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C4243

Sigma-Aldrich

Collagen solution from bovine skin

BioReagent, suitable for cell culture, and for 3D matrix formation, sterile-filtered

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MDL number:
NACRES:
NA.75

biological source

bovine skin

Quality Level

sterility

sterile-filtered

product line

BioReagent

Assay

≥99.9% (SDS-PAGE)

form

liquid

packaging

pkg of 100 mL
pkg of 20 mL

concentration

2.9-3.2 mg/mL

technique(s)

cell culture | mammalian: suitable

surface coverage

6‑10 μg/cm2

suitability

gelation test tested

UniProt accession no.

Binding Specificity

Peptide Source: Fibrinogen

foreign activity

endotoxin ≤1.0 μmole/min-mg protein

shipped in

wet ice

storage temp.

2-8°C

Gene Information

human ... COL1A1(282187)

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This Item
C2124C8919L7213
Sigma-Aldrich

C4243

Collagen solution from bovine skin

Sigma-Aldrich

C2124

Collagen solution from bovine skin

Sigma-Aldrich

C8919

Collagen from calf skin

Sigma-Aldrich

L7213

Collagen G

sterility

sterile-filtered

sterility

sterile-filtered

sterility

aseptically processed

sterility

-

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable

concentration

2.9-3.2 mg/mL

concentration

6 mg/mL

concentration

(0.1% solution in 0.1 M acetic acid)

concentration

4 mg/mL

assay

≥99.9% (SDS-PAGE)

assay

-

assay

-

assay

-

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

General description

Collagen solution is derived by dissolving collagen molecules in an aqueous solution. Collagen type Iα1 (COL1A1) is encoded by the gene that is located on human chromosome 17q21.33. It is the most abundant extracellular matrix (ECM) protein in humans. Type 1 collagen is the major structural protein of bone, tendon, skin and cornea. The encoded protein is a heterotrimer consisting of two α1-chains and one α2-chain.Type I collagen differs from other collagens by its low lysine hydroxylation and low carbohydrate composition. As a heterodimer composed of two a1 chains and one a2 chains, it spontaneously forms a triple helix scaffold at neutral pH and 37°C.

Application

Collagen solution from bovine skin has been used

  • in the preparation of collagen gels.
  • to coat cell culture dishes for HeLa cell line culture.
  • to construct hydrogels laden for HepG2 cell culture.
This highly purified solution is suitable for 3-D matrix formation in cell culture. 3-D collagen gels imitate the in vivo cell physiology better than traditional 2D systems and has been proven successful for several cell types including cardian and corneal fibroblasts, depatic stellate cells, and neuroblastoma cells. Such 3-D gels are also useful in studies of mechanotransduction, cell signaling involving the transformation of mechanical signals into biochemical signals

Biochem/physiol Actions

Collagen solution from bovine skin is a highly purified solution is suitable for 3-D matrix formation in cell culture. 3-D collagen gels imitate the in vivo cell physiology better than traditional 2D systems and has been proven successful for several cell types including cardian and corneal fibroblasts, depatic stellate cells, and neuroblastoma cells. Such 3-D gels are also useful in studies of mechanotransduction, cell signaling involving the transformation of mechanical signals into biochemical signals. Collagen, type I (COL1A1) participates in fibrosis. COL1A1 is an important component of the connective tissue matrix. It plays a vital role in the growth and maintenance of organ and tissue integrity. This protein also participates in the process of tissue repair.
In 3D environments, cell extensions can use integrins on cell surfaces to activate specific signaling pathways and integran-independent mechanical interactions resulting from the entanglement of matrix fibrils is possible.

Components

Type I collagen differs from other collagens by its low lysine hydroxylation and low carbohydrate composition. As a heterodimer composed of two a1 chains and one a2 chains, it spontaneously forms a triple helix scaffold at neutral pH and 37°C.

Caution

This product ships on wet ice and with recommended storage at 2-8°C, the product will last for 2 years.

Preparation Note

This product is prepared from type I bovine collagen purified and extracted from skin and contains a high monomer content. The raw collagen used to prepare this product has been isolated from a closed herd and purified with a GMP manufacturing process that includes inactivation of any possible prion or viral contamination. As supplied, it is a 3 mg/mL aqueous solution in 0.01 M HCl with a pH of 2.0. Collagen denatures when exposed to high temperatures or irradiation. Prior to a pH adjustment, store stock or diluted solutions refrigerated. Following a pH adjustment to 7, solutions should not exceed 40°C and should not be frozen.

Other Notes

Collagen is classified into a number of structurally and genetically distinct types. We use the nomenclature proposed by Bornstein and Traub. Be wary of confusing Sigma-type designations with recognized collagen classification types.

related product

Product No.
Description
Pricing

Storage Class Code

12 - Non Combustible Liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Oxygen Consumption Characteristics in 3D Constructs Depend on Cell Density
Chiara Magliaro, et al.
Frontiers in Bioengineering and Biotechnology, 7, 251-251 (2019)
Oxygen Consumption Characteristics in 3D Constructs Depend on Cell Density
Magliaro C, et al.
Frontiers in Bioengineering and Biotechnology, 7 (2019)
Xin-Hua Liao et al.
Scientific reports, 7, 43639-43639 (2017-03-07)
Hepatocellular carcinoma (HCC) is one of the most prevalent and malignant cancers with high inter- and intra-tumor heterogeneity. A central common signaling mechanism in cancer is proline-directed phosphorylation, which is further regulated by the unique proline isomerase Pin1. Pin1 is
Bursts of activity in collective cell migration
Chepizhko O, et al.
Journal of Separation Science, 113 (41) , 11408-11413 (2016)
Jun Ishihara et al.
Nature communications, 9(1), 2163-2163 (2018-06-06)
Laminin, as a key component of the basement membrane extracellular matrix (ECM), regulates tissue morphogenesis. Here, we show that multiple laminin isoforms promiscuously bind to growth factors (GFs) with high affinity, through their heparin-binding domains (HBDs) located in the α

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