protein

Collagen Type III

MBS634496

0.1 mg

375 USD

Protein

Collagen Type III

Collagen Type III

collagen type III alpha 1

Human placenta, negative for HbsAG, HCV, and HIV 1 and 2 antibodies

Human collagen type III: 90% pure by SDS-PAGE. Human collagen type I: <10% ; Human collagen types II, IV-VI, and non-collagen proteins:<1% Retention of native structure confirmed by ability to form microgibrils. Purified by serial salt precipitations, alc

Supplied as a liquid in 0.5M acetic acid, pH2.5

1mg/ml

Maintain at -20 deg. C in undiluted aliquots. Stable for 12 months at -20 deg. C. For maximum recovery of product, centrifuge the original cial after thawing and prior to removing the cap. Further diltions can be made in assay buffer.

Contaminants: >2% collagen type I, >2% collagen type IV, >1% collagen type V and 0.5% non-collagen proteins. Composition : [alpha1(III)]3, native triple helix. Ability to form native helical structure verified by ORD measurement, competence in microfibril formation and reactivity with anti-collagen type-specific monoclonal antibodies.

Molecular Biology; MB-Collagen

Collagen is an inert, rigid protein found predominantly in skin, ligaments, bones and teeth. Its most distinctive attribute, essential to a transmitter of mechanical force, is inelasticity. Its fundamental structural unit is tropo-collagen, a molecular rod about 2600 in length, 15 in diameter, and 300,000 molecular weight. In tendons these macromolecules, grouped as collagen fibrils, run parallel to the axis. In skin the fibrils are interlaced and branched.

494319369

AGL34959.1

This gene encodes the pro-alpha1 chains of type III collagen, a fibrillar collagen that is found in extensible connective tissues such as skin, lung, uterus, intestine and the vascular system, frequently in association with type I collagen. Mutations in this gene are associated with Ehlers-Danlos syndrome types IV, and with aortic and arterial aneurysms. Two transcripts, resulting from the use of alternate polyadenylation signals, have been identified for this gene. [provided by R. Dalgleish, Feb 2008]

CO3A1: Collagen type III occurs in most soft connective tissues along with type I collagen. Defects in COL3A1 are a cause of Ehlers-Danlos syndrome type 3 (EDS3); also known as benign hypermobility syndrome. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS3 is a form of Ehlers-Danlos syndrome characterized by marked joint hyperextensibility without skeletal deformity. Defects in COL3A1 are the cause of Ehlers-Danlos syndrome type 4 (EDS4). EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS4 is the most severe form of the disease. It is characterized by the joint and dermal manifestations as in other forms of the syndrome, characteristic facial features (acrogeria) in most patients, and by proneness to spontaneous rupture of bowel and large arteries. The vascular complications may affect all anatomical areas. Defects in COL3A1 are a cause of susceptibility to aortic aneurysm abdominal (AAA). AAA is a common multifactorial disorder characterized by permanent dilation of the abdominal aorta, usually due to degenerative changes in the aortic wall. Histologically, AAA is characterized by signs of chronic inflammation, destructive remodeling of the extracellular matrix, and depletion of vascular smooth muscle cells. Belongs to the fibrillar collagen family. 2 isoforms of the human protein are produced by alternative splicing. Protein type: Extracellular matrix; Motility/polarity/chemotaxis; Secreted, signal peptide; Cell adhesion; Secreted. Chromosomal Location of Human Ortholog: 2q31. Cellular Component: extracellular matrix; extracellular space; endoplasmic reticulum lumen; extracellular region; collagen type III. Molecular Function: integrin binding; protein binding; metal ion binding; platelet-derived growth factor binding; extracellular matrix structural constituent; SMAD binding. Biological Process: skin development; integrin-mediated signaling pathway; receptor-mediated endocytosis; axon guidance; platelet activation; extracellular matrix organization and biogenesis; collagen fibril organization; wound healing; heart development; cell-matrix adhesion; negative regulation of immune response; positive regulation of Rho protein signal transduction; collagen catabolic process; extracellular matrix disassembly; response to radiation; gut development; response to mechanical stimulus; response to cytokine stimulus; transforming growth factor beta receptor signaling pathway; fibril organization and biogenesis; peptide cross-linking; cerebral cortex development; skeletal development; aging. Disease: Ehlers-danlos Syndrome, Type Iv, Autosomal Dominant; Ehlers-danlos Syndrome, Type Iii

0.1 mg

375 USD