Recombinant Mouse CXCL4/PF4 Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

Order Details

Recombinant Mouse CXCL4/PF4 Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit the FGF basic-dependent proliferation of HUVEC human umbilical vein endothelial cells. Dubrac, A. et al. (2010) Blood 116:4703. The ED50 for this effect is 2-10 μg/mL.
Source
E. coli-derived mouse CXCL4/PF4 protein
Val30-Ser105
Accession #
N-terminal Sequence
Val30
Protein/Peptide Type
Recombinant Proteins
Gene
Pf4
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
8.2 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.
Publications
Read Publications using
595-P4 in the following applications:

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
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

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

Alternate Names for Recombinant Mouse CXCL4/PF4 Protein, CF

  • chemokine (C-X-C motif) ligand 4
  • C-X-C motif chemokine 4
  • CXCL4
  • CXCL4iroplact
  • Iroplact
  • MGC138298
  • Oncostatin-A
  • PF4
  • PF-4
  • platelet factor 4
  • SCYB4oncostatin-A

Background

CXCL4, also called PF4 (platelet factor 4), is an 8 kDa member of the CXC chemokine family, sharing features with CXCL8/IL-8 and CXCL7/NAP-2 (1-3). Mature mouse CXCL4 shares 76%, 88%, 64%, 64% and 63% amino acid sequence identity with human, rat, ovine, porcine and bovine CXCL4, respectively. The active protein is a tetramer of CXCL4 subunits that forms a ring of heparin-binding positive charges from sites at the C-terminal region of each monomer (3). Megakaryocytes synthesize CXCL4 and store it in platelet alpha -granules (2, 3). Secretion from activated platelets can produce micromolar levels in serum and over 100‑fold higher within clots (2, 3). In contrast to other CXC chemokines, CXCL4 does not contain an ELR motif and lacks binding to nearly all chemokine receptors (2, 3). A potential high-affinity G-protein-coupled receptor for CXCL4, the CXCR3 isoform CXCR3B, is expressed in human but not mouse (2, 3). In most cases, it is likely that cell surface binding and signaling properties of CXCL4 are due to binding of glycosaminoglycans chains, particularly chondroitin sulfates (2). CXCL4 released from activated platelets binds and regulates thrombin/thrombomodulin complexes, regulates and enhances production of activated Protein C (APC), and limits the coagulation cascade (2-6). It binds and influences the enzymatic activity of coagulation factor Xa (7). It binds fibrin and affects clot structure (8). Therapeutic doses of the anticoagulant heparin neutralize CXCL4 procoagulant effects (9). The complex between heparin and CXCL4 can be immunogenic, and circulating CXCL4-heparin antibodies cause the human syndrome HITT (heparin-induced thrombocytopenia and thrombosis, also called HIT) (2). In addition, immunogenic complexes of CXCL4 with apolipoprotein H can contribute to antiphospholipid syndrome (APS) (10). CXCL4 can be antiproliferative and antiangiogenic, at least in part via interfering with FGF-2 and VEGF heparin binding and thus inhibiting their signaling (3, 11-13). However, it can also be proinflammatory and pro‑atherogenic through multiple effects on monocytes, macrophages and endothelial cells (2, 3).

  1. Poncz, M. et al. (1987) Blood 69:219.
  2. Kowalska, M.A. et al. (2010) Thromb. Res. 125:292.
  3. Slungaard, A. (2005) Int. J. Biochem. Cell Biol. 37:1162.
  4. Slungaard, A. et al. (2003) Blood 102:146.
  5. Kowalska, M.A. et al. (2007) Blood 110:1903.
  6. Preston, R.J.S. et al. (2009) J. Biol. Chem. 284:5869.
  7. Fiore, M.M. and I.J. Mackie (2009) Biochem. Biophys. Res. Commun. 379:1072.
  8. Amelot, A.A. et al. (2007) J. Biol. Chem. 282:710.
  9. Eslin, D.E. et al. (2004) Blood 104:3173.
  10. Sikara, M.P. et al. (2010) Blood 115:713.
  11. Perollet, C. et al. (1998) Blood 91:3289.
  12. Gengrinovitch, S. et al. (1995) Journal of Biological Chemistry 270:15059.
  13. Sulpice, E. et al. (2004) Eur. J. Biochem. 271:3310.

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Publications for CXCL4/PF4 (595-P4)(5)

We have publications tested in 1 confirmed species: Mouse.

We have publications tested in 2 applications: Binding Assay, Bioassay.


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Bioinformatics

Gene Symbol Pf4
Uniprot