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CC050

Sigma-Aldrich

Human Collagen Type I

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eCl@ss:
32160405
NACRES:
NA.75

biological source

human

Quality Level

Assay

>90% (collagen type I, SDS-PAGE)

form

liquid

manufacturer/tradename

Chemicon®

concentration

1 mg/mL

technique(s)

cell culture | mammalian: suitable

impurities

<1% collagen type II,IV-VI & non-collagen proteins.
<10% collagen type III

input

sample type pancreatic stem cell(s)
sample type mesenchymal stem cell(s)
sample type epithelial cells
sample type induced pluripotent stem cell(s)
sample type neural stem cell(s)
sample type: human embryonic stem cell(s)
sample type hematopoietic stem cell(s)

solubility

water: soluble at 20 °C

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... COL1A1(1277)

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This Item
C6745AB765PC3867
Sigma-Aldrich

Sigma-Aldrich

CC050

Human Collagen Type I

assay

>90% (collagen type I, SDS-PAGE)

assay

-

assay

-

assay

>95% (SDS-PAGE)

form

liquid

form

solution

form

-

form

liquid

concentration

1 mg/mL

concentration

0.3 mg/mL

concentration

-

concentration

-

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable

technique(s)

ELISA: suitable, immunohistochemistry: suitable, radioimmunoassay: suitable, western blot: suitable

technique(s)

cell culture | mammalian: suitable

impurities

<1% collagen type II,IV-VI & non-collagen proteins., <10% collagen type III

impurities

-

impurities

-

impurities

-

General description

COL1A1 is the gene responsible for the production of the alpha1(I) chain of type I collagen. Collagen, which adds structure and strength to connective tissues, is found throughout the body for example, in skin, tendon, cartilage, ligaments, bone, the part of the eyeball that is white (sclera), and the spaces between cells and tissues called the extracellular matrix.

Type I collagen is initially produced as procollagen in cells. This protein consists of two pro-alpha1(I) protein strands combined with a pro-alpha2(I) procollagen strand that form a triple-stranded rope-like structure. While in the cell, enzymes modify certain amino acids in the protein (lysine and proline) by adding chemical groups that are necessary for the three strands to form stable molecules and make connections (cross-links) between chains. Other enzymes add sugars to the protein. Now complete, the triple-stranded type I procollagen molecule leaves the cell and is processed by enzymes that clip small segments off both ends. The procollagen 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}
Human type I collagen purified by serial salt precipitations, alcohol precipitation and DEAE chromatography of a pepsin extraction of human placenta. Composition: [α1(I)]2, <α2(I), native triple helix.

Physical form

Purified protein. Liquid containing 0.5 M Acetic acid, pH 2.5. Can be diluted in PBS for applications.

Analysis Note

Purity was controlled by SDS-PAGE and reaction with anti-collagen type-specific antibodies

Legal Information

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

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Physicochemical characterization and molecular organization of the collagen A and B chains.
R K Rhodes et al.
Biochemistry, 17(17), 3442-3448 (1978-08-22)
Characterization of a novel collagen chain in human placenta and its relation to AB collagen.
Sage, H and Bornstein, P
Biochemistry, 18, 3815-3822 (1979)
R W Glanville et al.
European journal of biochemistry, 95(2), 383-389 (1979-04-02)
Native type IV collagen was isolated from human placenta using pepsin solubilisation followed by fractional salt precipitation and chromatogarphic purification. The native preparation was characterised using amino acid analyses, disc gel electrophoresis, segment-long-spacing crystallites and immunological methods. Two component alpha

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