Recombinant Human GPVI Fc Chimera Protein, CF

When Bovine Collagen I is immobilized at 10 μg/mL (100 μL/well), Recombinant Human GPVI Fc Chimera (10452-GP) binds with an ED50 of 0.04-0.36 μg/mL.

2 μg/lane of Recombinant Human GPVI Fc Chimera Protein (Catalog # 10452-GP) was resolved withSDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized byCoomassie® Blue staining, showing bands at kDa.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human GPVI Fc Chimera Protein, CF Summary

• Additional Information: HEK293 Expressed
• Details of Functionality: Measured by its binding ability in a functional ELISA. When Bovine Collagen I is immobilized at 10 µg/mL (100 μL/well), Recombinant Human GPVI Fc Chimera (Catalog # 10452-GP) binds with an ED₅₀ of 0.04-0.36 μg/mL.
• Source: Human embryonic kidney cell, HEK293-derived human GPVI protein
  

  Human GPVI (Gln21-Lys267) Accession # Q9HCN6.4	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: Q9HCN6.4
• N-terminal Sequence: Gln21
• 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: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 54 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: 68-76 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 with Trehalose.
• 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 GPVI Fc Chimera Protein, CF

• Glycoprotein 6
• glycoprotein VI (platelet)
• GP6
• GPIV
• GPVI
• GPVIplatelet collagen receptor
• MGC138168
• platelet glycoprotein VI

Background

Glycoprotein VI (GPVI) is a 63 kDa platelet/megakaryocyte-specific type I transmembrane glycoprotein of the immunoglobulin superfamily that is an important collagen receptor and initiator of platelet activation, aggregation and thrombin generation (1, 2). GPVI is also a secondary receptor required for platelet spreading on laminin (3). Human GPVI contains a 20 amino acid (aa) signal sequence, a 247 aa extracellular domain (ECD) that has two C-type Ig-like domains followed by a mucin-like, presumably O-glycosylated Ser-Thr-rich region, a 21 aa transmembrane (TM) domain and a 51 aa cytoplasmic tail that contains calmodulin-binding and SH3 domains. Human GPVI ECD shows 69%, 65% and 70% aa identity with mouse, bovine and canine GPVI ECD, respectively. Two splice variants exist; one is 17 aa shorter in the ECD, while the other diverges at aa 260, creating an inactive monomeric and presumably secreted 681 aa protein (3).GPVI associates with the FcR gamma via charged amino acid in the TM domains of GPVI (arginine) and the FcR gamma (aspartic acid) (2). Collagen binding by the GPVI Ig-like domains initiates signaling through the FcR gamma ITAM sequence (2). Dimerization of GPVI (2:2 with FcR gamma ) and N-glycosylation greatly enhances collagen binding (5, 6). Type I and III collagens are strong thrombus-forming components in the vascular subendothelium and atherosclerotic plaques (7). GPVI initiates binding to fibrillar collagens under flow conditions, then activates integrin alpha 2 beta 1 which binds collagen more tightly (8). GPVI deficiencies cause only a mild bleeding tendency, probably because integrin alpha 2 beta 1 is able to minimally initiate collagen binding (8). Normal human GPVI concentration can vary widely and affect maximum thrombin generation (9). Engagement of GPVI by collagens or other agonists, including autoantibodies, causes calmodulin-regulated metalloproteinase cleavage of the 57 kDa ECD and depletes surface GPVI (10).

1. Jandrot-Perrus, M. et al. (2000) Blood 96:1798.
2. Moroi, M. and S. M. Jung (2004) Thromb. Res. 114:221.
3. Inoue, O. et al. (2006) Blood 107:1405.
4. Ezumi, Y. et al. (2000) Biochem. Biophys. Res. Comm. 277:27.
5. Horii, K. et al. (2006) Blood 108:936.
6. Kunicki, T. J. et al. (2005) Blood 106:2744.
7. Cosemans, J. M. et al. (2005) Atherosclerosis 181:19.
8. Lecut, C. et al. (2005) Thromb. Haemost. 94:107.
9. Furihata, K. et al. (2001) Arterioscler. Thromb. Vasc. Biol. 21:1857.
10. Stephens, G. et al. (2005) Blood 105:186.

Bioinformatics

• Uniprot:
  • Q9HCN6.4()