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Human Collagen Type II

Catalog No.
C15-1348-148
Manufacturer No.
CC052
Manufacturer Name
Sigma-Aldrich
Quantity
100
Unit of Measure
UG
Price: $663.58
List Price: $737.31

COL2A1 is the gene responsible for the production of the alpha1(II) chain of type II collagen. Type II collagen, which adds structure and strength to connective tissues, is found primarily in cartilage, the gel that fills the eyeball (vitreous

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General description

COL2A1 is the gene responsible for the production of the alpha1(II) chain of type II collagen. Type II collagen, which adds structure and strength to connective tissues, is found primarily in cartilage, the gel that fills the eyeball (vitreous body), inner ear, and the center portion of the discs between the vertebrae in the spine (nucleus pulposus).

There are two forms of type II collagen made in the body. One version, type IIA, is made mainly in the vitreous body of the eye. The second version, type IIB, is preferentially produced in adult cartilage tissue.

Collagen II is initially produced as type II procollagen, a protein consisting of three pro-alpha1(II) chains twisted together to form a triple-stranded helical (spiral-shaped) molecule. While in the cell, enzymes modify certain amino acids (the building blocks of proteins), specifically lysine and proline, by adding chemical groups that are necessary for the strands to come together in a stable structure and then cross-link with other molecules. Other enzymes add sugars to the protein. The triple-stranded type II procollagen molecule leaves the cell and is converted to collagen by enzymes that clip small segments off both ends. The collagen molecules arrange themselves into long, thin fibrils outside of the cell. The fibrils come together in side-by-side groups to form collagen fibers. Cross-linking between molecules in fibrils produces a very stable protein structure, which contributes to collagen′s tissue-strengthening function.{http://ghr.nlm.nih.gov}

Collagen type II was purified by using differential salt precipitation, alcohol precipitation and DEAE chromatography. Multiple purification steps provide final preparations of collagen types in the native triple helical form, free of any non-collagenous protein. Contamination of other collagen types in a standard preparation is lower then five percent totally.

Physical form

Purified protein. Liquid in 0.5M acetic acid. No preservative.

Storage and Stability

Aliquot and freeze. Maintain at -20°C up to 12 months. Avoid repeated freeze/thaw cycles.

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

UPC:
41123201
Condition:
New
Weight:
1.00 Ounces
HazmatClass:
No
WeightUOM:
LB
MPN:
CC052


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