C3867
Rat Collagen Type I
from rat tail, liquid, 4 mg/mL, suitable for cell culture
동의어(들):
Collagen from rat tail, Col1a1
제품 이름
Collagen, Type I solution from rat tail, BioReagent, suitable for cell culture, sterile-filtered
biological source
rat tail
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
soluble, clear to hazy, colorless (solubilized in 0.02M 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
Quality Level
Gene Information
rat ... Col1a1(29393)
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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.
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.
Other Notes
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.
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.
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%.
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%.
저장 등급
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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)
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)
On the adhesion-cohesion balance and oxygen consumption characteristics of liver organoids
Mattei G, et al.
Testing, 12(3), e0173206-e0173206 (2017)
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)
문서
The extracellular matrix (ECM) is secreted by cells and surrounds them in tissues.
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