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CC050 Sigma-Aldrich

Human Collagen Type I

  •  eCl@ss 32160405

  •  NACRES NA.75

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Properties

Quality Level   100
biological source   human
assay   >90% (collagen type I, SDS-PAGE)
form   liquid
mfr. no.   Chemicon®
concentration   1 mg/mL
application(s)   cell culture | mammalian: suitable
impurities   <1% collagen type II,IV-VI & non-collagen proteins.
  <10% collagen type III
input   sample type mesenchymal stem cell(s)
sample type induced pluripotent stem cell(s)
sample type neural stem cell(s)
sample type: human embryonic stem cell(s)
sample type epithelial cells
sample type pancreatic 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
shipped in   dry ice
storage temp.   −20°C
Gene Information   human ... COL1A1(1277)

Description

General description

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}

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.

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

Safety & Documentation

Safety Information

Flash Point(F) 
Not applicable
Flash Point(C) 
Not applicable
Protocols & Articles

Articles

Extracellular Matrix Proteins and tools for cell culture optimization

Animal cells and tissue culture techniques are constantly improved to optimize in vitro cell culture conditions. Extracellular Matrix (ECM) proteins coating, chemical or physical modification of the ...
Keywords: Adhesion, Angiogenesis, Apoptosis, Asymmetric synthesis, Cancer, Cell attachment, Cell culture, Cell proliferation, Coagulation, Endocrinology, Growth factors, Hormones

What is the Extracellular Matrix?

The extracellular matrix (ECM) is secreted by cells and surrounds them in tissues. It has long been understood to be the structural support for cells since its characteristics set the characteristics...
Keywords: Adhesion, Cell culture, Cellular processes, Epimerizations, Growth factors, Immobilization, Sulfations

Protocols

ECM Coating Protocols for Millicell

Coating of membranes and plastic surfaces with extra cellular matrices (ECMs) promotes cell attachment and monolayer formation. We have developed protocols for four types of ECMs on Millicell®-CM ins...
Keywords: Cell attachment, Cell culture, Condensations

Peer-Reviewed Papers
15

References

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