目录号 | 产品详情 | 靶点 | |
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T78875 | Mitochondrial Metabolism | ||
BTM-3528是一种线粒体蛋白酶OMA1的激活剂,能够过度激活线粒体整合应激反应(ISR)。该化合物促进了OMA1依赖的DELE1和OPA1的裂解,导致线粒体断裂。此外,BTM-3528通过激活eIF2α激酶HRI,引发细胞生长停滞及apoptosis。在多种DLBCL细胞系中表现出抗癌活性,且在异种移植人DLBCL SU-DHL-10细胞小鼠模型中显示出明显的体内抑制作用。 | |||
T78119 | HSV | ||
Z-L(D-Val)G-CHN2(即Z-LVG-CHN2)是半胱氨酸蛋白酶抑制剂的异构体,作为一种三肽衍生物,模仿了人体半胱氨酸蛋白酶结合中心的部分结构。它可以抑制HSV,并且能有效阻断SARS-COV-2的3CL pro蛋白酶,从而抑制病毒活性(EC50=190 nM),但对脊髓灰质炎病毒复制无显著作用。 | |||
T80240 | |||
Ala-parafluoroPhe-Arg-Cha-Cit-Tyr-NH2是一类具有生物活性的肽,作为蛋白酶激活受体1 (PAR-1) 的选择性激动剂,其特异性优于PAR-2。该肽通过HEK293细胞进行的基于细胞的钙信号传导测定确认了其对PAR-1的高特异性,并可用于研究PAR-1在体内的激活。PAR-1除了介导凝血酶的多种细胞作用外,还与PAR-4协作,参与调控凝血酶诱导的被分类为“凝血型”的肝细胞癌。 | |||
T38052 | |||
CRA-2059 is a highly specific and selective tryptase inhibitor, with a Ki of 620 pM for recombinant human tryptase-β (rHTβ)[1][2]. Tryptase is a trypsin-like serine protease found as a major protein component in human mast cell secretory granules. CRA-2059 has the potential for inflammatory bowel disease research[1]. [1]. Tremaine WJ, et al. Treatment of mildly to moderately active ulcerative colitis with a tryptase inhibitor (APC 2059): an open-label pilot study. Aliment Pharmacol Ther. 2002;16(3):407-413.[2]. Selwood T, et al. Potent bivalent inhibition of human tryptase-beta by a synthetic inhibitor. Biol Chem. 2003;384(12):1605-1611. | |||
T80234 | |||
SFNGGP-NH2是一种具有生物活性的肽。PAR-3是一种与凝血酶高亲和力结合的受体,其mRNA在人类皮肤肥大细胞中得到表达。研究指出,蛋白酶激活受体(PAR)在瘙痒反应中的作用涉及组胺依赖性及独立途径。虽然PAR-3本身不直接诱发瘙痒,却可能与PAR-4共同促发此症状。它们的共同表达可增强凝血酶的效应,这表明PAR-3单独时不进行跨膜信号传导,而是作为激活PAR-4的协同因子。 | |||
T38051 | |||
CRA-2059 hydrochloride is a highly specific and selective tryptase inhibitor, with a Ki of 620 pM for recombinant human tryptase-β (rHTβ)[1][2]. Tryptase is a trypsin-like serine protease found as a major protein component in human mast cell secretory granules. CRA-2059 hydrochloride has the potential for inflammatory bowel disease research[1]. [1]. Tremaine WJ, et al. Treatment of mildly to moderately active ulcerative colitis with a tryptase inhibitor (APC 2059): an open-label pilot study. Aliment Pharmacol Ther. 2002;16(3):407-413.[2]. Selwood T, et al. Potent bivalent inhibition of human tryptase-beta by a synthetic inhibitor. Biol Chem. 2003;384(12):1605-1611. | |||
T36225 | |||
N-p-Tosyl-Gly-Pro-Lys-pNA is a colorimetric substrate for plasmin.1,2,3Plasmin binds and hydrolyzes N-p-tosyl-Gly-Pro-Lys-pNA to releasep-nitroanilide (pNA), which can be quantified by colorimetric detection at 405 nm as a measure of plasmin activity. 1.Jespersen, J., Gram, J., and Astrup, T.The autodigestion of human plasmin follows a bimolecular mode of reaction subject to product inhibitionThromb. Res.41(3)395-404(1986) 2.Kim, S.H., and Choi, N.S.Electrophoretic analysis of protease inhibitors in fibrin zymographyAnal. Biochem.270(1)179-181(1999) 3.Chen, T., and Rael, E.D.Purification of M5, a fibrinolytic proteinase from Crotalus molossus molossus venom that attacks complementInt. J. Biochem. Cell Biol.29(5)789-799(1997) | |||
T35955 | |||
