CC050

Human Collagen Type I

• UNSPSC Code: 12352202
• eCl@ss: 32160405
• NACRES: NA.75

Properties

• biological source: human
• Quality Level: 100
• Assay: >90% (collagen type I, SDS-PAGE)
• form: liquid
• manufacturer/tradename: Chemicon^®
• concentration: 1 mg/mL
• technique(s): cell culture | mammalian: suitable
• impurities: <1% collagen type II,IV-VI & non-collagen proteins.; <10% collagen type III
• input: sample type pancreatic stem cell(s); sample type mesenchymal stem cell(s); sample type epithelial cells; sample type induced pluripotent stem cell(s); sample type neural stem cell(s); sample type: human embryonic stem cell(s); sample type hematopoietic stem cell(s)
• solubility: water: soluble at 20 °C
• NCBI accession no.: NM_000088.3
• UniProt accession no.: P02452
• Binding Specificity: Peptide Source: Elastin; ; Peptide Source: Fibronectin
• shipped in: dry ice
• storage temp.: −20°C
• Gene Information: human ... COL1A1(1277)

Description

General description

Human type I collagen is purified by serial salt precipitations, alcohol precipitation and DEAE chromatography of a pepsin extraction of human placenta. Collagen is a major structural protein found in connective tissues such as skin, tendon, cartilage, ligaments, bone, the part of the eyeball that is white (sclera), and the spaces between cells and tissues called the extracellular matrix. It imparts structure and strength to the connective tissues. The gene for collagen type I alpha 1 (COL1A1) is mapped to human chromosome 17q21.33.Type I collagen is initially produced as procollagen in cells. This protein consists of two pro-alpha1(I) protein strands combined with a pro-alpha2(I) procollagen strand that form a triple-stranded rope-like structure. While in the cell, enzymes modify certain amino acids in the protein (lysine and proline) by adding chemical groups that are necessary for the three strands to form stable molecules and make connections (cross-links) between chains. Other enzymes add sugars to the protein. Now complete, the triple-stranded type I procollagen molecule leaves the cell and is processed by enzymes that clip small segments off both ends. The procollagen molecules arrange themselves into long, thin fibrils outside of the cell. The fibrils come together in side-by-side groups to form collagen fibers. Cross-linking between molecules in fibrils produces a very stable protein structure, which contributes to collagen tissue strengthening function.

Application

Human Collagen Type I has been used:

• as a control in the 2B4 nuclear factor of activated T-cells (NFAT)–GFP reporter cell assay, where its interaction with reporter cells can be evaluated for nuclear factor of activated T-cells (NFAT) promoter-driven GFP expression
• for coating glass slides in dynamic binding assays to create a substrate for the specific binding and study of platelets and conjugates in flow channels
• as a protein standard in histological analysis of lung tissue samples, providing a reference for the composition and characterization of extracellular matrix (ECM) components

Biochem/physiol Actions

Mutations in the collagen type I alpha 1 (COL1A1) gene are associated with osteogenesis imperfecta types I–IV, Ehlers-Danlos syndrome type VIIA, Ehlers-Danlos syndrome Classical type, Caffey Disease and idiopathic osteoporosis.

Physical form

Purified protein. Liquid containing 0.5 M Acetic acid, pH 2.5. Can be diluted in PBS for applications.

Analysis Note

Purity was controlled by SDS-PAGE and reaction with anti-collagen type-specific antibodies

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.

Safety Information

• Storage Class Code: 12 - Non Combustible Liquids
• WGK: WGK 1
• Flash Point(F): Not applicable
• Flash Point(C): Not applicable