C5483

Human Collagen Type I

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

• Numéro CAS: 9007-34-5
• Numéro CE : 232-697-4
• Numéro MDL: MFCD02687105
• Code UNSPSC : 12352202
• Nomenclature NACRES : NA.77

Propriétés

• Nom du produit: Collagen human, Bornstein and Traub Type I, acid soluble, powder, ~95% (SDS-PAGE)
• Source biologique: human
• Niveau de qualité: 100
• Essai: ~95% (SDS-PAGE)
• Forme: powder
• Technique(s): cell culture | stem cell: suitable
• Solubilité: aqueous acid: ≤5 mg/mL
• Numéro d'accès UniProt: P08123
• Température de stockage: 2-8°C
• Informations sur le gène: human ... COL1A2(1278)

Description

Description générale

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]

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.[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]

Actions biochimiques/physiologiques

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]

Notes préparatoires

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

Informations sur la sécurité

• Code de la classe de stockage: 11 - Combustible Solids
• Classe de danger pour l'eau (WGK): WGK 1
• Point d'éclair (°F): Not applicable
• Point d'éclair (°C): Not applicable
• Équipement de protection individuelle: Eyeshields, Gloves, type N95 (US)