ELISA with Human EMMPRIN/CD147 Protein 3607

Human EMMPRIN/CD147 Protein 3607

$240.00 – $800.00

Summary

Expression: HEK293
Functional: Yes (ELISA)
Amino Acid Range: Ala22-His205

SKU: 3607parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	NP_940991
express system	HEK293
product tag	C-His
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	CD147, also known as extracellular matrix metalloproteinase inducer (EMMPRIN) or basigin, is expressed in a variety of cell types. It is involved in the regulation of extracellular matrix (ECM) remodeling during physiological and pathological processes including wound healing, inflammatory diseases, and cancer. CD147 is a diagnostic and therapeutic target in cancer and inflammatory diseases, either directly or indirectly, by targeting CD147 partners.
molecular weight	The protein has a predicted MW of 21.2 kDa. Due to glycosylation, the protein migrates to 28-40 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Human EMMPRIN/CD147 Protein 3607

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
CD147, also known as extracellular matrix metalloproteinase inducer (EMMPRIN) or basigin, is expressed in a variety of cell types. It is involved in the regulation of extracellular matrix (ECM) remodeling during physiological and pathological processes including wound healing, inflammatory diseases, and cancer. CD147 is a diagnostic and therapeutic target in cancer and inflammatory diseases, either directly or indirectly, by targeting CD147 partners.
Protein names Peptidyl-prolyl cis-trans isomerase A (PPIase A) (EC 5.2.1.8) (Cyclophilin A) (Cyclosporin A-binding protein) (Rotamase A) [Cleaved into: Peptidyl-prolyl cis-trans isomerase A, N-terminally processed]
Protein family Cyclophilin-type PPIase family, PPIase A subfamily
Mass 18012Da
Function Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (PubMed:2001362, PubMed:20676357, PubMed:21245143, PubMed:21593166, PubMed:25678563). Exerts a strong chemotactic effect on leukocytes partly through activation of one of its membrane receptors BSG/CD147, initiating a signaling cascade that culminates in MAPK/ERK activation (PubMed:11943775, PubMed:21245143). Activates endothelial cells (ECs) in a pro-inflammatory manner by stimulating activation of NF-kappa-B and ERK, JNK and p38 MAP-kinases and by inducing expression of adhesion molecules including SELE and VCAM1 (PubMed:15130913). Induces apoptosis in ECs by promoting the FOXO1-dependent expression of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (PubMed:31063815). In response to oxidative stress, initiates proapoptotic and antiapoptotic signaling in ECs via activation of NF-kappa-B and AKT1 and up-regulation of antiapoptotic protein BCL2 (PubMed:23180369). Negatively regulates MAP3K5/ASK1 kinase activity, autophosphorylation and oxidative stress-induced apoptosis mediated by MAP3K5/ASK1 (PubMed:26095851). Necessary for the assembly of TARDBP in heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and regulates TARDBP binding to RNA UG repeats and TARDBP-dependent expression of HDAC6, ATG7 and VCP which are involved in clearance of protein aggregates (PubMed:25678563). Plays an important role in platelet activation and aggregation (By similarity). Regulates calcium mobilization and integrin ITGA2B:ITGB3 bidirectional signaling via increased ROS production as well as by facilitating the interaction between integrin and the cell cytoskeleton (By similarity). Binds heparan sulfate glycosaminoglycans (PubMed:11943775). Inhibits replication of influenza A virus (IAV) (PubMed:19207730). Inhibits ITCH/AIP4-mediated ubiquitination of matrix protein 1 (M1) of IAV by impairing the interaction of ITCH/AIP4 with M1, followed by the suppression of the nuclear export of M1, and finally reduction of the replication of IAV (PubMed:22347431, PubMed:30328013). {ECO:0000250\|UniProtKB:P17742, ECO:0000269\|PubMed:11943775, ECO:0000269\|PubMed:15130913, ECO:0000269\|PubMed:19207730, ECO:0000269\|PubMed:2001362, ECO:0000269\|PubMed:20676357, ECO:0000269\|PubMed:21245143, ECO:0000269\|PubMed:21593166, ECO:0000269\|PubMed:22347431, ECO:0000269\|PubMed:23180369, ECO:0000269\|PubMed:25678563, ECO:0000269\|PubMed:26095851, ECO:0000269\|PubMed:30328013, ECO:0000269\|PubMed:31063815}.; (Microbial infection) May act as a mediator between human SARS coronavirus nucleoprotein and BSG/CD147 in the process of invasion of host cells by the virus (PubMed:15688292). {ECO:0000269\|PubMed:15688292}.; (Microbial infection) Stimulates RNA-binding ability of HCV NS5A in a peptidyl-prolyl cis-trans isomerase activity-dependent manner. {ECO:0000269\|PubMed:21593166}.
