Recombinant Human EMMPRIN/CD147 Fc Chimera (NS0) Protein, CF

Isoform 2. aa 22-205
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Recombinant Human EMMPRIN/CD147 Fc Chimera (NS0) Protein Binding Activity
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Citations (3)
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Recombinant Human EMMPRIN/CD147 Fc Chimera (NS0) Protein, CF Summary

Product Specifications

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by the ability of the immobilized protein to induce active MMP-1 secretion by NHLF human normal lung fibroblasts. The ED50 for this effect is 2‑8 µg/mL. Measured by its binding ability in a functional ELISA with Recombinant SARS-CoV-2 Spike RBD Fc Chimera (Catalog # 10499-CV).
Mouse myeloma cell line, NS0-derived human EMMPRIN/CD147 protein
Accession # NP_001309172.1
6-His tag
N-terminus C-terminus
Accession #
N-terminal Sequence
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
47.4 kDa (monomer)
60 - 65 kDa, under reducing conditions.

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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 with Trehalose.
Reconstitution Reconstitute at 100 μg/mL in sterile 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.

Data Image

Binding Activity Recombinant Human EMMPRIN/CD147 Fc Chimera (NS0) Protein Binding Activity View Larger

Recombinant Human EMMPRIN/CD147 Fc Chimera (972-EMN) binds Recombinant SARS-CoV-2 Spike RBD Fc Chimera (10499-CV) in a functional ELISA.

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Background: EMMPRIN/CD147

Extracellular matrix metalloproteinase (MMP) inducer (EMMPRIN), also known as basigin and CD147, is a 44‑66 kDa, variably N‑ and O‑glycosylated, type I transmembrane protein that belongs to the immunoglobulin superfamily (1‑4). Human EMMPRIN is 269 amino acids (aa) in length and contains a 24 aa signal sequence, a 183 aa extracellular domain (ECD), a 21 aa transmembrane (TM) segment and a 41 aa cytoplasmic tail. The ECD contains one C2‑type and one V‑type Ig‑like domain. There is one 385 aa splice variant that contains an extra N‑terminal IgCAM domain and is found only in the retina (5). There are additional multiple potential isoform variants for EMMMPRIN. Two that have been characterized are 205 and 176 aa in length. The 176 aa isoform utilizes an alternative start site at Met94, while the 205 aa isoform contains an 11 aa substitution for aa 1‑75. Notably, the 176 aa isoform heterodimerizes with the standard EMMPRIN isoform and down‑modulates its activity. This is in contrast to EMMPRIN homodimers that show full biological activity (6). EMMPRIN is expressed in areas of tissue remodeling, including endometrium, placenta, skin, and regions undergoing angiogenesis (1, 2, 7‑10). It is also expressed on cells with high metabolic activity, such as lymphoblasts, macrophages and particularly tumor cells (2, 11). On such cells, EMMPRIN is often co‑expressed with the amino acid transporter CD98h (12). EMMPRIN also interacts with caveolin-1 (via its C2‑like domain), and this reduces the level of EMMPRIN glycosylation and subsequent EMMPRIN multimerization and activity (13). In addition, EMMMPRIN is reported to complex with both annexin II and beta 1 integrins alpha 3 and alpha 6, an interaction that contributes to tumor growth and metastasis (14‑16). Finally, the soluble calcium‑binding protein S100A9 has now been identified as a ligand for EMMPRIN, and may mediate many of the tumorigenic activities attributed to EMMPRIN (17). EMMPRIN’s TM sequence contains a charged aa (Glu), and a Pro important for intracellular interactions with cyclophilins (CyP) (3, 18, 19). CyPA (cyclosporin A receptor) and CyP60 interactions with the TM segment promote leukocyte inflammatory chemotaxis and surface expression of EMMPRIN, respectively (18, 19). An active 22 kDa fragment can be shed from tumor cells by MT1‑MMP (1). Tumor cells can also release active, full‑length EMMPRIN in microvesicles (20, 21). Functionally, EMMPRIN is known to induce urokinase‑type plasminogen activator (uPA), VEGF, hyaluronan and multiple MMPs (1, 2, 8‑10). Human EMMPRIN (269 aa) shows 58%, 58%, 62% and 52% aa identity with mouse, rat, cow and chick EMMPRIN, respectively. It also shows 25% and 38% aa identity with the related proteins, embigin and neuroplastin (SDR‑1), respectively.

