ELISA with Human PLAU/uPA Protein (pro form) 3521

Human PLAU/uPA Protein (pro form) 3521

$300.00 – $1,000.00

Summary

Expression: HEK293
Functional: Yes (ELISA)
Amino Acid Range: Ser21-Leu431

SKU: 3521parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	P00749
express system	HEK293
product tag	C-His
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	Plasminogen activator, urokinase (uPA) is a secreted serine protease whose Dysregulation is often accompanied by various cancers. PLAU inhibition could suppress tumor growth. Collectively, PLAU is necessary for tumor progression and can be a diagnostic and prognostic biomarker in HNSCC.
molecular weight	The protein has a predicted MW of 47.5 kDa. Due to glycosylation, the protein migrates to 52-60 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Human PLAU/uPA Protein (pro form) 3521

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
Plasminogen activator, urokinase (uPA) is a secreted serine protease whose Dysregulation is often accompanied by various cancers. PLAU inhibition could suppress tumor growth. Collectively, PLAU is necessary for tumor progression and can be a diagnostic and prognostic biomarker in HNSCC.
Protein names Urokinase-type plasminogen activator (U-plasminogen activator) (uPA) (EC 3.4.21.73) [Cleaved into: Urokinase-type plasminogen activator long chain A; Urokinase-type plasminogen activator short chain A; Urokinase-type plasminogen activator chain B]
Gene names PLAU,PLAU
Protein family Peptidase S1 family
Mass 9606Da
Function Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.
Subellular location Secreted .
Tissues Expressed in the prostate gland and prostate cancers.
Structure Found in high and low molecular mass forms. Each consists of two chains, A and B. The high molecular mass form contains a long chain A which is cleaved to yield a short chain A. Forms heterodimer with SERPINA5. Binds LRP1B; binding is followed by internalization and degradation. Interacts with MRC2. Interacts with PLAUR. In complex with SERPINE1, interacts with PLAUR/uPAR (PubMed:15053742). Interacts with SORL1 and LRP1, either alone or in complex with SERPINE1; these interactions are abolished in the presence of LRPAP1/RAP (PubMed:15053742). The ternary complex composed of PLAUR-PLAU-PAI1 also interacts with SORLA (PubMed:15053742).
Post-translational modification Phosphorylation of Ser-158 and Ser-323 abolishes proadhesive ability but does not interfere with receptor binding.; Produced as an inactive single-chain protein (pro-uPA or sc-uPA), is processed into the active disulfide-linked two-chain form of PLAU/uPA by a proteolytic event mediated, at least, by TMPRSS4.
Target Relevance information above includes information from UniProt accession: P00749
The UniProt Consortium

ELISA with Human PLAU/uPA Protein (pro form)

Immobilized Human PLAU, His Tag at 0.5µg/ml (100µl/Well) on the plate. Dose response curve for Human uPAR, hFc Tag with the EC50 of 2.4ng/ml determined by ELISA.

HPLC of Human PLAU/uPA Protein (pro form)

The purity of Human PLAU (pro form) is greater than 95% as determined by SEC-HPLC.

SDS-PAGE gel of Human PLAU/uPA Protein (pro form)

Human PLAU (pro form) on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

pmid	title	authors	citation
We haven't added any publications to our database yet.

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.