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C8919

Sigma-Aldrich

Bovine Collagen Type I

from bovine skin, liquid, 1 mg/mL, suitable for cell culture

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About This Item

Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.75

product name

Collagen from calf skin, Bornstein and Traub Type I, (0.1% solution in 0.1 M acetic acid), aseptically processed, BioReagent, suitable for cell culture

Source biologique

bovine (calf) skin

Niveau de qualité

Stérilité

aseptically processed

Gamme de produits

BioReagent

Forme

solution (0.1% solution in 0.1 M acetic acid)

Conditionnement

pkg of 20 mL

Concentration

(0.1% solution in 0.1 M acetic acid)

Technique(s)

cell culture | mammalian: suitable

Couverture de surface

6‑10 μg/cm2

Numéro d'accès UniProt

Spécificité de la liaison

Peptide Source: Collagen

Peptide Source: Elastin

Peptide Source: Fibronectin

Conditions d'expédition

wet ice

Température de stockage

2-8°C

Informations sur le gène

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Description générale

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

Application

Collagen from calf skin has been used:
  • for pre-coting glass slides for immunofluorescence studies
  • as a cell adhesion factor and modification of poly(vinylidene fluoride-trifluoroethylene) (P(VDF-TrFE)) films for neuron culture
  • for coating culture dishes for murine embryonic fibroblasts 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.

Actions biochimiques/physiologiques

Collagen type I on heat denaturation results in disruption of triple helix to a randomly coil. Mutations in the collagen gene are implicated in a variety of cattle diseases. It has applications in food and cosmetics. Collagen is used as a biomaterial and as a tissue scaffold in tissue engineering. Collagen type I fiber assembly is very crucial for physiological processes and cellular signaling.

Composants

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.

Notes préparatoires

This product is a 0.1% (1mg/ml) solution of calf skin collagen 0.1 M acetic acid. The product′s appearance is turbid, milky white solution. It is recommended that dilutions of product are prepared in sterile water. Please refer to information given on the product information sheet prior to introduction of product to cells and media.

Autres remarques

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.

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Extracellular Collagen VI Has Prosurvival and Autophagy Instructive Properties in Mouse Fibroblasts
Castagnaro S, et al.
Frontiers in Physiology, 9(3), 1129-1129 (2018)
Collagen: a network for regenerative medicine
Pawelec KM, et al.
Journal of Material Chemistry B: Materials for Biology and Medicine, 4(40), 6484-6496 (2016)
Hedgehog antagonist cyclopamine isomerizes to less potent forms when acidified
Wilson SR, et al.
Journal of Pharmaceutical and Biomedical Analysis, 52(5), 707-713 (2010)
Culturing neurons on MEMS fabricated P (VDF-TrFE) films for implantable artificial cochlea
Shintaku H, et al.
Journal of Biomechanical Science and Engineering, 5(3), 229-235 (2010)
Extraction and characterization of collagen from buffalo skin for biomedical applications
Rizk MA and Mostafa NY
Orient. J. Chem., 32(3), 1601-1609 (2016)

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