Recombinant Human Transmembrane Protease Serine 2 (TMPRSS2) Protein (His), Active

Name: Recombinant Human Transmembrane Protease Serine 2 (TMPRSS2) Protein (His), Active
Brand: Beta LifeScience
SKU: BLC-05685P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Activity Recombinant Human TMPRSS2 His tag protein b0) enzyme activity is measured by its ability to cleave fluorogenic peptide substrate(Boc-Gln-Ala-Arg-AMC), The Km is 19.16μM. Biological Activity Assay

Activity Measured by Bromhexine Hydrochloride inhibit ratio on TMPRSS2 b0), which can cleave fluorogenic peptide substrate (Boc-Gln-Ala-Arg-AMC). The Bromhexine Hydrochloride inhibit EC 50 is 81.79-154.2μM. Biological Activity Assay

Activity Measured by Camostat Mesylate inhibit ratio on TMPRSS2 b0), which can cleave fluorogenic peptide substrate (Boc-Gln-Ala-Arg-AMC). The Camostat Mesylate inhibit EC 50 is 0.005877- 0.01293μM. Biological Activity Assay

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Product Overview

Description	Recombinant Human Transmembrane Protease Serine 2 (TMPRSS2) Protein (His), Active is produced by our Mammalian cell expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Endotoxin	Less than 1.0 EU/ug as determined by LAL method.
Activity	1. Recombinant Human TMPRSS2 His tag protein b0) enzyme activity is measured by its ability to cleave fluorogenic peptide substrate(Boc-Gln-Ala-Arg-AMC), The Km is 19.16μM. 2. Measured by Bromhexine Hydrochloride inhibit ratio on TMPRSS2 b0), which can cleave fluorogenic peptide substrate (Boc-Gln-Ala-Arg-AMC). The Bromhexine Hydrochloride inhibit EC 50 is 81.79-154.2μM. 3. Measured by Camostat Mesylate inhibit ratio on TMPRSS2 b0), which can cleave fluorogenic peptide substrate (Boc-Gln-Ala-Arg-AMC). The Camostat Mesylate inhibit EC 50 is 0.005877- 0.01293μM.
Uniprotkb	O15393
Target Symbol	TMPRSS2
Synonyms	TMPRSS2; PRSS10; Transmembrane protease serine 2; Serine protease 10
Species	Homo sapiens (Human)
Expression System	Mammalian cell
Tag	N-10His
Target Protein Sequence	WKFMGSKCSNSGIECDSSGTCINPSNWCDGVSHCPGGEDENRCVRLYGPNFILQVYSSQRKSWHPVCQDDWNENYGRAACRDMGYKNNFYSSQGIVDDSGSTSFMKLNTSAGNVDIYKKLYHSDACSSKAVVSLRCIACGVNLNSSRQSQIVGGESALPGAWPWQVSLHVQNVHVCGGSIITPEWIVTAAHCVEKPLNNPWHWTAFAGILRQSFMFYGAGYQVEKVISHPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEEKGKTSEVLNAAKVLLIETQRCNSRYVYDNLITPAMICAGFLQGNVDSCQGDSGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWIYRQMRADG-
Expression Range	106-492aa(R255Q)
Protein Length	Partial
Mol. Weight	46.4 kDa
Research Area	Biochemicals
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 μm sterile filtered 20 mM Tris-HCl, 0.5 M NaCl, 6% Trehalose, pH 8.0
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Plasma membrane-anchored serine protease that participates in proteolytic cascades of relevance for the normal physiologic function of the prostate. Androgen-induced TMPRSS2 activates several substrates that include pro-hepatocyte growth factor/HGF, the protease activated receptor-2/F2RL1 or matriptase/ST14 leading to extracellular matrix disruption and metastasis of prostate cancer cells. In addition, activates trigeminal neurons and contribute to both spontaneous pain and mechanical allodynia.; (Microbial infection) Facilitates human coronaviruses SARS-CoV and SARS-CoV-2 infections via two independent mechanisms, proteolytic cleavage of ACE2 receptor which promotes viral uptake, and cleavage of coronavirus spike glycoproteins which activates the glycoprotein for host cell entry. Upon SARS-CoV-2 infection, increases syncytia formation by accelerating the fusion process. Proteolytically cleaves and activates the spike glycoproteins of human coronavirus 229E (HCoV-229E) and human coronavirus EMC (HCoV-EMC) and the fusion glycoproteins F0 of Sendai virus (SeV), human metapneumovirus (HMPV), human parainfluenza 1, 2, 3, 4a and 4b viruses (HPIV). Essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9); involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity.
Subcellular Location	Cell membrane; Single-pass type II membrane protein.; [Transmembrane protease serine 2 catalytic chain]: Secreted.
Protein Families	Peptidase S1 family
