Recombinant Human EMMPRIN/CD147 (aa 138-323) His Protein, CF Summary
Additional Information |
Isoform 1, HEK293 Expressed |
Details of Functionality |
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 0.70-5.60 μg/mL. |
Source |
Human embryonic kidney cell, HEK293-derived human EMMPRIN/CD147 protein Glu138-Ala323, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Glu138 |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
21 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. |
SDS-PAGE |
25-41 kDa, under reducing conditions |
Packaging, Storage & Formulations
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.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human EMMPRIN/CD147 (aa 138-323) His Protein, CF
Background
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.
SARS-CoV-2 invades host cells via two receptors: angiotensin-converting
enzyme 2 (ACE2) and EMMPRIN. Spike protein (SP) from virus binds to ACE2 or EMMPRIN
on the host cell, mediating viral invasion and dissemination of virus among other
cells (22). EMMPRIN is a second entry receptor for SARS-CoV-2 (22). It is
present in multiple cellular types in lung and highly expressed in type II pneumocytes
and macrophages at the edges of the fibrotic zones (22). Therefore, the
blockade of EMMPRIN could also play a beneficial role in pulmonary fibrosis due
to COVID-19 (22).
- Gabison, E. E. et al. (2005) Biochimie 87:361.
- Yurchenko, V. et al. (2006) Immunology 117:301.
- Kasinrerk, W. et al. (1992) J. Immunol. 149:847.
- Iacono, K.T. et al. (2007) Exp. Mol. Pathol. 83:283.
- Hanna, S. M. et al. (2003) BMC Biochem. 4:17.
- Liao, C-G. et al. (2011) Mol. Cell. Biol. 31:2591.
- Riethdorf, S. et al. (2006) Int. J. Cancer 119:1800.
- Braundmeier, A. G. et al. (2006) J. Clin. Endocrinol. Metab. 91:2358.
- Tang, Y. et al. (2006) Mol. Cancer Res. 4:371.
- Quemener, C. et al. (2007) Cancer Res. 67:9.
- Wilson, M. C. et al. (2005) J. Biol. Chem. 280:27213.
- Xu, D. and M. E. Hemler, (2005) Mol. Cell. Proteomics 4:1061.
- Tang, W. et al. (2004) Mol. Biol. Cell 15:4043.
- Zhao, P. et al. (2010) Cancer Sci. 101:387.
- Dai, J. et al. (2009) BMC Cancer 9:337.
- Li, Y. et al. (2012) J. Biol. Chem. 287:4759.
- Hibino, T. et al. (2013) Cancer Res. 73:172.
- Arora, K. et al. (2005) J. Immunol. 175:517.
- Pushkarsky, T. et al. (2005) J. Biol. Chem. 280:27866.
- Egawa, N. et al. (2006) J. Biol. Chem. 281:37576.
- Sidhu, S. S. et al. (2004) Oncogene 23:956.
- Ulrich, H. et al. (2020) Stem Cell Rev. and Rep., https://doi.org/10.1007/s12015-020-09976-7.
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