C4243
Collagen solution from bovine skin
BioReagent, suitable for cell culture, and for 3D matrix formation, sterile-filtered
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About This Item
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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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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
Certificates of Analysis (COA)
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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
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
The Biomedical Engineering Handbook (1999)
TGF-β and TNF-α: antagonistic cytokines controlling type I collagen gene expression.
Verrecchia F & Mauviel A
Cellular Signalling, 16(8), 873-880 (2004)
Experimental murine myopia induces collagen type Iα1 (COL1A1) DNA methylation and altered COL1A1 messenger RNA expression in sclera.
Zhou X, et al.
Molecular Vision, 18, 1312-1312 (2012)
Articles
Extracellular matrix proteins such as laminin, collagen, and fibronectin can be used as cell attachment substrates in cell culture.
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