  1. Gabison, E. E. et al. (2005) Biochimie 87:361.
  2. Yurchenko, V. et al. (2006) Immunology 117:301.
  3. Kasinrerk, W. et al. (1992) J. Immunol. 149:847.
  4. Iacono, K.T. et al. (2007) Exp. Mol. Pathol. 83:283.
  5. Hanna, S. M. et al. (2003) BMC Biochem. 4:17.
  6. Liao, C-G. et al. (2011) Mol. Cell. Biol. 31:2591.
  7. Riethdorf, S. et al. (2006) Int. J. Cancer 119:1800.
  8. Braundmeier, A. G. et al. (2006) J. Clin. Endocrinol. Metab. 91:2358.
  9. Tang, Y. et al. (2006) Mol. Cancer Res. 4:371.
  10. Quemener, C. et al. (2007) Cancer Res. 67:9.
  11. Wilson, M. C. et al. (2005) J. Biol. Chem. 280:27213.
  12. Xu, D. and M. E. Hemler, (2005) Mol. Cell. Proteomics 4:1061.
  13. Tang, W. et al. (2004) Mol. Biol. Cell 15:4043.
  14. Zhao, P. et al. (2010) Cancer Sci. 101:387.
  15. Dai, J. et al. (2009) BMC Cancer 9:337.
  16. Li, Y. et al. (2012) J. Biol. Chem. 287:4759.
  17. Hibino, T. et al. (2013) Cancer Res. 73:172.
  18. Arora, K. et al. (2005) J. Immunol. 175:517.
  19. Pushkarsky, T. et al. (2005) J. Biol. Chem. 280:27866.
  20. Egawa, N. et al. (2006) J. Biol. Chem. 281:37576.
  21. Sidhu, S. S. et al. (2004) Oncogene 23:956.
Long Name
Extracellular Matrix Metalloproteinase Inducer
Entrez Gene IDs
682 (Human); 12215 (Mouse); 102121721 (Cynomolgus Monkey)
Alternate Names
5F7; basigin (Ok blood group); Basigin; BSG; CD147 antigen; CD147; Collagenase stimulatory factor; EMMPRIN; EMMPRINTCSF; Extracellular matrix metalloproteinase inducer; Leukocyte activation antigen M6; M6; OK blood group antigen; OK; Tumor cell-derived collagenase stimulatory factor

Citations for Recombinant Human EMMPRIN/CD147 Fc Chimera (NS0) 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.

3 Citations: Showing 1 - 3
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  1. Proximity ligation assays for precise quantification of femtomolar proteins in single cells using self-priming microfluidic dPCR chip
    Authors: J Hu, T Gou, W Wu, J Sun, S Zhang, S Zhou, J Yin, Y Mu
    Anal. Chim. Acta, 2019;1076(0):118-124.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. EMMPRIN Inhibits bFGF-Induced IL-6 Secretion in an Osteoblastic Cell Line, MC3T3-E1
    Authors: A Saiki, M Motoyoshi, K Motozawa, T Okamura, K Ueki, N Shimizu, M Asano
    Int J Med Sci, 2017;14(12):1173-1180.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Resveratrol blocks interleukin-18-EMMPRIN cross-regulation and smooth muscle cell migration.
    Authors: Venkatesan B, Valente AJ, Reddy VS, Siwik DA, Chandrasekar B
    Am. J. Physiol. Heart Circ. Physiol., 2009;297(2):H874-86.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay


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