Merck
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C5483

Sigma-Aldrich

Collagen human

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

Número CAS:
Número EC:
Número MDL:

Nível de qualidade

100

fonte biológica

human

teor

~95% (SDS-PAGE)

forma

powder

technique(s)

cell culture | stem cell: suitable

solubilidade

aqueous acid: ≤5 mg/mL

nº de adesão UniProt

temperatura de armazenamento

2-8°C

Gene Information

human ... COL1A2(1278)

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Descrição geral

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.

Aplicação

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

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.

Embalagem

1 mg in glass bottle

Ações bioquímicas/fisiológicas

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.

Nota de preparo

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

Código de classe de armazenamento

13 - Non Combustible Solids

WGK

WGK 1

Ponto de fulgor (ºF)

Not applicable

Ponto de fulgor (ºC)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)

Certificado de análise

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Certificado de origem

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Aggregation as a consequence of glycation: insight into the pathogenesis of arthritis
Shamsi A, et al.
European Biophysics Journal, 45(6), 523-534 (2016)
Regulation of type I collagen genes expression
Rossert J, et al.
Nephrology, Dialysis, and Transplantation, 15(6), 66-68 (2000)
An insertion/deletion polymorphism within the 3'-untranslated region of COL1A2 confers susceptibility to osteoporosis
Jiang ZS and Hao ZH
Molecular Medicine Reports, 14(5), 4415-4421 (2016)
Tissue engraftment of hypoxic-preconditioned adipose-derived stem cells improves flap viability
Hollenbeck SC, et al.
Wound Repair and Regeneration, 20(6), 872-878 (2012)
Integrin activation or alpha9 expression allows retinal pigmented epithelial cell adhesion on Bruch?s membrane in wet age-related macular degeneration
Afshari FT, et al.
Brain, 133(2), 448-464 (2010)

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