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C5483 Sigma-Aldrich

Collagen human

Bornstein and Traub Type I, acid soluble, powder, ~95% (SDS-PAGE)

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Properties

Related Categories Biochemicals and Reagents, Collagen, Proteins and Derivatives, Structural Proteins
assay   ~95% (SDS-PAGE)
form   powder
solubility   aqueous acid: ≤5 mg/mL
storage temp.   2-8°C
Gene Information   human ... COL1A2(1278)

Description

General description

Collagen type 1 alpha 2 (COL1A2) encodes pro-alpha2 chain and is a component of heterodimer, type 1 collagen fiber. It is mapped to human chromosome 7q21.3. COL1A2 associates with COL1A1 in the ratio 1:2 and undergoes posttranslational modification to form mature type I collagen fibre.

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.

Application

Collagen type I may be used in research of Idiopathic pulmonary fibrosis (IPF). Robust expression of collagen-type I is one distinctive feature of IPF. Additionally, collagen-type I has been used in studies on the effect of endoplasmic reticulum (ER) stress from IPF on myofibroblastic differentiation of lung fibroblasts. Collagen-type I soluble in acidic solution produces three dimensional scaffolding useful in bioengineering and cell culture applications where biomaterials are needed to replace native collagen extracellular matrices.

Collagen Type I has been used as a scaffold for the growth in vitro of stem cells in a wide variety of biomaterial engineering studies.

Human collagen has been used:
• as a component of extracellular matrix in the chemotaxis assay of the rat adipose-derived stem cells
• in adhesion assay of the adult retinal pigmented epithelium-19 (ARPE-19) cell line
• in the glycation aggregation and adsorption studies as a model system for arthritis

Packaging

1 mg in glass bottle

Biochem/physiol Actions

Collagen type 1 alpha 2 (COL1A2) is crucial for bone formation, cartilage and blood vessels. Imbalance in COL1A2 may be the cause for dental fluorosis. Missense mutations involving glycine substitutions in the COL1A2 gene alters the collagen triple helix structure decreasing its stability and is implicated in osteogenesis imperfecta. Mutations near the splice site of COL1A2 gene results in exon skipping and is associated with Ehlers-Danlos Syndrome. An insertion or deletion polymorphism in the COL1A2 gene impairs its interaction with microRNA and modulates the bone mineral density resulting in high susceptibility to osteoporosis.

Preparation Note

Prepared from human skin by modification of Gallop, P.M.

Safety & Documentation

Safety Information

RIDADR 
NONH for all modes of transport
WGK Germany 
1

Documents

Certificate of Analysis

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Certificate of Origin

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Protocols & Articles
Peer-Reviewed Papers
15

References

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