Recombinant Human CXCL4/PF4 Protein


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Applications Bioactivity

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Recombinant Human CXCL4/PF4 Protein 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 typically 2-10 µg/mL.
E. coli-derived human CXCL4/PF4 protein
Accession #
N-terminal Sequence
Protein/Peptide Type
Recombinant Proteins
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.


Theoretical MW
7.8 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.
Read Publications using
795-P4 in the following applications:

Packaging, Storage & Formulations

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.
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein.
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 250 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.


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

Alternate Names for Recombinant Human CXCL4/PF4 Protein

  • 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


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 human CXCL4 shares 65-76% amino acid sequence identity with mouse, rat, bovine, ovine and porcine CXCL4. 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 pathological 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 (795-P4)(12)

We have publications tested in 3 confirmed species: Human, Mouse, Virus.

We have publications tested in 3 applications: Binding Assay, Bioassay, Flow Cytometry Control.

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Showing Publications 1 - 10 of 12. Show All 12 Publications.
Publications using 795-P4 Applications Species
A Ojha, A Bhasym, S Mukherjee, GK Annarapu, T Bhakuni, I Akbar, T Seth, NK Vikram, S Vrati, A Basu, S Bhattachar, P Guchhait Platelet factor 4 promotes rapid replication and propagation of Dengue and Japanese encephalitis viruses EBioMedicine, 2019;39(0):332-347. 2019 [PMID: 30527622] (Bioassay, Human) Bioassay Human
C Daly, X Qian, C Castanaro, E Pasnikowsk, X Jiang, BR Thomson, SE Quaggin, N Papadopoul, Y Wei, JS Rudge, G Thurston, GD Yancopoulo, S Davis Angiopoietins bind thrombomodulin and inhibit its function as a thrombin cofactor Sci Rep, 2018;8(1):505. 2018 [PMID: 29323190] (Bioassay, Human) Bioassay Human
B Schludi, ASM Moin, C Montemurro, T Gurlo, AV Matveyenko, D Kirakossia, DW Dawson, SM Dry, PC Butler, AE Butler Islet inflammation and ductal proliferation may be linked to increased pancreatitis risk in type 2 diabetes JCI Insight, 2017;2(13):. 2017 [PMID: 28679961] (Bioassay, Human) Bioassay Human
H Bronger, A Karge, T Dreyer, D Zech, S Kraeft, S Avril, M Kiechle, M Schmitt Induction of cathepsin B by the CXCR3 chemokines CXCL9 and CXCL10 in human breast cancer cells Oncol Lett, 2017;13(6):4224-4230. 2017 [PMID: 28599423] (Bioassay, Human) Bioassay Human
RK Schneider, A Mullally, A Dugourd, F Peisker, R Hoogenboez, PMH Van Strien, EM Bindels, D Heckl, G Büsche, D Fleck, G Müller-New, J Wongboonsi, M Ventura Fe, VG Puelles, J Saez-Rodri, BL Ebert, BD Humphreys, R Kramann Gli1(+) Mesenchymal Stromal Cells Are a Key Driver of Bone Marrow Fibrosis and an Important Cellular Therapeutic Target Cell Stem Cell, 2017;0(0):. 2017 [PMID: 28457748] (Bioassay, Mouse) Bioassay Mouse
Ollivier V, Syvannarath V, Gros A, Butt A, Loyau S, Jandrot-Perrus M, Ho-Tin-Noe B Collagen can selectively trigger a platelet secretory phenotype via glycoprotein VI. PLoS ONE, 2014;9(8):e104712. 2014 [PMID: 25116206] (Flow Cytometry Control, Human) Flow Cytometry Control Human
Guzzo C, Fox J, Lin Y, Miao H, Cimbro R, Volkman B, Fauci A, Lusso P The CD8-derived chemokine XCL1/lymphotactin is a conformation-dependent, broad-spectrum inhibitor of HIV-1. PLoS Pathog, 2013;9(12):e1003852. 2013 [PMID: 24385911] (Bioassay, Human) Bioassay Human
Balan M, Pal S A novel CXCR3-B chemokine receptor-induced growth-inhibitory signal in cancer cells is mediated through the regulation of Bach-1 protein and Nrf2 protein nuclear translocation. J Biol Chem, 2014;289(6):3126-37. 2014 [PMID: 24366869] (Bioassay, Human) Bioassay Human
Wilson TR, Fridlyand J, Yan Y, Penuel E, Burton L, Chan E, Peng J, Lin E, Wang Y, Sosman J, Ribas A, Li J, Moffat J, Sutherlin DP, Koeppen H, Merchant M, Neve R, Settleman J Widespread potential for growth-factor-driven resistance to anticancer kinase inhibitors. Nature, 2012;487(7408):505-9. 2012 [PMID: 22763448] (Bioassay, Human) Bioassay Human
Zhu Y, Vergote D, Pardo C, Noorbakhsh F, McArthur JC, Hollenberg MD, Overall CM, Power C CXCR3 activation by lentivirus infection suppresses neuronal autophagy: neuroprotective effects of antiretroviral therapy. FASEB J., 2009;23(9):2928-41. 2009 [PMID: 19380511] (Bioassay, Human) Bioassay Human
Show All 12 Publications.

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Gene Symbol PF4