Human Transmembrane Protease, Serine 2 (TMPRSS2) Protein

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Description
Human Transmembrane Protease, Serine 2 (TMPRSS2) is a recombinant Human protein produced in a Prokaryotic expression system (E. coli).
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Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Transmembrane Protease, Serine 2 (TMPRSS2) |
| Host | E. coli |
| Origin | Human |
| Conjugation | Unconjugated |
| Observed MW | Molecular Weight: Calculated MW: 27.0 kDa Observed MW (SDS-PAGE): 27 kDa Concentration: Prior to lyophilization: 300 µg/ml Sequence Fragment: Ser284-Gly492 Tag: N-terminal His tag |
| Expression | Recombinant |
| Purity | > 97% |
| Size 1 | 10 µg |
| Size 2 | 50 µg |
| Size 3 | 100 µg |
| Size 4 | 200 µg |
| Size 5 | 500 µg |
| Form | Lyophilized To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in 20 mM Tris, 150 mM NaCl, pH 8.0. If a higher concentration is required, the product can be reconstituted directly in 20 mM Tris, 150 mM NaCl, pH 8.0, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex. |
| Tested Applications | WB, SDS-PAGE |
| Buffer | Prior to lyophilization: 20 mM Tris, 150 mM NaCl, pH 8.0, containing 0.01% Sarcosyl, 5% Trehalose. |
| Availability | Shipped within 5-7 working days. |
| Storage | Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | O15393 |
| Background | Protein TMPRSS2 |
| Status | RUO |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
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This gene encodes a protein that belongs to the serine protease family. The encoded protein contains a type II transmembrane domain, a receptor class A domain, a scavenger receptor cysteine-rich domain and a protease domain. Serine proteases are known to be involved in many physiological and pathological processes. This gene was demonstrated to be up-regulated by androgenic hormones in prostate cancer cells and down-regulated in androgen-independent prostate cancer tissue. The protease domain of this protein is thought to be cleaved and secreted into cell media after autocleavage. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
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