other

Human LMW urokinase

MBS135608

0.1 mg

425 USD

Protease

Human LMW urokinase

[LMW urokinase]

[urokinase-type plasminogen activator isoform 2; Urokinase-type plasminogen activator; urokinase-type plasminogen activator; U-plasminogen activator; plasminogen activator, urinary; plasminogen activator, urokinase]

[PLAU]

[PLAU; PLAU; ATF; QPD; UPA; URK; u-PA; BDPLT5; U-plasminogen activator; uPA]

UROK_HUMAN

414

>95% by SDS-PAGE analysis

Frozen liquid

6.4 mg/ml

Store at -70°C. Shelf Life: 3 years from delivery. Shipping: Ships with Dry Ice.

Source: Insect cell culture

Buffer: 0.05M Sodium Acetate; 0.1M NaCl; 1mM EDTA; pH 5.0. Extinction Coefficient: 1.4. Volume: 0.016ml. Aliquot: 1 x 0.1mg

Urokinase (uPA); Human Urokinase

The low molecular weight form of uPA is purified from auto-catalytic digestion of recombinant human urokinase produced in insect cells. LMW uPA contains the proteinase domain and is separated from the amino terminal fragment by cleavage at the Lys135-Lys136 bond. For plasminogen activation and receptor binding studies.

222537759

NP_001138503.1

NM_001145031.1

P00749

33,000

ATF-2 Transcription Factor Network Pathway (138006); Blood Clotting Cascade Pathway (198840); Complement And Coagulation Cascades Pathway (198880); Complement And Coagulation Cascades Pathway (83073); Complement And Coagulation Cascades Pathway (484); DNA Damage Response (only ATM Dependent) Pathway (198827); Dissolution Of Fibrin Clot Pathway (106061); E2F Transcription Factor Network Pathway (137934); Endochondral Ossification Pathway (198812); FGF Signaling Pathway (137989)

This gene encodes a serine protease involved in degradation of the extracellular matrix and possibly tumor cell migration and proliferation. A specific polymorphism in this gene may be associated with late-onset Alzheimer's disease and also with decreased affinity for fibrin-binding. This protein converts plasminogen to plasmin by specific cleavage of an Arg-Val bond in plasminogen. Plasmin in turn cleaves this protein at a Lys-Ile bond to form a two-chain derivative in which a single disulfide bond connects the amino-terminal A-chain to the catalytically active, carboxy-terminal B-chain. This two-chain derivative is also called HMW-uPA (high molecular weight uPA). HMW-uPA can be further processed into LMW-uPA (low molecular weight uPA) by cleavage of chain A into a short chain A (A1) and an amino-terminal fragment. LMW-uPA is proteolytically active but does not bind to the uPA receptor. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Feb 2009]

uPA: Specifically cleave the zymogen plasminogen to form the active enzyme plasmin. Defects in PLAU are the cause of Quebec platelet disorder (QPD). QPD is an autosomal dominant bleeding disorder due to a gain-of-function defect in fibrinolysis. Although affected individuals do not exhibit systemic fibrinolysis, they show delayed onset bleeding after challenge, such as surgery. The hallmark of the disorder is markedly increased PLAU levels within platelets, which causes intraplatelet plasmin generation and secondary degradation of alpha-granule proteins. Belongs to the peptidase S1 family. 2 isoforms of the human protein are produced by alternative splicing. Protein type: Protease; EC 3.4.21.73; Secreted, signal peptide; Secreted; Motility/polarity/chemotaxis. Chromosomal Location of Human Ortholog: 10q22.2. Cellular Component: extracellular space; focal adhesion; cell surface; plasma membrane; extracellular region. Molecular Function: protein binding; serine-type endopeptidase activity. Biological Process: fibrinolysis; regulation of cell adhesion mediated by integrin; regulation of smooth muscle cell migration; smooth muscle cell migration; response to hypoxia; regulation of receptor activity; blood coagulation; chemotaxis; signal transduction; proteolysis; regulation of cell proliferation. Disease: Quebec Platelet Disorder; Alzheimer Disease

0.1 mg

425 USD

1 mg

2785