Skip to Content
Merck
All Photos(1)

Key Documents

C2124

Sigma-Aldrich

Bovine Collagen Type I

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

Sign Into View Organizational & Contract Pricing


About This Item

MDL number:
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

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

Looking for similar products? Visit Product Comparison Guide

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.

Storage Class Code

10 - Combustible liquids

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Collagen: structure and mechanics, an introduction
Collagen, 1-13 (2008)
Collagen in arterial walls: biomechanical aspects
Collagen, 285-324 (2008)
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
Chuan-Hang Yu et al.
International journal of molecular sciences, 21(8) (2020-04-29)
Oral submucous fibrosis (OSF) has been recognized as a precancerous disorder in the oral cavity. Great effort has been made to inhibit the malignant progression of OSF over the past decades, but the cure of this fibrosis disease has not
Richard G J Dohmen et al.
NPJ science of food, 6(1), 6-6 (2022-01-26)
Cultured meat is an emergent technology with the potential for significant environmental and animal welfare benefits. Accurate mimicry of traditional meat requires fat tissue; a key contributor to both the flavour and texture of meat. Here, we show that fibro-adipogenic

Articles

Extracellular matrix proteins such as laminin, collagen, and fibronectin can be used as cell attachment substrates in cell culture.

Extracellular matrix proteins such as laminin, collagen, and fibronectin can be used as cell attachment substrates in cell culture.

Extracellular matrix proteins such as laminin, collagen, and fibronectin can be used as cell attachment substrates in cell culture.

Extracellular matrix proteins such as laminin, collagen, and fibronectin can be used as cell attachment substrates in cell culture.

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service