Recombinant Human Glycoprotein V/CD42d Protein, CF

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Recombinant Human Glycoprotein V/CD42d Protein, CF Summary

Product Specifications

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<1.0 EU per 1 μg of the protein by the LAL method.
Measured by its binding ability in a functional ELISA. When rhvWF-A2 (Catalog # 2764-WV) is coated at 1 μg/mL (100 μL/well), the concentration of rhGPV that produces 50% optimal binding response is found to be approximately 10-50 ng/mL. Measured by the ability of the immobilized protein to support the adhesion of thrombin-activated human platelets.

When 5 x 106 cells per well are added to rhGPV coated plates (5 μg/mL, 100 μL/well), approximately 50%-70% will adhere after 1 hour at 37 °C. 

Optimal dilutions should be determined by each laboratory for each application. 

Mouse myeloma cell line, NS0-derived human Glycoprotein V/CD42d protein
Gln17-Gly523, with a C-termninal 6-His tag
Accession #
N-terminal Sequence
No results obtained: Gln17 predicted
Predicted Molecular Mass
56 kDa
75-85 kDa, reducing conditions

Product Datasheets

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Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.


Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 500 μg/mL in PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.
Reconstitution Calculator

Reconstitution Calculator

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Background: Glycoprotein V/CD42d

GPV (platelet glycoprotein V; designated CD42d) is an 83 kDa type I transmembrane (TM) glycoprotein of the leucine-rich repeat (LRR) family (1, 2). It is expressed exclusively within the platelet / megakaryocyte lineage, where it noncovalently interacts with other platelet TM LRR proteins, GPIb alpha / beta and GPIX, at a ratio of one GPV to two of each other subunit (2). The GPI-V-IX complex tethers platelets to von Willebrand factor on the surface of injured endothelial cells. Absence of the complex results in Bernard-Soulier syndrome, a rare bleeding disorder (1 - 3). The human GPV cDNA encodes a 560 amino acid (aa) protein with a 16 aa signal sequence, a 507 aa extracellular domain (ECD) containing 15 LRR, a 21 aa TM sequence, and a short (16 aa) cytoplasmic tail that binds calmodulin in resting, but not activated platelets. The human GPV ECD shares 70%, 71% and 81% aa identity with mouse, rat and equine GPV, respectively. GPV can form soluble fragments of 80 kDa by ADAM10 or ADAM17 cleavage after P507, or 69 kDa by thrombin cleavage after R476 (1, 4, 5). High circulating soluble GPV may be an indicator of platelet activation, but may also be caused by high doses of aspirin (6 - 8). The function of GPV is not entirely clear. Deletion of GPV in mice does not produce any obvious change to surface expression or function of GPIb and GPIX, but surface expression of GPV requires GPIb (9, 10). Deletion studies also indicate that GPV may play a minor role in collagen adhesion, and may modify platelet aggregation in response to thrombin (3, 11 - 15).

  1. Lanza, F. et al. (1993) J. Biol. Chem. 268:20801.
  2. Hickey, M.J. et al. (1993) Proc. Natl. Acad. Sci. USA 90:8327.
  3. Ozaki, Y. et al. (2005) J. Thromb. Haemost. 3:1745.
  4. Rabie, T. et al. (2005) J. Biol. Chem. 280:14462.
  5. Gardiner, E.E. et al. (2007) J. Thromb. Haemost. 5:1530.
  6. Wolff, V. et al. (2005) Stroke 36:e17.
  7. Javela, K. et al. (2005) Transfusion 45:1504.
  8. Aktas, B. et al. (2005) J. Biol. Chem. 280:39716.
  9. Kahn, M.L. (1999) Blood 94:4112.
  10. Strassel, C. et al. (2004) Eur. J. Biochem. 271:3671.
  11. Nonne, C. et al. (2008) J. Thromb. Haemost. 6:210.
  12. Moog, S. et al. (2001) Blood 98:1038.
  13. Ramakrishnan, V. et al. (1999) Proc. Natl. Acad. Sci. USA 96:13336.
  14. Ni, H. et al. (2001) Blood 98:368.
  15. Andrews, R.K. et al. (2001) Blood 98:681.
Entrez Gene IDs
2814 (Human); 14729 (Mouse); 25259 (Rat)
Alternate Names
platelet glycoprotein V; CD42d; glycoprotein V (platelet); Glycoprotein V; GP5; GPV

Citation for Recombinant Human Glycoprotein V/CD42d Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

1 Citation: Showing 1 - 1

  1. Glycoprotein V is a relevant immune target in patients with immune thrombocytopenia
    Authors: R Vollenberg, R Jouni, PAA Norris, M Burg-Roder, N Cooper, MJ Rummel, G Bein, I Marini, B Bayat, R Burack, AH Lazarus, T Bakchoul, UJ Sachs
    Haematologica, 2019;0(0):.
    Species: Human
    Sample Types: Serum
    Applications: Surface Plasmon Resonance (SPR


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