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Recombinant Human uPAR Fc Chimera Protein, CF

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When Recombinant Human uPAR Fc Chimera (Catalog # 10378-UK) is immobilized at 1 μg/mL (100 μL/well), Recombinant Human u-Plasminogen Activator/Urokinase (Catalog # 1310-SE) binds with an ED50 of 2‑16 ng/mL.
2 μg/lane of Recombinant Human uPAR Fc Chimera (Catalog # 10378-UK) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

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Recombinant Human uPAR Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA.

When Recombinant Human uPAR Fc Chimera (Catalog # 10378-UK) is immobilized at 1 µg/mL (100 µL/well), Recombinant Human u-Plasminogen Activator (uPA)/Urokinase (Catalog # 1310-SE) binds with an ED50 of 2-16 ng/mL.

Source
Chinese Hamster Ovary cell line, CHO-derived human uPAR protein
Human uPAR
(Leu23-Arg303)
Accession # Q03405.1
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Leu23
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
58 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
74-85 kDa, under reducing conditions

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human uPAR Fc Chimera Protein, CF

  • CD87 antigen
  • CD87
  • Monocyte activation antigen Mo3
  • plasminogen activator, urokinase receptor
  • PLAUR
  • uPAR
  • U-PAR
  • UPARurokinase plasminogen activator surface receptor
  • u-plasminogen activator receptor form 2
  • URKRMO3

Background

uPAR (urokinase-type plasminogen activator receptor, also known as CD87), is a cell surface receptor that binds urokinase-type plasminogen activator (uPA) which cleaves the zymogen plasminogen to form the active enzyme plasmin. uPAR expression is activated during inflammation, immune responses, and conditions of tissue remodeling and wound healing (1). Human uPAR is synthesized as a 335 amino acid (aa) residue precursor protein with a 22 aa signal peptide. Removal of the C-terminal propeptide generates a fully processed uPAR containing 283 aa with five potential N-linked glycosylation sites and a C-terminal GPI-anchor site (2). Variants due to alternative splicing of uPAR also exist (3). Human and mouse uPAR share approximately 60% aa sequence identity and the receptor-ligand interaction is strictly species-specific (4). The uPA/uPAR interaction initiates signal transduction responses resulting in activation of protein tyrosine kinases, gene expression, cell adhesion, and chemotaxis. uPAR can interact with integrins to suppress normal integrin adhesive function and promote adhesion to vitronectin through a high affinity vitronectin binding site on uPAR. uPAR is considered as a biomarker in many inflammatory diseases including cancer, cardiovascular diseases, chronic kidney diseases and diabetes (5).
  1. Smith, H.W. and C.J. Marshall (2010) Nat. Rev. Mol. Cell Biol. 11:23.
  2. Ploug, M. et al. (1991) J. Biol. Chem. 266:1926.
  3. Dear, A.E. and R.L. Medcalf (1998) Eur. J. Biochemistry 252:185.
  4. Ellis, V. et al. (1992) Ann. N.Y. Acad. Sci. 667:13.
  5. Desmedt, S. et al. (2017) Crit. Rev. Clin. Lab. Sci. 54:117.

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