Database References	HGNC: 11876 OMIM: 602060 KEGG: hsa:7113 STRING: 9606.ENSP00000381588 UniGene: PMID: 27285981 Study shows that T2E fusion transcripts are associated with higher levels of AMACR mRNA in patients with atypical small acinar proliferation (ASAP) which represents an indicator of risk for prostate cancer in patients with ASAP. PMID: 29277318 TMPRSS2-ERG may have a role in progression of prostate neoplasms and in alteration of the metabolic profile PMID: 27276682 We propose that epigenetic events are a significant and alternative driver of aggressive disease in TMPRSS2-ERG fusion-negative prostate cancer. PMID: 27814612 Meta-analysis showed the prevalence of TMPRSS2:ERG fusions in prostate cancer to be highest in men of European descent (49%), followed by Asians (27%) and then African (25%) descent. PMID: 28633309 Data show that tumors displaying TMPRSS2-ERG fusions that retained interstitial genes were less likely to be associated with biochemical recurrence PMID: 29127096 We demonstrate a role for inflammation-induced oxidative stress in the formation of DNA breaks leading to recurrent TMPRSS2-ERG gene fusions. The transcriptional status and epigenetic features of the target genes influence this effect. PMID: 27926866 NOTCH pathway inhibition antagonizes the growth and invasion of transmembrane protease serine 2 (TMPRSS2)-transforming protein ERG (ERG) (T2E) -positive prostate cancer cells. PMID: 28783165 The TMPRSS2-ERG gene fusion is the most frequently observed genetic aberration in prostate cancer. PMID: 28845585 Study provide evidence that PTEN deletion and TMPRSS2-ERG gene fusion were mutually exclusive in patients with prostate neoplasm. TMPRSS2-ERG gene fusion was rare compared to peripheral zone tumors and to PTEN inactivation in T1a transition zone tumors. PMID: 27500376 miR-204 upregulates androgen receptor (AR ) and downregulates TMPRSS2/ERG through direct regulation of their promoter methylation and set of transcription factors during AR cancer-related reprogramming. PMID: 28050800 differential expression of TMPRSS2:ERG in urine exosomes in prostate cancer and controls PMID: 27144529 The present study established evidence for the first two common PrCa risk variants differentially associated with TMPRSS2:ERG fusion status. TMPRSS2:ERG phenotyping of larger studies is required to determine comprehensive sets of variants with subtype-specific roles in prostate cancer. PMID: 27798103 Human coronavirus 229E presumably evolved to bypass the endosome by entering the cell via TMPRSS2. PMID: 27733646 Studies indicate that TMPRSS2-ERG fusion gene positive prostate cancers cells rewire intracellular signaling cascades and modulate gene and protein network. PMID: 28364793 TMPRSS2-ERG role in prostate cancer invasiveness and regulation of MMP-9 and plexin B1. PMID: 28004109 Our results indicate that it is possible to predict pT3 stage at final histology from TMPRSS2:ERG gene fusion at initial core needle biopsy. FISH determination of TMPRSS2:ERG gene fusion may be particularly useful for patients scheduled to undergo a radical prostatectomy in order to improve oncological and functional results PMID: 27377958 Data show there was a good agreement of transcriptional regulator ERG protein (ERG) immunostaining with the presence of TMPRSS2:ERG fusion protein. PMID: 27320318 A combination of high preoperative serum PSA and high expression of TMPRSS2-ERG could be promising in distinguishing those tumors that are aggressive and life-threatening. PMID: 27630329 Studies showed that urinary TMPRSS2:ERG transcripts seem to be indicative of Prostate cancer aggressiveness upon biopsy. [review] PMID: 26774207 Aspirin was associated with a significant reduction in the relative risk of TMPRSS2:ERG (T2E )fusion positive, but not T2E negative PMID: 26503111 the type II transmembrane serine protease TMPRSS2 was able to activate hemagglutinin for cell entry indicating that bat influenza A virus can utilize human proteases for hemagglutinin activation. PMID: 27028521 The relatively low rate of ERG-positive prostatic intraepithelial neoplasia counts in favor of the limited role of chimeric transcript TMPRSS2/ERG in the differential diagnosis of prostatic intraepithelial neoplasia PMID: 26978019 TMPRSS2 isoform 1 is expressed in viral target cells. PMID: 26379044 The TMPRSS2-ERG Gene Fusion Blocks XRCC4-Mediated Nonhomologous