Collagen from calf skin
SIGMA/C9791 - Bornstein and Traub Type I, solid, BioReagent, suitable for cell culture
Synonym: Type I collagen
CAS Number: 9007-34-5
EC Number: 232-697-4
MDL Number: MFCD00130825
Product Type: Chemical
This picture is provided solely for illustration purposes. Optical properties of the actual product may deviate. Relevant product information is printed on labeled products and other accompanying or available information material. This image depicts SKU: C9791-100MG
This picture is provided solely for illustration purposes. Optical properties of the actual product may deviate. Relevant product information is printed on labeled products and other accompanying or available information material. This image depicts SKU: C9791-10MG
This picture is provided solely for illustration purposes. Optical properties of the actual product may deviate. Relevant product information is printed on labeled products and other accompanying or available information material. This image depicts SKU: C9791-50MG
This picture is provided solely for illustration purposes. Optical properties of the actual product may deviate. Relevant product information is printed on labeled products and other accompanying or available information material. This image depicts SKU: C9791-250MG
| binding specificity | Peptide Source: Fibronectin |
| Peptide Source: Laminin |
|
| biological source | bovine (calf) skin |
| form | solid |
| packaging | poly bottle of 10 mg |
| poly bottle of 100 mg | |
| poly bottle of 250 mg | |
| poly bottle of 50 mg | |
| product line | BioReagent |
| Quality Level | 200  |
| shipped in | ambient |
| solubility | 0.1 M acetic acid: 1 mg/mL (Allow to stir at room temperature 1-3 hours until dissolved.) |
| storage temp. | 2-8°C |
| surface coverage | 6‑10 μg/cm2 |
| technique(s) | cell culture | mammalian: suitable |
| UniProt accession no. | P02453  |
| Application: | Collagen from calf skin has been used: • as a component of collagen gel matrix for culturing preantral follicles • as a component of Roswell Park Memorial Institute, for culturing gilthead seabream kidney leukocytes and macrophages and acidophilic granulocytes • to coat transwells prior to seeding of epithelial cell culture |
| 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. |
| Biochem/physiol Actions: | Collagen from calf skin 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. Mutations in collagen encoding proteins are implicated cattle diseases. Collagen type I on heat denaturation results in disruption of triple helix to a randomly coils. It has applications in food and cosmetics and is used as biomaterial in in tissue engineering. |
| 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. Collagen type I is a component of skin, bone, tendon, and other fibrous connective tissues. It is a left handed helix with three polypeptide chains and contains repeating units of glycine, proline and hydroxyproline amino acids. It is a component of extracellular matrix and close to 28 types is present in bovine. |
| Other Notes: | 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. |
| 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. |
| Packaging: | 10, 50, 100, 250 mg in poly bottle |
| Preparation Note: | This product was prepared by a modification of Gallop, P.M. and Seifter, S., Meth. Enzymol., VI, 635 (1963). It is soluble at 1 mg/mL in .1 M acetic acid and should be stirred at room temperature for 1-3 hours until dissolved. |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 1 |
| Flash Point(F) | Not applicable |
| Flash Point(C) | Not applicable |
| Storage Temp. | 2-8°C |
| UNSPSC | 12352202 |