protein

Eukaryotic Procollagen III N-Terminal Propeptide (PIIINP)

MBS2086718

0.01 mg

185 USD

Protein

Eukaryotic Procollagen III N-Terminal Propeptide (PIIINP)

[Procollagen III N-Terminal Propeptide (PIIINP)]

[P3NP; N-Propeptide Of Type III Procollagen; Procollagen III Amino Terminal Propeptide]

[collagen alpha-1(III) chain preproprotein; Collagen alpha-1(III) chain; collagen alpha-1(III) chain; collagen type III alpha 1 chain]

[PIIINP]

[COL3A1; COL3A1; EDS4A]

293F cell

> 97%

PBS, pH7.4, containing 5% Trehalose.

Original Concentration: 250ug/mL

Storage:. Avoid repeated freeze/thaw cycles. Store at 2-8ºC for one month. Aliquot and store at -80ºC for 12 months. Stability Test:. The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37°C for 48h, and no obvious degradation and precipitation were observed. The loss rate is less than 5% within the expiration date under appropriate storage condition.

Positive Control; Immunogen; SDS-PAGE; Western Blot (WB).

(May be suitable for use in other assays to be determined by the end user.)

SDS-Page

Identification

Organism Species: Homo sapiens (Human). Source: Eukaryotic expression. Tags: N-terminal His Tag. Subcellular Location: Secreted, Extracellular matrix. Usage: Reconstitute in PBS (pH7.4) to a concentration of 0.1-1.0 mg/mL. Do not vortex.

Traits: Freeze-dried powder. Predicted isoelectric point: 4.0. Phenomenon explanation: The possible reasons that the actual band size differs from the predicted are as follows:. 1. Splice variants: Alternative splicing may create different sized proteins from the same gene. 2. Relative charge: The composition of amino acids may affects the charge of the protein. 3. Post-translational modification: Phosphorylation, glycosylation, methylation etc. 4. Post-translation cleavage: Many proteins are synthesized as pro-proteins, and then cleaved to give the active form. 5. Polymerization of the target protein: Dimerization, multimerization etc. Usage: Reconstitute in ddH2O to a concentration of 0.1-1.0 mg/mL. Do not vortex.

Eukaryotic proteins

4502951

NP_000081.1

NM_000090.3

P02461

Predicted Molecular Mass: 14.8kDa. Accurate Molecular Mass: 30kDa as determined by SDS-PAGE reducing conditions.

Amoebiasis Pathway (167324); Amoebiasis Pathway (167191); Assembly Of Collagen Fibrils And Other Multimeric Structures Pathway (730306); 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); Focal Adhesion Pathway (198795)

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: Cell adhesion; Extracellular matrix; Motility/polarity/chemotaxis; Secreted; Secreted, signal peptide. Chromosomal Location of Human Ortholog: 2q32.2. Cellular Component: collagen type III; endoplasmic reticulum lumen; extracellular matrix; extracellular region; extracellular space. Molecular Function: extracellular matrix structural constituent; integrin binding; platelet-derived growth factor binding; protein binding. Biological Process: cell-matrix adhesion; cerebral cortex development; collagen catabolic process; collagen fibril organization; extracellular matrix organization and biogenesis; fibril organization and biogenesis; heart development; integrin-mediated signaling pathway; negative regulation of immune response; peptide cross-linking; positive regulation of Rho protein signal transduction; regulation of immune response; response to cytokine stimulus; response to radiation; skin development; transforming growth factor beta receptor signaling pathway; wound healing. Disease: Ehlers-danlos Syndrome, Type Iii; Ehlers-danlos Syndrome, Type Iv, Autosomal Dominant

0.01 mg

185 USD

0.05 mg

390

0.1 mg

600

0.2 mg

745

0.5 mg

1460

1 mg

2175