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C7661

Sigma-Aldrich

Collagen from rat tail

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

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

biological source

rat tail

product line

BioReagent

form

powder

mol wt

120—160 kDa

packaging

glass bottle of 5 mg

technique(s)

cell culture | mammalian: suitable

surface coverage

6‑10 μg/cm2

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.)

NCBI accession no.

UniProt accession no.

Binding Specificity

Peptide Source: Fibrinogen

Peptide Source: Laminin

storage temp.

2-8°C

Gene Information

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This Item
C386711179179001C9791
Collagen from rat tail Bornstein and Traub Type I, powder, BioReagent, suitable for cell culture

Sigma-Aldrich

C7661

Collagen from rat tail

Collagen from rat tail tendon

Roche

11179179001

Collagen

form

powder

form

liquid

form

lyophilized (clear, colorless solution after reconstitution)

form

solid

packaging

glass bottle of 5 mg

packaging

pkg of 1 vial

packaging

pkg of 30 mg

packaging

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

-

surface coverage

6‑10 μg/cm2

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.)

solubility

-

solubility

-

solubility

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

General description

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. Col1a1 (collagen, type I, α1) or collagen is a major structural human protein, which assembles in the form of fibrils. It is a very long, thin and the most abundant protein found in the human body. It is a supercoiled right-helix of three left-handed polypeptide chains. These chains are composed of ~1040 amino acids, which are essentially repeats of three amino acids -(Gly-X-Y)n. Gly is glycine and X and Y can be any amino acids, but in humans are usually proline and hydroxyproline, respectively.

Application

Collagen from rat tail is used for the following applications:

  • Immunohistochemistry
  • Cellular activity assays
  • Used in generation of dorsal root ganglion (DRG) explant cultures
  • Used as one of the components during the preparation of the functionalized surface (in NMR setup)
  • Used in cell culture (the glass coverslips were coated with nanowires at high concentrations mixed with collagen)
  • Used for biofunctionalization of the microchannels

Biochem/physiol Actions

Collagen is an essential ingredient of connective tissue. Studies in a Chinese family show that mutation in COL1A1 (collagenase type I) is linked with type I osteogenesis imperfecta. Collagen is linked with subchondral turnover of bone, and might have potential as marker to determine the state of joint space narrowing and osteophytes in osteoarthritis.Collagen from rat tail 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.

Preparation Note

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.

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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