Human Urokinase-Type Plasminogen Activator (PLAU) Protein
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Description
Human Urokinase-Type Plasminogen Activator (PLAU) Protein is a recombinant Human protein expressed in HEK293 cells.
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Product specifications
| Category | Proteins and Peptides |
| Host | HEK293 cells |
| Origin | Human |
| Observed MW | Molecular Weight: Calculated MW: 47.3 kDa Observed MW (SDS-PAGE): 45 kDa Sequence Fragment: Met1-Leu431 Tag: C-terminal His tag |
| Expression | Recombinant |
| Purity | >95% (SDS-PAGE) |
| Size 1 | 20 µg |
| Size 2 | 100 µg |
| Form | Lyophilized Reconstitute in sterile H2O. Do not vortex. |
| Tested Applications | SDS-PAGE |
| Buffer | Prior to lyophilization: PBS, pH 7.4, containing 5% - 8% Trehalose, Mannitol and 0.01% Tween-80. |
| Availability | Shipped within 5-15 working days. |
| Storage | Store lyophilized between -20 °C and -80 °C. |
| Dry Ice | No |
| UniProt ID | P00749 |
| OMIM | 19184 |
| Background | Protein PLAU |
| Status | RUO |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
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PLAU(Urokinase-type plasminogen activator) is also named as uPA and belongs to the peptidase S1 family.UPA initiates a proteolytic cascade, which degrades extracellular matrix during tissue growth and remodelling.The secreted proform of UPA is activated after binding to a specific high affinity cell surface receptor. Secreted UPA is exposed to rapid inactivation in the pericellular space by plasminogen activator inhibitor-1(PAI-1), which is stored in the extracellular matrix bound to vitronectin(PMID:9665342).It has 2 isoforms produced by alternative splicing.Defects in PLAU are the cause of Quebec platelet disorder(QPD).
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PLAU Antibody is a Rabbit Polyclonal antibody against PLAU. 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.
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