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C9791

Sigma-Aldrich

Collagen from calf skin

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

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CAS Number:
EC Number:
MDL number:
NACRES:
NA.75

biological source

bovine (calf) skin

product line

BioReagent

form

solid

packaging

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

availability

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

technique(s)

cell culture | mammalian: suitable

surface coverage

6‑10 μg/cm2

solubility

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

UniProt accession no.

shipped in

ambient

storage temp.

2-8°C

Gene Information

bovine ... COL1A1(282187)

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1 of 4

This Item
C2124C9301C7661
Collagen from rat tail Bornstein and Traub Type I, powder, BioReagent, suitable for cell culture

Sigma-Aldrich

C7661

Collagen from rat tail

form

solid

form

liquid

form

powder

form

powder

packaging

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

packaging

pkg of 50 mL

packaging

glass bottle of 100 mg, poly bottle of 25 mg, glass bottle of 5 mg

packaging

glass bottle of 5 mg

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable

surface coverage

6‑10 μg/cm2

surface coverage

6‑10 μg/cm2

surface coverage

6‑10 μg/cm2

surface coverage

6‑10 μg/cm2

solubility

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

solubility

-

solubility

acetic acid: 0.5-2.0 mg/mL (Dissolve for several hours at 2-8 °C, occasionally swirling.)

solubility

soluble (Product is clear to hazy colorless solution with a few insolubles at 1 mg/ml in water with 2 μl acetic acid (or 0.1 N acetic acid). The insolubles can be removed by settling or centrifugation.)

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.

Application

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.

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.

Components

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.

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Isolation and air-liquid interface culture of human large airway and bronchiolar epithelial cells
Bals R, et al.
Journal of Cystic Fibrosis : Official Journal of the European Cystic Fibrosis Society, 3, 49-51 (2004)
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)

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