Collagen from rat tail
SIGMA/C7661 - Bornstein and Traub Type I, powder, BioReagent, suitable for cell culture
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: C7661-100MG
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: C7661-10MG
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: C7661-25MG
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: C7661-50MG
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: C7661-5MG
| binding specificity | Peptide Source: Fibrinogen |
| Peptide Source: Laminin |
|
| biological source | rat tail |
| form | powder |
| mol wt | 120—160 kDa |
| NCBI accession no. |   |
| packaging | glass bottle of 5 mg |
| product line | BioReagent |
| Quality Level | 200 |
| solubility | soluble |
| storage temp. | 2-8°C |
| surface coverage | 6‑10 μg/cm2 |
| technique(s) | cell culture | mammalian: suitable |
| UniProt accession no. | P02454 |
| Application: | Collagen from rat tail is used for the following applications: • Immunohistochemistry • Cellular activity assays • Used in generation of dorsal root ganglion (DRG) explant cultures • Used as one of the components during the preparation of the functionalized surface (in NMR setup) • Used in cell culture (the glass coverslips were coated with nanowires at high concentrations mixed with collagen) • Used for biofunctionalization of the microchannels |
| Biochem/physiol Actions: | Collagen is an essential ingredient of connective tissue. Studies in a Chinese family show that mutation in COL1A1 (collagenase type I) is linked with type I osteogenesis imperfecta. Collagen is linked with subchondral turnover of bone, and might have potential as marker to determine the state of joint space narrowing and osteophytes in osteoarthritis.Collagen from rat tail 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. |
| 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. Col1a1 (collagen, type I, α1) or collagen is a major structural human protein, which assembles in the form of fibrils. It is a very long, thin and the most abundant protein found in the human body. It is a supercoiled right-helix of three left-handed polypeptide chains. These chains are composed of ~1040 amino acids, which are essentially repeats of three amino acids -(Gly-X-Y)n. Gly is glycine and X and Y can be any amino acids, but in humans are usually proline and hydroxyproline, respectively. |
| General description: | Product is clear to hazy colorless solution with a few insolubles at 1 mg/ml in water with 2 μl acetic acid (or 0.1 N acetic acid). The insolubles can be removed by settling or centrifugation. |
| 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, 25, 50, 100 mg in poly bottle |
| Packaging: | 5 mg in glass bottle |
| Preparation Note: | Product is clear to hazy colorless solution with a few insolubles at 1 mg/ml in water with addition of 2 μl acetic acid per mL H2O. The insolubles can be removed by settling or centrifugation. |
| 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 |