Collagen from calf skin

Bornstein and Traub Type I, solid, BioReagent, suitable for cell culture

CAS Number:
EC Number:
MDL number:

Quality Level

biological source

bovine (calf) skin



product line





poly bottle of 10 mg
poly bottle of 100 mg
poly bottle of 250 mg
poly bottle of 50 mg


not available in Canada (at this time; for questions or status updates, please email us at antibody.canada@sial.com)


cell culture | mammalian: suitable

surface coverage

6‑10 μg/cm2


0.1 M acetic acid: 1 mg/mL (Allow to stir at room temperature 1-3 hours until dissolved.)

UniProt accession no.

shipped in


storage temp.


Gene Information

bovine ... COL1A1(282187)

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General description

Collagen type I is a component of skin, bone, tendon, and other fibrous connective tissues. It is a left handed helix with three polypeptide chains and contains repeating units of glycine, proline and hydroxyproline amino acids. It is a component of extracellular matrix and close to 28 types is present in bovine.


Collagen from calf skin has been used:
  • as a component of collagen gel matrix for culturing preantral follicles
  • as a component of Roswell Park Memorial Institute, for culturing gilthead seabream kidney leukocytes and macrophages and acidophilic granulocytes
  • to coat transwells prior to seeding of epithelial cell culture

This product is intended to produce thin layer coatings on tissue culture plates to facilitate attachment of anchorage-dependent cells, recommended for use at 6-10 μg/cm2. It is NOT intended for production of 3-D gels. Type I collagen is often used in cell culture as an attachment substratum with myoblasts, spinal ganglia, hepatocytes, embryonic lung, heart explants, fibroblasts, endothelial cells, and islet cells have all been cultured successfully on films or gels of type I collagen. Collagen type I may also be used in research of Idiopathic pulmonary fibrosis (IPF), studies on the effect of ER stress IPF on lung fibroblasts. Collagen in acidic solution can produce three dimensional scaffolding with use in bioengineering and cell culture applications.


10, 50, 100, 250 mg in poly bottle

Biochem/physiol Actions

Mutations in collagen encoding proteins are implicated cattle diseases. Collagen type I on heat denaturation results in disruption of triple helix to a randomly coils. It has applications in food and cosmetics and is used as biomaterial in in tissue engineering.
Type I collagen is a component of skin, bone, tendon, and other fibrous connective tissues.


All collagen molecules are composed of three polypeptide chains arranged in a triple helical conformation, with a primary structure that is mostly a repeating motif with glycine in every third position and proline or 4-hydroxyproline frequently preceding the glycine residue. Type I collagen differs from other collagens by its low lysine hydroxylation and low carbohydrate composition.

Preparation Note

This product was prepared by a modification of Gallop, P.M. and Seifter, S., Meth. Enzymol., VI, 635 (1963). It is soluble at 1 mg/mL in .1 M acetic acid and should be stirred at room temperature for 1-3 hours until dissolved.

Other Notes

Collagen is classified into a number of structurally and genetically distinct types. We use the nomenclature proposed by Bornstein and Traub. Do not confuse Sigma type designations with recognized collagen classification types.

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves


NONH for all modes of transport

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

Krister Gjestvang Grønlien et al.
International journal of biological macromolecules, 156, 394-402 (2020-04-15)
Natural deep eutectic solvents (NADES) have previously shown antibacterial properties alone or in combination with photosensitizers and light. In this study, we investigated the behavior of the structural protein collagen in a NADES solution. A combination of collagen and NADES...
Collagen regulates the activation of professional phagocytes of the teleost fish gilthead seabream
Castillo-Briceno P, et al.
Molecular Immunology, 46(7), 1409-1415 (2009)
D Warnecke et al.
Osteoarthritis and cartilage, 28(11), 1482-1491 (2020-08-03)
Because the literature relating to the influence of degeneration on the viscoelasticity and tissue composition of human lateral menisci remains contradictory or completely lacking, the aim of this study was to fill these gaps by comprehensively characterising the biomechanical properties...
Survival and developmental competence of buffalo preantral follicles using three-dimensional collagen gel culture system
Sharma GT, et al.
Animal Reproduction Science, 114(1-3), 115-124 (2009)
Thermal stability of calf skin collagen type I in salt solutions
Komsa-Penkova R, et al.
Biochimica et Biophysica Acta, Protein Structure and Molecular Enzymology, 1297(2), 171-181 (1996)
Cancer stem cell media, spheroid plates and cancer stem cell markers to culture and characterize CSC populations.
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Extracellular matrix proteins such as laminin, collagen, and fibronectin can be used as cell attachment substrates in cell culture.
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