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Recombinant Mouse uPAR/CD87 protein (rFc Tag)

Species

Mouse

Purity

>90 %, SDS-PAGE

Tag

rFc Tag

Activity

not tested

Cat no : Eg3156

Validation Data Gallery

  • Purity of Recombinant Mouse 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 Mouse 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 Mouse uPAR protein Leu24-Thr297 (Accession# P35456-1) with a rabbit IgG Fc tag at the C-terminus.
GeneID 18793
Accession P35456-1
PredictedSize 56.0 kDa
SDS-PAGE 65-90 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/CD87 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. et al. (1991). J Biol Chem. 266(3):1926-1933.
2. Stephens RW. et al. (1997). Clin Chem. 43(10):1868-1876.
3. Blasi F. et al. (2002). Nat Rev Mol Cell Biol. 3(12):932-943.
4. Smith HW. et al. (2010). Nat Rev Mol Cell Biol. 11(1):23-36.