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Sigma-Aldrich

Bovine Collagen Type I

from bovine skin, liquid, 6 mg/mL, suitable for cell culture, used for 3D gel formation

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About This Item

MDL number:
MFCD00130825
UNSPSC Code:
12352202
NACRES:
NA.75

product name

Collagen solution from bovine skin, Type I, 6 mg/mL, sterile-filtered, BioReagent, and for 3D matrix formation., suitable for cell culture

biological source

bovine skin

Quality Level

200

sterility

sterile-filtered

product line

BioReagent

form

liquid

packaging

pkg of 50 mL

concentration

6 mg/mL

technique(s)

cell culture | mammalian: suitable using and for 3D matrix formation.

surface coverage

6‑10 μg/cm2

Binding Specificity

Peptide Source: Collagen

Peptide Source: Elastin

Peptide Source: Fibronectin

foreign activity

endotoxin ≤1.0 μmole/min-mg protein

shipped in

wet ice

storage temp.

2-8°C

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General description

In mammals, collagen type 1 is a widely expressed fibrous protein. It constitutes to one-third of the total protein in humans. Collagen fibril is the basic component of the tissues containing collagen. It is predominantly expressed in the extracellular matrix, and is also found in arterial walls, tendons, ligaments, skin, cornea, bone and dentin. Collagen structure possesses a triple helix polypeptide strand.

Application

Collagen solution from bovine skin has been used as a substrate in cell adhesion assay.
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 type 1 is a versatile building material required for tissue elasticity and maintains the stability and strength in a variety of tissues. Collagen is also present in byssus thread of invertebrates, which helps in surface attachment. Defective collagen affects the biomechanical property of arterial tissue.
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.

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 6 mg/mL aqueous solution in 0.01 M HCl at a pH of 2.0.

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.

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Dario Mendes Júnior et al.
Antibiotics (Basel, Switzerland), 10(6) (2021-07-03)
The experimental use of poly (alcohol-vinyl) (PVA) as a skin curative is increasing widely. However, the use of this hydrogel is challenging due to its favorable properties for microbiota growth. The association with silver nanoparticles (AgNPs) as an antimicrobial agent
Collagen: structure and mechanics, an introduction
Collagen, 1-13 (2008)
Collagen in arterial walls: biomechanical aspects
Collagen, 285-324 (2008)
Collagen structure and stability
Shoulders M D and Raines R T
Annual Review of Biochemistry, 78 (2009)
Sanghun Park et al.
Biomolecules, 12(6) (2022-06-25)
Among future food problems, the demand for meat is expected to increase rapidly, but the production efficiency of meat, which is a protein source, is very low compared to other foods. To address this problem, research on the development and
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