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Merck

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

CAS-Nummer:
EG-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352202
NACRES:
NA.77

CHF 392.00


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Produktbezeichnung

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

Biologische Quelle

human

Qualitätsniveau

Assay

~95% (SDS-PAGE)

Form

powder

Methode(n)

cell culture | stem cell: suitable

Löslichkeit

aqueous acid: ≤5 mg/mL

UniProt-Hinterlegungsnummer

Lagertemp.

2-8°C

Angaben zum Gen

human ... COL1A2(1278)

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Allgemeine Beschreibung

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]

Anwendung

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]

Biochem./physiol. Wirkung

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]

Angaben zur Herstellung

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

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 1

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


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Die Dokumentenbibliothek aufrufen

Structural models of osteogenesis imperfecta-associated variants in the COL1A1 gene
Mooney SD and Klein TE
Molecular and Cellular Proteomics, 1(11), 868-875 (2002)
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)
Rare autosomal recessive cardiac valvular form of Ehlers-Danlos syndrome results from mutations in the COL1A2 gene that activate the nonsense-mediated RNA decay pathway
Schwarze U, et al.
American Journal of Human Genetics, 74(5), 917-930 (2004)
Aggregation as a consequence of glycation: insight into the pathogenesis of arthritis
Shamsi A, et al.
European Biophysics Journal, 45(6), 523-534 (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)

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