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C3511

Sigma-Aldrich

Collagen from calf skin

Bornstein and Traub Type I (Sigma Type III), solid

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About This Item

Numéro CAS:
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352202

Source biologique

bovine (calf) skin

Forme

solid

Technique(s)

cell culture | mammalian: suitable

Solubilité

aqueous acid: soluble

Adéquation

suitable for substrate for collagenase

Numéro d'accès UniProt

Température de stockage

2-8°C

Informations sur le gène

bovine ... COL1A1(282187)

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Application

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

Type I collagen is a component of skin, bone, tendon, and other fibrous connective tissues.

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

Prepared by a modification of the method of Gallop, P.M., and Seifter, S., Meth. Enzymol., VI, 635 (1963).

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

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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The Biochemical journal, 314 ( Pt 1), 159-166 (1996-02-15)
The small dermatan sulphate protein decorin interacts via its core protein with fibrillar collagens, and its glycosaminoglycan chains were proposed to be capable of self-association. It was therefore of interest to study the role of decorin in the contraction of
Qiyin Fang et al.
The Review of scientific instruments, 75(1), 151-162 (2004-01-01)
We report the design and development of a compact optical fiber-based apparatus for in situ time-resolved laser-induced fluorescence spectroscopy (tr-LIFS) of biological systems. The apparatus is modular, optically robust, and compatible with the clinical environment. It incorporates a dual output
S Teixeira et al.
Journal of biomedical materials research. Part A, 95(1), 1-8 (2010-08-27)
This study concerns the preparation and in vitro characterization of functionalized hydroxyapatite (HA) porous scaffolds, which are intended to be used as drug-delivery systems and bone-regeneration matrices. Hydroxyapatite scaffolds were prepared using the polymer replication method, and, after being submitted
Zhongcheng Gong et al.
Biomedical materials (Bristol, England), 5(5), 055005-055005 (2010-09-10)
The objective was to investigate synovium-derived stromal cells (SDSCs) coupled with chitosan/collagen type I (CS/COL-I) scaffolds for cartilage engineering. CS/COL-I scaffolds were fabricated through freeze-drying and cross-linked by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide. SDSCs were isolated from synovium and cultured onto CS/COL-I scaffolds, constructs

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