End-Joining Repair and Radiosensitizes Prostate Cancer Cells to PARP Inhibition PMID: 26026052 The potential for TMPRSS2:ERG gene fusion, detected by IHC, to modify the role of PTEN loss in lethal progression of prostate cancer. PMID: 26615022 Results indicate that PTEN loss occurs in cooperation with TMPRSS2-ERG fusion in prostate cancer and the majority of the samples harbor TMPRSS2-ERG fusion as well as PTEN gene deletion. PMID: 26424596 Elucidation of ERG regulation of ABEs in castration-resistant prostate cancer (CRPC) may help to stratify TMPRSS2-ERG fusion-positive prostate cancer patients in the clinic for anti-androgen receptor-driven therapies. PMID: 25754347 these data show that the androgen-driven events causing TMPRSS2-ERG fusions and other rearrangements of androgen-dependent genes in prostate epithelial cells of young patients preferentially lead to low-grade (and not high-grade) prostate cancer. PMID: 25015038 TMPRSS2-ERG fusion gene transcript was found in 63, 55 and 73% of the prostate cancer cases on urine alone, biopsy rinse material alone and paired samples, respectively. PMID: 24997128 Genetic inhibition of TMPRSS2-ERG junction oncogene in prostate cancer by means of siRNA has strong antineoplastic effect in a mouse model and in vitro. PMID: 25933120 Data showed that TMPRSS2 expression is not only dramatically increased in the primary cancers of patients but TMPRSS2 immunopositivity is also directly correlated with cancer pain severity in these patients. PMID: 25734995 High AR gene copy number emerges during the development of Small cell carcinoma of the prostate, often in association with TMPRSS2-ERG rearrangement. PMID: 24777847 Both IHC and qRT-PCR are useful tools in detecting TMPRSS2:ERG fusions. PMID: 25007891 Membrane bound meprin Beta is activated by transmembrane serine protease matriptase-2 at the cell surface. PMID: 26251449 Data indicate that inhibition of transcriptional regulator ERG protein expression in transmembrane protease serine 2 protein (TMPRSS2):ERG-positive prostate cancer cells increased neuroendocrine cell gene expression. PMID: 25263440 TMPRSS2 promotes the growth, invasion, and metastasis of prostate cancer cells via matriptase activation and extracellular matrix disruption. PMID: 26018085 Analysis of prostate cancer tissues showed that the presence of a TMPRSS2-ERG rearrangement was highly correlated with lower levels of NKX3.1 expression consistent with the role of NKX3.1 as a suppressor of the pathogenic gene rearrangement. PMID: 25977336 The TMPRSS2 Met160Val polymorphism is a genetic risk factor for sporadic prostate cancer in a Japanese population. PMID: 25040002 The expression levels of the TMPRSS2-ERG fusion is related to a more aggressive phenotype, have an effect on prognosis and could be molecular markers of progression for prostate cancer. PMID: 25939480 Results provide suggestive evidence that men with TMPRSS2:ERG positive tumors may have longer prostate cancer survival after ADT. PMID: 25728532 recent and maximum BMI are inversely associated with the odds of developing T2E-positive prostate cancer, but no associations were observed for T2E-negative prostate canc PMID: 25852077 TMPRSS2-ERG gene fusions induce prostate tumorigenesis by modulating microRNA miR-200c. PMID: 24186205 activates hepatitis C virus infection at the postbinding and entry stage PMID: 25203900 results demonstrate the ability of confocal microscopy and FISH to identify the cell-to-cell differences in common gene fusions such as TMPRSS2-ERG that may arise independently within the same tumor focus PMID: 25175909 The effect of TMPRSS2/ERG gene fusions had differing effects on radiosensitivity and chemosensitivity depending on cell line and fusion type. PMID: 21394739 These findings indicate that TMPRSS2-ERG may or may not lead to prostate cancer development PMID: 24961351 Report prognostic value of tissue/urinary TMPRSS2-ERG levels in prostate neoplasms. PMID: 24072184 concurrent in situ detection of gene expression, point mutations, and gene fusions of the prostate cancer relevant targets TMPRSS2-ERG PMID: 24931216 TMPRSS2:ERG gene fusion synergizes with the VDR to induce CYP24A1 expression-limiting VDR signaling. PMID: 24926821

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.