TMPRSS2 Protein, Human (P.pastoris, His)

The TMPRSS2 protein is a plasma membrane-anchored serine protease that plays critical roles in prostate physiology, cancer metastasis, pain modulation, and viral infection. Its lytic activity affects proteolytic cascades involved in prostate function, and androgen-induced activation contributes to cancer progression. TMPRSS2 Protein, Human (P.pastoris, His) is the recombinant human-derived TMPRSS2 protein, expressed by P. pastoris , with N-6*His labeled tag.

TMPRSS2 Protein, a plasma membrane-anchored serine protease, exhibits a distinct role in various physiological and pathological processes. Known for its cleavage activity at arginine residues, TMPRSS2 plays a pivotal role in proteolytic cascades crucial for the normal physiological function of the prostate. In the context of prostate cancer, androgen-induced TMPRSS2 activation leads to the cleavage of substrates like pro-hepatocyte growth factor/HGF, protease-activated receptor-2/F2RL1, and matriptase/ST14, promoting extracellular matrix disruption and metastasis. Additionally, TMPRSS2 contributes to the modulation of pain sensitivity by activating trigeminal neurons, influencing both spontaneous pain and mechanical allodynia. In the realm of microbial infection, TMPRSS2 plays a critical role in facilitating infections by human coronaviruses SARS-CoV and SARS-CoV-2 through two independent mechanisms: the proteolytic cleavage of the ACE2 receptor, promoting viral uptake, and the cleavage of coronavirus spike glycoproteins, activating the glycoprotein for host cell entry. This protease is also essential for the spread and pathogenesis of influenza A virus, participating in the proteolytic cleavage and activation of the hemagglutinin (HA) protein, which is indispensable for viral infectivity. The diverse functions of TMPRSS2 underscore its significance in both normal physiological processes and disease pathogenesis.

Recombinant Human TMPRSS2 His tag protein enzyme activity is measured by its ability to cleave fluorogenic peptide substrate(Boc-Gln-Ala-Arg-AMC), The Km is 50-80 μM.

Human

P. pastoris

N-6*His

O15393-1 (W106-G492)

7113  [NCBI]

Extracellular Domain

WKFMGSKCSNSGIECDSSGTCINPSNWCDGVSHCPGGEDENRCVRLYGPNFILQVYSSQRKSWHPVCQDDWNENYGRAACRDMGYKNNFYSSQGIVDDSGSTSFMKLNTSAGNVDIYKKLYHSDACSSKAVVSLRCIACGVNLNSSRQSRIVGGESALPGAWPWQVSLHVQNVHVCGGSIITPEWIVTAAHCVEKPLNNPWHWTAFAGILRQSFMFYGAGYQVEKVISHPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEEKGKTSEVLNAAKVLLIETQRCNSRYVYDNLITPAMICAGFLQGNVDSCQGDSGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWIYRQMRADG

Approximately 45 kDa, based on SDS-PAGE under reducing conditions.

≥ 90%, as determined by reducing SDS-PAGE.

Lyophilized powder

1.Lyophilized from a 0.22 μm sterile filtered of 20 mM Tris-HCl, 0.5 M NaCl, 6% trehalose, pH 8.0.
2.Lyophilized from a 0.22 μm sterile filtered of PBS, 6% trehalose, pH 7.4.
Please refer to the lot-specific COA for specific buffer information.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

• [1]. /biology-dictionary/bhy-cell.html