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C5483

Sigma-Aldrich

Collagen human

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

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CAS Number:
EC Number:
MDL number:

biological source

human

Quality Level

Assay

~95% (SDS-PAGE)

form

powder

technique(s)

cell culture | stem cell: suitable

solubility

aqueous acid: ≤5 mg/mL

UniProt accession no.

storage temp.

2-8°C

Gene Information

human ... COL1A2(1278)

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This Item
C9301C9879CC052
Collagen human Bornstein and Traub Type I, acid soluble, powder, ~95% (SDS-PAGE)

Sigma-Aldrich

C5483

Collagen human

Sigma-Aldrich

Sigma-Aldrich

CC052

Human Collagen Type II

assay

~95% (SDS-PAGE)

assay

-

assay

-

assay

90% (Human collagen type II)

form

powder

form

powder

form

powder

form

liquid

technique(s)

cell culture | stem cell: suitable

technique(s)

cell culture | mammalian: suitable

technique(s)

ELISA: suitable, activity assay: suitable

technique(s)

cell culture | mammalian: suitable

solubility

aqueous acid: ≤5 mg/mL

solubility

acetic acid: 0.5-2.0 mg/mL (Dissolve for several hours at 2-8 °C, occasionally swirling.)

solubility

-

solubility

water: soluble at 20 °C

UniProt accession no.

P08123

UniProt accession no.

P02460

UniProt accession no.

P02459

UniProt accession no.

P02458

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

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.

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Customers Also Viewed

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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)
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)
Gene expression of collagen type I alpha 2 and its relationship with dental fluorosis.
Gastelbondo-Pastrana B, et al.
Journal of Oral Research, 7(6), 172-175 (2018)
Aggregation as a consequence of glycation: insight into the pathogenesis of arthritis
Shamsi A, et al.
European Biophysics Journal, 45(6), 523-534 (2016)

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