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Recombinant Human uPAR/CD87 protein (His Tag)

Species

Human

Purity

>90 %, SDS-PAGE

Tag

His Tag

Activity

not tested

Cat no : Eg0901

Validation Data Gallery

  • Purity of Recombinant Human uPAR was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) conditions and stained using Coomassie blue.

    Purity of Recombinant Human uPAR was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) conditions and stained using Coomassie blue.

Product Information

Purity >90 %, SDS-PAGE
Endotoxin <0.1 EU/μg protein, LAL method
Activity 
Not tested
Expression HEK293-derived Human uPAR protein Leu23-Arg303 (Accession# Q03405-1) with a His tag at the C-terminus.
GeneID 5329
Accession Q03405-1
PredictedSize 32.4 kDa
SDS-PAGE 36-55 kDa, reducing (R) conditions
Formulation Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
Reconstitution Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
Storage Conditions
It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

Background

uPAR/PLAUR is a highly glycosylated GPI-anchored membrane protein. In addition to the membrane-anchored form, uPAR is released from the plasma membrane by cleavage of the GPI anchor and can be found as a soluble form (suPAR). uPAR contains three homologous domains (D1-D3) of which the N-terminal one (D1) represents the uPA-binding domain. After binding to uPAR, uPA cleaves plasminogen, generating the active protease plasmin which is involved in a wide variety of physiologic and pathologic processes. In addition to regulating proteolysis, uPAR has important function in cell adhesion, migration and proliferation. Studies reveal that uPAR expression is elevated during inflammation and tissue remodelling and in many human cancers, in which it frequently indicates poor prognosis. suPAR has been detected in plasma, and increased plasma concentrations of suPAR have been found in patients with some advanced cancers.

References:

1. Ploug M, Rønne E, Behrendt N, Jensen AL, Blasi F, Danø K. Cellular receptor for urokinase plasminogen activator. Carboxyl-terminal processing and membrane anchoring by glycosyl-phosphatidylinositol. J Biol Chem. 1991;266(3):1926-1933.
2. Stephens RW, Pedersen AN, Nielsen HJ, et al. ELISA determination of soluble urokinase receptor in blood from healthy donors and cancer patients. Clin Chem. 1997;43(10):1868-1876.
3. Blasi F, Carmeliet P. uPAR: a versatile signalling orchestrator. Nat Rev Mol Cell Biol. 2002 Dec;3(12):932-43.
4. Smith HW, Marshall CJ. Regulation of cell signalling by uPAR. Nat Rev Mol Cell Biol. 2010 Jan;11(1):23-36.