Human EMMPRIN/CD147 Biotinylated Antibody

(2 citations)   
  • Species Reactivity
    Human
  • Specificity
    Detects human EMMPRIN/CD147 in Western blots. In Western blots, approximately 5% cross‑reactivity with recombinant mouse EMMPRIN is observed.
  • Source
    Polyclonal Goat IgG
  • Purification
    Antigen Affinity-purified
  • Immunogen
    Mouse myeloma cell line NS0-derived recombinant human EMMPRIN/CD147
    Thr25-His205
    Accession # Q54A51
  • Formulation
    Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
  • Label
    Biotin
Applications
  •  
    Recommended
    Concentration
    Sample
  • Western Blot
    0.1 µg/mL
    Recombinant Human EMMPRIN/CD147 Fc Chimera (Catalog # 972-EMN)
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Preparation and Storage
  • Reconstitution
    Reconstitute at 0.2 mg/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.
    • 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: EMMPRIN/CD147
Extracellular matrix metalloproteinase (MMP) inducer (EMMPRIN), also known as basigin and CD147, is a 44-66 kDa, variably 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) domain and a 41 aa intracellular domain. 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). mRNA transcripts, but not protein, have been reported for additional 432, 388, 205, 176, and 174 aa variants.

EMMPRIN is expressed in areas of tissue remodeling, including tumors, endometrium, placenta, skin, and regions undergoing angiogenesis (1, 2, 6-9). It is also expressed in cells with high metabolic activity, such as lymphoblasts, macrophages and tumor cells (2, 10). On cells with elevated metabolic rates, EMMPRIN is often co-expressed with the amino acid transporter CD98h (11). 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 (12). EMMPRIN’s TM sequence contains a Glu and a Pro which are important for intracellular interactions with cyclophilins (CyP) (3, 13, 14). CyPA (cyclosporin A receptor) and CyP60 interactions with the TM segment promote leukocyte inflammatory chemotaxis and surface expression of EMMPRIN, respectively (13, 14). 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 (15, 16). Functionally, EMMPRIN is known to induce urokinase-type plasminogen activator (uPA), VEGF, hyaluronan, and multiple MMPs (1, 2, 7, 8, 9). Human EMMPRIN (269 aa) shows 58%, 58%, 62%, and 52% aa identity with mouse, rat, bovine, and chicken EMMPRIN, respectively. It also shows 25% and 38% aa identity with the related proteins, embigin and neuroplastin (SDR-1), respectively (4).

  • References:
    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. Miyauchi, T. et al. (1991) J. Biochem. 110:770.
    5. Hanna, S.M. et al. (2003) BMC Biochem. 4:17.
    6. Riethdorf, S. et al. (2006) Int. J. Cancer 119:1800.
    7. Braundmeier, A.G. et al. (2006) J. Clin. Endocrinol. Metab. 91:2358.
    8. Tang, Y. et al. (2006) Mol. Cancer Res. 4:371.
    9. Quemener, C. et al. (2007) Cancer Res. 67:9.
    10. Wilson, M.C. et al. (2005) J. Biol. Chem. 280:27213.
    11. Xu, D. and M.E. Hemler (2005) Mol. Cell. Proteomics 4:1061.
    12. Tang, W. et al. (2004) Mol. Biol. Cell 15:4043.
    13. Arora, K. et al. (2005) J. Immunol. 175:517.
    14. Pushkarsky, T. et al. (2005) J. Biol. Chem. 280:27866.
    15. Egawa, N. et al. (2006) J. Biol. Chem. 281:37576.
    16. Sidhu, S.S. et al. (2004) Oncogene 23:956.
  • Long Name:
    Extracellular Matrix Metalloproteinase Inducer
  • Entrez Gene IDs:
    682 (Human); 12215 (Mouse)
  • 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
Related Research Areas
Citations:

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.

2 Citations: Showing 1 - 2
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Species
Applications
Sample Type
  1. Combined cell surface carbonic anhydrase 9 and CD147 antigens enable high-efficiency capture of circulating tumor cells in clear cell renal cell carcinoma patients
    Authors: S Liu, Z Tian, L Zhang, S Hou, S Hu, J Wu, Y Jing, H Sun, F Yu, L Zhao, R Wang, HR Tseng, HE Zhau, LW Chung, K Wu, H Wang, JB Wu, Y Nie, C Shao
    Oncotarget, 2016;7(37):59877-59891.
    Species: Human
    Sample Type: Plasma
    Application: Functional Assay
  2. Oxidized low-density lipoproteins stimulate extracellular matrix metalloproteinase Inducer (EMMPRIN) release by coronary smooth muscle cells.
    Authors: Haug C, Lenz C, Diaz F, Bachem MG
    Arterioscler. Thromb. Vasc. Biol., 2004;24(10):1823-9.
    Species: Human
    Sample Type: Cell Culture Supernates
    Application: ELISA Development
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