: 1092 From Chondrex.
Research Field: Immunology
Clonality: N/A
Cross-Reactivity:
Host Origin: N/A
Applications: N/A
Isotype: N/A
Detection Range: N/A
Sample Type: N/A
Concentration: N/A
Immunogen:
DESCRIPTION: Bovine type V collagen purified from pepsin-solubilized amnion by repeat salt precipitation.
Amnion type V collagen consists of two α1 chains and one α2 chain, [α1(V)]2 and α2(V).
APPLICATION: Use as an immunizing antigen to generate antibodies, an antigen to detect anti-type V collagen
antibodies in ELISA, or as a standard for gel analysis.
QUANTITY: 1 mg
FORM: Lyophilized powder
SOURCE: Bovine
MOLECULAR WEIGHT: Intact amnion type V collagen: approximately 540 kDa. By 6% gel analysis, amnion type V
collagen separates into two chains: α1(V) and α2(V) (1840 and 1258 amino acid residues) from
the top of the gel.
PURITY: >90% by SDS-PAGE gel analysis
STORAGE: 4°C in the dark for lyophilized form and -20°C for solution form. Collagen may gradually degrade
under neutral conditions
STABILITY: 2 years for lyophilized form
NOTES: Type V collagen can be dissolved at 4 mg/ml in acidic solutions such as 0.01-0.05M acetic acid,
pH 3.0-3.3 or 0.15M citrate buffer, pH 3.6 by stirring at 4°C overnight. To neutralize the solution,
add 10x neutral buffer containing 1.5M NaCl or dialyze the solution against a neutral buffer.
REFERENCES: C. Niyibizi, P. Fietzek, M. van der Rest, Human placenta type V collagens. Evidence for the
existence of an alpha 1(V) alpha 2(V) alpha 3(V) collagen molecule. J Biol Chem 259, 14170-4
(1984).
M. Abedin, S. Ayad, J. Weiss, Type V collagen: the presence of appreciable amounts of alpha
3(V) chain in uterus. Biochem Biophys Res Commun 102, 1237-45 (1981).
Sato, K et al. Simple and Rapid Chromatographic Purification of Type V Collagen from a
Pepsin Digest of Porcine Intestinal Connective Tissue, an Unmanageable Starting Material for
Conventional Column Chromatography. Journal of Chromatography 790:277-283 (2003).