Catalytic activity CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000269\|PubMed:2001362, ECO:0000269\|PubMed:20676357, ECO:0000269\|PubMed:21245143, ECO:0000269\|PubMed:21593166, ECO:0000269\|PubMed:25678563, ECO:0000305\|PubMed:19207730, ECO:0000305\|PubMed:26095851};
Subellular location Cytoplasm {ECO:0000269\|PubMed:26095851}. Secreted {ECO:0000269\|PubMed:16527992}. Nucleus {ECO:0000269\|PubMed:25678563}. Note=Secretion occurs in response to oxidative stress in vascular smooth muscle through a vesicular secretory pathway that includes Rho GTPase signaling, actin remodeling, and myosin II activation. {ECO:0000269\|PubMed:16527992}.
Structure Interacts with protein phosphatase PPP3CA/calcineurin A (PubMed:12218175, PubMed:12357034). Interacts with PRPF19 isoform 2 (via N-terminus) (By similarity). Interacts with isoform 2 of BSG/CD147 (PubMed:11353871, PubMed:11943775, PubMed:15688292, PubMed:21245143). Interacts with FOXO1; the interaction promotes FOXO1 dephosphorylation, nuclear accumulation and transcriptional activity (PubMed:31063815). Interacts with integrin ITGA2B:ITGB3; the interaction is ROS and peptidyl-prolyl cis-trans isomerase (PPIase) activity-dependent and is increased in the presence of thrombin (By similarity). Interacts with MAP3K5 (PubMed:26095851). Interacts with TARDBP; the interaction is dependent on the RNA-binding activity of TARDBP and the PPIase activity of PPIA/CYPA and the acetylation of PPIA/CYPA at Lys-125 favors the interaction (PubMed:25678563). Interacts with HNRNPA1, HNRNPA2B1, HNRNPC, RBMX, HNRNPK and HNRNPM (PubMed:25678563). {ECO:0000250\|UniProtKB:P17742, ECO:0000269\|PubMed:11353871, ECO:0000269\|PubMed:11943775, ECO:0000269\|PubMed:12218175, ECO:0000269\|PubMed:12357034, ECO:0000269\|PubMed:15688292, ECO:0000269\|PubMed:21245143, ECO:0000269\|PubMed:25678563, ECO:0000269\|PubMed:26095851, ECO:0000269\|PubMed:31063815}.; (Microbial infection) Interacts with HIV-1 capsid protein (PubMed:20364129, PubMed:8513493). {ECO:0000269\|PubMed:20364129, ECO:0000269\|PubMed:8513493}.; (Microbial infection) Interacts with human SARS coronavirus nucleoprotein. {ECO:0000269\|PubMed:15688292}.; (Microbial infection) Interacts with measles virus nucleoprotein. {ECO:0000269\|PubMed:20147391}.; (Microbial infection) Interacts with influenza A virus matrix protein 1. {ECO:0000269\|PubMed:19207730}.; (Microbial infection) Interacts with HCV NS5A; the interaction stimulates RNA-binding ability of NS5A and is dependent on the peptidyl-prolyl cis-trans isomerase activity of PPIA/CYPA. {ECO:0000269\|PubMed:21593166}.
Post-translational modification Acetylation at Lys-125 markedly inhibits catalysis of cis to trans isomerization and stabilizes cis rather than trans forms of the HIV-1 capsid. PPIA acetylation also antagonizes the immunosuppressive effects of cyclosporine by inhibiting the sequential steps of cyclosporine binding and calcineurin inhibition (PubMed:20364129, Ref.12). Acetylation at Lys-125 favors its interaction with TARDBP (PubMed:25678563). {ECO:0000269\|PubMed:20364129, ECO:0000269\|PubMed:25678563, ECO:0000269\|Ref.12}.
Target Relevance information above includes information from UniProt accession: P62937
The UniProt Consortium

Data

Immobilized Human EMMPRIN, His Tag at 0.5µg/ml (100µl/Well) on the plate. Dose response curve for Anti-EMMPRIN Antibody, hFc Tag with the EC50 of 8.4ng/ml determined by ELISA.

The purity of Human EMMPRIN is greater than 95% as determined by SEC-HPLC.

SDS-PAGE gel of Human EMMPRIN/CD147 Protein

Human EMMPRIN on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.