Human Collagen Type I
Description:
Human Collagen Type I
Trade Name:
Chemicon (Millipore)
Product Overview:
Human type I collagen purified by serial salt precipitations, alcohol precipitation and DEAE chromatography of a pepsin extraction of human placenta. Composition: [α1(I)]2, <α2(I), native triple helix.
Background Information:
COL1A1 is the gene responsible for the production of the alpha1(I) chain of type I collagen. Collagen, which adds structure and strength to connective tissues, is found throughout the body for example, in 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.
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's tissue strengthening function. {http://ghr.nlm.nih.gov}
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's tissue strengthening function. {http://ghr.nlm.nih.gov}
Key Applications:
- Positive Control
- Cell Culture
Usage Statement:
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Cell Culture Reagent Type:
- Stem Cell Reagents
- Attachment Factors
Concentration:
1 mg/mL
Stem Cell Workflow Stage:
Maintenance & Expansion
Gene Symbol:
- COL1A1
- OI4
Presentation:
Purified protein. Liquid containing 0.5 M Acetic acid, pH 2.5. Can be diluted in PBS for applications.
Stem Cell Type:
- Human Embryonic Stem Cells
- Mesenchymal Stem Cells
- Neural Stem Cells
- Hematopoietic Stem Cells
- Epithelial Progenitor Cells
- Pancreatic Stem Cells
Purity:
> 90% collagen type I. Purity was controlled by SDS-PAGE and reaction with anti-collagen type-specific antibodies. Contaminants: < 10% collagen type III, < 1% collagen type II, IV-VI and non-collagen proteins.
Protein or Enzyme Type:
Extracellular Matrix Proteins
Storage Conditions:
Maintain at -20°C in undiluted aliquots for up to 12 months. Avoid repeated freeze/thaw cycles.
Species:
Human
Source:
Human placenta, negative for HBsAG and HIV antibodies.