Immunization Grade Porcine Type XI Collagen, 5 mg, lyophilized

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SKU:
445-1083
Size:
5 mg
Shipping:
Gel Packs
Storage:
4C, in the dark
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Description

Immunization Grade Porcine Type XI Collagen, 5 mg, lyophilized - Cat Number: 1083 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: Type XI collagen is purified from pepsin-solubilized cartilage by repeat salt precipitation.
Type XI collagen is one of three types of collagen which make up cartilage fibrils and consists
of three α-chains, α1 (XI), α2 (XI), and α3 (XI), where α3 (XI) is homologous to the α1 (II) chain
of type II collagen (1).
NOTE: Type XI collagen shares significant similarities with type V collagen, which consists of
α1 (V), α2 (V), and α3 (V) chains, but these alpha chains are not identical (2).
APPLICATION: Use as an immunizing antigen to generate antibodies, an antigen to detect anti-type XI collagen
antibodies in ELISA, or as a standard for gel analysis.
NOTE: Antibodies against type II collagen partially cross-react to type XI collagen due to the
homology between α3 (XI) and α1 (II).
QUANTITY: 5 mg
FORM: Lyophilized powder
SOURCE: Porcine articular cartilage
MOLECULAR WEIGHT: Intact type XI collagen: approximately 360 kDa. By 6% gel analysis, type XI collagen is
separated into three α-chains: α1 (XI), α2(XI), and α3 (XI) (1052, 1478, and 1060 A.A. 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
NOTES: Type XI collagen can be dissolved at 4 mg/ml in an acidic solution 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:
1. K. von der Mark, M. van Menxel, H. Wiedemann, Isolation and characterization of new
collagens from Porcine cartilage. Eur. J. Biochem. 124: 57-62 (1982)
2. R. Burgeson, P. Hebda, N. Morris, D. Hollister, Human cartilage collagens. Comparison of
cartilage collagens with human type V collagen. J Biol Chem 257, 7852-6 (1982).

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