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C5483

Sigma-Aldrich

Human Collagen Type I

from human placenta, powder, ~95% (SDS-PAGE), suitable for cell culture

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About This Item

Numero CAS:
Numero CE:
Numero MDL:
Codice UNSPSC:
12352202
NACRES:
NA.77

413,00 €


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Nome del prodotto

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

Origine biologica

human

Livello qualitativo

Saggio

~95% (SDS-PAGE)

Stato

powder

tecniche

cell culture | stem cell: suitable

Solubilità

aqueous acid: ≤5 mg/mL

N° accesso UniProt

Temperatura di conservazione

2-8°C

Informazioni sul gene

human ... COL1A2(1278)

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Descrizione generale

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.
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.[1] COL1A2 associates with COL1A1 in the ratio 1:2 and undergoes posttranslational modification to form mature type I collagen fibre.[2]

Applicazioni

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.[3][4]
Human collagen has been used:
  • as a component of extracellular matrix in the chemotaxis assay of the rat adipose-derived stem cells[5]
  • in adhesion assay of the adult retinal pigmented epithelium-19 (ARPE-19) cell line[6]
  • in the glycation aggregation and adsorption studies as a model system for arthritis[7]

Azioni biochim/fisiol

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.[8] Missense mutations involving glycine substitutions in the COL1A2 gene alters the collagen triple helix structure decreasing its stability and is implicated in osteogenesis imperfecta.[9] Mutations near the splice site of COL1A2 gene results in exon skipping and is associated with Ehlers-Danlos Syndrome.[10] 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.[11]

Nota sulla preparazione

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

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)


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I clienti hanno visto anche

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1 of 4

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)
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)
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)
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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