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C3867

Sigma-Aldrich

Collagen, Type I solution from rat tail

BioReagent, suitable for cell culture, sterile-filtered

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Synonym(s):
Collagen from rat tail
CAS Number:
EC Number:
MDL number:
NACRES:
NA.75

biological source

rat tail

Quality Level

description

Approx. 100mg/vial ((35 - 40 ml) )

sterility

sterile-filtered

product line

BioReagent

Assay

>95% (SDS-PAGE)

form

liquid

mol wt

apparent mol wt 115-130 kDa by SDS-PAGE (doublet)
apparent mol wt 215-235 kDa by SDS-PAGE (doublet)

packaging

pkg of 1 vial

concentration

>0.5 mg/mL Biuret

technique(s)

cell culture | mammalian: suitable

surface coverage

6‑10 μg/cm2

impurities

Mycoplasma Test by Barile, none detected

solubility

water: 1 mg/mL, clear to hazy, colorless (with 2 ul acetic acid or 0.1 N acetic acid)

NCBI accession no.

UniProt accession no.

Binding Specificity

Peptide Source: Collagen

Peptide Source: Fibronectin

shipped in

wet ice

storage temp.

2-8°C

Gene Information

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1 of 4

This Item
C7661C6745C9791
Collagen from rat tail Bornstein and Traub Type I, powder, BioReagent, suitable for cell culture

C7661

Collagen from rat tail

Collagen from calf skin Bornstein and Traub Type I, solid, BioReagent, suitable for cell culture

C9791

Collagen from calf skin

sterility

sterile-filtered

sterility

-

sterility

sterile-filtered

sterility

-

biological source

rat tail

biological source

rat tail

biological source

human cell culture

biological source

bovine (calf) skin

assay

>95% (SDS-PAGE)

assay

-

assay

-

assay

-

concentration

>0.5 mg/mL Biuret

concentration

-

concentration

0.3 mg/mL

concentration

-

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

General description

Collagen is an extracellular matrix protein comprising triple helical structure. The structure of collagen type I, in particular, is characterized by the presence of three identical α-chains in its homotrimetric form. Among these three α-chains, one exhibits slight sequence variation. Type I collagen was first isolated from rat-tail tendon, has two main α chains (α and α ) and one β chain.

Application

Collagen, Type I solution from rat tail has been used for coating culture plates and dishes for human hepatocyte HepG2 cell line and podocytes. It has also been used as a standard for total collagen content calibration curve generation for the quantification of liver extracellular matrix pre-gel.
Used as a coating material to support adherent cells growth and differentiation.

Biochem/physiol Actions

Collagen protein is essential for the mechanical integrity of tendons and bone. Rat tail tendon collagen is used in tissue engineering especially in the generation of 3-D scaffolds based gels. It has low antigenicity and is compatible with human gingival fibroblasts and human oral keratinocytes.

Features and Benefits

  • Sourced from rat tail.
  • Sterile-filtered to minimize contamination risks.
  • Suitable for a wide range of cell culture applications.
  • Provides optimal surface coverage (6-10 μg/cm2) for promoting cell adhesion and proliferation.

Preparation Note

Recommended for use as a cell culture substratum. May not be suitable for 3-D gel formation.
Sterile solution prepared from rat tail tendons by a modification of the published extraction method 1. It is supplied as an aqueous solution in 20mM acetic acid with a protein concentration as stated on the bottle. (approx.100mg protein per vial). Protein concentration was estimated by the Biuret method 2.
SDS polyacrylamide gel electrophoresis analysis shows the typical band pattern for Type I collagen, with a doublet at apparent molecular weights of 115 and 130kDa and another doublet at 215 and 235kDa. Based on this analysis, the purity of the collagen sample is >95%.

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.
When C3867 is first removed from the cooler it will appear gelled. When it is allowed to come fully to 37°C it will appear as a liquid.

related product

Product No.
Description
Pricing

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Thermal helix-coil transition in UV irradiated collagen from rat tail tendon
Sionkowska A and Kaminska A
International Journal of Biological Macromolecules, 24(4), 337-340 (1999)
Preparation of ready-to-use, storable and reconstituted type I collagen from rat tail tendon for tissue engineering applications
Rajan N, et al.
Nature Protocols, 1(6), 2753-2753 (2006)
Type I collagen extracted from rat-tail and bovine Achilles tendon for dental application: a comparative study
Techatanawat S, et al.
Asian Biomedicine : Research, Reviews and News, 5(6), 787-798 (2011)
Ectopic adenine nucleotide translocase activity controls extracellular ADP levels and regulates the F1-ATPase-mediated HDL endocytosis pathway on hepatocytes
Cardouat G, et al.
Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids, 1862(9), 832-841 (2017)
On the adhesion-cohesion balance and oxygen consumption characteristics of liver organoids
Mattei G, et al.
Testing, 12(3), e0173206-e0173206 (2017)

Articles

The extracellular matrix (ECM) and its attachment factor components are discussed in this article in relation to their function in structural biology and their availability for in vitro applications.

The extracellular matrix (ECM) is secreted by cells and surrounds them in tissues.

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