Human EMMPRIN/CD147 Biotinylated Antibody

Catalog # Availability Size / Price Qty
BAF972
Product Details
Citations (2)
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Human EMMPRIN/CD147 Biotinylated Antibody Summary

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.

Reconstitution Calculator

Reconstitution Calculator

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Preparation and Storage

Reconstitution
Reconstitute at 0.2 mg/mL in sterile PBS.
Reconstitution Buffer Available
Reconstitution Buffer 1 (PBS)
Catalog #
Availability
Size / Price
Qty
RB01
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

Product Datasheets

Citations for Human EMMPRIN/CD147 Biotinylated Antibody

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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  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 Types: Plasma
    Applications: 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 Types: Cell Culture Supernates
    Applications: ELISA Development

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