Emmprin, Fc Chimera, Recombinant, Human (Extracellular Matrix Metalloproteinase (MMP) Inducer)
Catalog No : USB-E2260-04
740.25€
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| Product name | Emmprin, Fc Chimera, Recombinant, Human (Extracellular Matrix Metalloproteinase (MMP) Inducer) | ||
|---|---|---|---|
| Catalog No | USB-E2260-04 | ||
| Supplier’s Catalog No | E2260-04 | ||
| Supplier | US Biologicals | ||
| Source antigen | Recombinant, Mouse myeloma cell line, NS0 | ||
| Reactivity | |||
| Cross reactivity | |||
| Applications | |||
| Molecular weight | |||
| Storage | -20°C | ||
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| Other names | |||
| Grade | Highly Purified | ||
| Purity | ≥ 95%, as determined by SDS-PAGE and visualized by silver stain. | ||
| Form | Supplied as a lyophilized powder in PBS. | ||
| Reactivity life | 6 months | ||
| Note | For reserch purpose only | ||
| Purity | ≥ 95%, as determined by SDS-PAGE and visualized by silver stain. | ||
| Description | Extracellular matrix metalloproteinase (MMP) inducer (EMMPRIN), also known as basigin and CD147, is a 44-66kD, 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 kD 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, cow, and chicken EMMPRIN, respectively. It also shows 25% and 38% aa identity with the related proteins, embigin and neuroplastin (SDR-1), respectively (4). Source: Human Signal Peptide (Met 1-Met 17), Human EMMPRIN, (Ala 22-His 205), DIEGRMD, Human IgG1, (Pro 100-Lys 330), HHHHHH; A DNA sequence encoding the extracellular domain of human EMMPRIN (amino acid residues 22-205; Accession # P35613) (Kasinrerk, W. et al., 1992, J. Immunol. 149(3):847) was fused to the carboxy-terminal 6X histidine tagged Fc region of human IgG1 via a polypeptide linker. The chimeric protein was expressed in a mouse myeloma cell line, NS0. Molecular Mass: The recombinant mature human EMMPRIN/Fc is a disulfide-linked homodimeric protein. Based on N-terminal sequencing, the mature protein starts at Thr 25. The recombinant human EMMPRIN/Fc monomer has a calculated molecular mass of approximately 47.4 kD. As a result of glycosylation, the recombinant monomer migrates as an approximately 60-65 kD protein in SDS-PAGE under reducing conditions. Endotoxin Level: < 1.0 EU per 1 μg of the protein as determined by the LAL method. Activity: Measured by the ability of the immobilized protein to induce active MMP-1 production in NHLF cells. The ED50 for this effect is typically 2-8ug/ml. Reconstitution: It is recommended that sterile PBS be added to the vial to prepare a working stock solution of no less than 100ug/ml. The carrier-free protein should be used immediately upon reconstitution to avoid losses in activity due to non-specific binding to the inside surface of the vial. For long-term storage as a dilute solution, a carrier protein (e.g. 0.1% HSA or BSA) should be added to the vial. Storage: Lyophilized samples are stable for up to twelve months at -20°C. Upon reconstitution, this protein, in the presence of a carrier protein, can be stored under sterile conditions at 2-8°C for one month or at -20°C in a manual defrost freezer for three months without detectable loss of activity. Avoid repeated freeze-thaw cycles. | ||
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