Recombinant Cynomolgus/Rhesus EMMPRIN/CD147 Fc Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 10797-EM

aa 138-327
R&D Systems, part of Bio-Techne
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Key Product Details

Source

CHO

Accession #

XP_005587353.1

Structure / Form

Disulfide-linked homodimer

Conjugate

Unconjugated

Applications

Bioactivity

View all EMMPRIN/CD147 Proteins and Enzymes »

Product Specifications

Source

Chinese Hamster Ovary cell line, CHO-derived EMMPRIN/CD147 protein
Cynomolgus/Rhesus EMMPRIN/CD147
(Glu138-Ala327)
Accession # XP_005587353.1		 IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus

Purity

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Glu138

Predicted Molecular Mass

47 kDa

SDS-PAGE

63 - 72 kDa, under reducing conditions.

Activity

Measured by its binding ability in a functional ELISA.
When Recombinant SARS-CoV-2 Spike RBD Fc Chimera  (Catalog # 10499-CV) is immobilized at 1 µg/mL (100 µL/well), Recombinant Cynomolgus Monkey EMMPRIN/CD147 Fc Chimera (Catalog # 10797-EM) binds with an ED50 of 1.50-12.0 µg/mL.

Scientific Data Images for Recombinant Cynomolgus/Rhesus EMMPRIN/CD147 Fc Protein, CF

Recombinant Cynomolgus Monkey EMMPRIN/CD147 Fc Chimera Protein Binding Activity.

When Recombinant SARS-CoV-2 Spike RBD Fc Chimera (10499-CV) is immobilized at 1 µg/mL (100 µL/well), Recombinant Cynomolgus Monkey EMMPRIN/CD147 Fc Chimera (Catalog # 10797-EM) binds with an ED50 of 1.50-12.0 µg/mL.

Recombinant Cynomolgus Monkey EMMPRIN/CD147 Fc Chimera Protein SDS-PAGE.

2 μg/lane of Recombinant Cynomolgus Monkey EMMPRIN/CD147 Fc Chimera Protein (Catalog # 10797-EM) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 63-72 kDa and 120-140 kDa, respectively.

Formulation, Preparation and Storage

10797-EM
Formulation Supplied as a 0.2 μm filtered solution in PBS with Trehalose.
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 2 weeks, 2 to 8 °C under sterile conditions after opening.
  • 3 months, -20 to -70 °C under sterile conditions after opening.

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). Based on its high homology with human EMMPRIN, cynomolgus EMMPRIN is predicted to  contain a 24 aa signal sequence, a 190 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 human 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 beta1 integrins alpha3 and alpha6, 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). Cynomolgus EMMPRIN (269 aa) shows 78% aa identity with human EMMPRIN. 

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. 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

Alternate Names

Basigin, BSG, CD147

Entrez Gene IDs

682 (Human); 12215 (Mouse); 102121721 (Cynomolgus Monkey)

Gene Symbol

BSG

UniProt

XP_005587353.1

Additional EMMPRIN/CD147 Products

Product Documents for Recombinant Cynomolgus/Rhesus EMMPRIN/CD147 Fc Protein, CF

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