protein

Recombinant Human Collagen-3

MBS143033

10 mg

280 USD

Recombinant Protein

Recombinant Human Collagen-3

Collagen-3

Collagen alpha-1(III) chain, COL3A1, EDS4A, FLJ34534

collagen alpha-1(III) chain preproprotein; Collagen alpha-1(III) chain; collagen alpha-1(III) chain; collagen alpha-1(III) chain; Ehlers-Danlos syndrome type IV, autosomal dominant; alpha1 (III) collagen; collagen, fetal; collagen, type III, alpha 1

COL3A1; COL3A1; EDS4A

CO3A1_HUMAN

Pichia Pastoris

1466

3.4 mg/ml in 10mM HCl. Appearance: Sterile Filtered colorless solution.

3.4 mg/ml

Collagen-III should be stored at 2-8 degree C.

RECOMBINANT & NATURAL PROTEINS; Recombinant Proteins; Collagen

Description: DNA sequences encoding the human proalpha1 (III) and both alpha and beta subunits of prolyl hydroxylase were co-expressed in the yeast Pichia pastoris. Procollagen III was converted into mature collagen by a controlled proteinase digestion. Introduction: Collagen, a major component of the extracellular matrix, is a fibrous protein that provides tensile strength to tissues giving them structural integrity. Collagen and its derivative, gelatin, have been widely used in medical, pharmaceutical and consumer products for more than 100 years. The supply of these materials, created from animal remains, is both abundant and inexpensive. However, most formulations are not highly purified and have the potential to cause an inflammatory reaction in some product users. In addition, concerns have been raised over the last several years about the potential for contamination of bovine products with the agent that causes mad cow disease and its human variant, Creutzfeldt-Jakob Disease. Animal collagens are subject to extensive modifications that continue over the life of the molecule in the extracellular space. These differences influence both the extractability of collagens from tissue and the biophysical characteristics of these collagens. As a result, collagens isolated from tissues exhibit significant lot-to-lot variability and, as bulk materials, are often analytically intractable. Products that contain animal-derived collagen can induce potentially harmful inflammatory or immune responses in humans and pose risk of contamination with viruses or prions, potentially life-threatening pathogens. Recombinant collagens are essentially identical to the native collagen protein thereby reducing the risk of inflammation, immune response, and disease as compared to animal-sourced collagen.

4502951

NP_000081.1

NM_000090.3

P02461

Amoebiasis Pathway (167324); Amoebiasis Pathway (167191); Assembly Of Collagen Fibrils And Other Multimeric Structures Pathway (730306); Binding And Uptake Of Ligands By Scavenger Receptors Pathway (771599); Collagen Biosynthesis And Modifying Enzymes Pathway (645289); Collagen Formation Pathway (645288); ECM-receptor Interaction Pathway (83068); ECM-receptor Interaction Pathway (479); Endothelins Pathway (137958); Extracellular Matrix Organization Pathway (576262)

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: Motility/polarity/chemotaxis; Secreted, signal peptide; Cell adhesion; Secreted; Extracellular matrix. 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: integrin-mediated signaling pathway; skin development; platelet activation; receptor-mediated endocytosis; axon guidance; extracellular matrix organization and biogenesis; collagen fibril organization; wound healing; cell-matrix adhesion; heart development; 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

10 mg

280 USD

50 mg

895

100 mg

1415