PAR2 (1-6) amide is a synthetic peptide agonist of proteinase-activated receptor 2 (PAR2) that corresponds to residues 1-6 of the amino terminal tethered ligand sequence of human PAR2 and residues 37-42 of the full-length sequence.1It binds to NCTC 2544 cells expressing human PAR2 (Ki= 9.64 μM in a radioligand binding assay) and induces calcium mobilization in the same cells (EC50= 0.075 μM).2PAR2 (1-6) amide (100 μM) reduces colony formation of A549 lung cancer cells.1It induces superoxide production and degranulation in isolated human eosinophils when used at a concentration of 500 μM.3PAR2 (1-6) amide (5 μmol/kg) induces tear secretion in rats when used in combination with amastatin .4 1.Bohm, S.K., Kong, W., Bromme, D., et al.Molecular cloning, expression and potential functions of the human proteinase-activated receptor-2Biochem. J.314(Pt 3)1009-1016(1996) 2.Kanke, T., Ishiwata, H., Kabeya, M., et al.Binding of a highly potent protease-activated receptor-2 (PAR2) activating peptide, [3H]2-furoyl-LIGRL-NH2, to human PAR2Br. J. Pharmacol.145(2)255-263(2005) 3.Miike, S., McWilliam, A.S., and Kita, H.Trypsin induces activation and inflammatory mediator release from human eosinophils through protease-activated receptor-2J. Immunol.167(11)6615-6622(2001) 4.Nishikawa, H., Kawai, K., Tanaka, M., et al.Protease-activated receptor-2 (PAR-2)-related peptides induce tear secretion in rats: Involvement of PAR-2 and non-PAR-2 mechanismsJ. Pharmacol. Exp. Ther.312(2)324-331(2005) | |||
T36903 | |||
Rasagiline-13C3is intended for use as an internal standard for the quantification of rasagiline by GC- or LC-MS. Rasagiline is an inhibitor of monoamine oxidase B (MAO-B; IC50= 4.43 nM for the rat brain enzyme).1It is selective for MAO-B over MAO-A (IC50= 412 nM for the rat brain enzyme). It inhibits serum and NGF withdrawal-induced apoptosis of PC12 cells when used at concentrations ranging from 0.01 to 100 μM.2Rasagiline inhibits rat brain MAO-Bin vivo(ED50= 0.1 mg/kg).1It reduces cerebral edema in a mouse model of traumatic brain injury.2Rasagiline (0.1 mg/kg) reduces cortical and hippocampal levels of full-length and soluble amyloid precursor protein (APP) in rats and mice. It also reduces α-synuclein-induced substantia nigral neuron loss and improves motor dysfunction in a mouse model of Parkinson's disease.3Formulations containing rasagiline have been used in the treatment of Parkinson's disease. 1.Youdim, M.B.H., Gross, A., and Finberg, J.P.Rasagiline [N-propargyl-1R(+)-aminoindan], a selective and potent inhibitor of mitochondrial monoamine oxidase BBrit. J. Pharmacol.132(2)500-506(2001) 2.Youdim, M.B.H., and Weinstock, M.Molecular basis of neuroprotective activities of rasagiline and the anti-Alzheimer drug TV3326 [(N-propargyl-(3R) aminoindan-5-YL)-ethyl methyl carbamate]Cell. Mol. Neurobiol.21(6)555-573(2001) 3.Kang, S.S., Ahn, E.H., Zhang, Z., et al.α-Synuclein stimulation of monoamine oxidase-B and legumain protease mediates the pathology of Parkinson's diseaseEMBO J.37(12)e98878(2018) | |||
T36717 | |||
RWJ-56110 dihydrochloride is a potent, selective, peptide-mimetic inhibitor of PAR-1 activation and internalization (binding IC50=0.44 uM) and shows no effect on PAR-2, PAR-3, or PAR-4. RWJ-56110 dihydrochloride inhibits the aggregation of human platelets induced by both SFLLRN-NH2 (IC50=0.16 μM) and thrombin (IC50=0.34 μM), quite selective relative to U46619 . RWJ-56110 dihydrochloride blocks angiogenesis and blocks the formation of new vessels in vivo. RWJ-56110 dihydrochloride induces cell apoptosis[1][2]. Proteinase-activated receptors (PARs) are a family of G protein-coupled receptors activated by the proteolytic cleavage of their N-terminal extracellular domain, exposing a new amino terminal sequence that functions as a tethered ligand to activate the receptors.RWJ56110 inhibits the aggregation of human platelets induced by both SFLLRN-NH2 (IC50=0.16 μM) and thrombin (IC50=0.34 μM) while being quite selective relative to collagen and the thromboxane mimetic U46619 [1].RWJ-56110 dihydrochloride is fully inhibits thrombin-induced RASMC proliferation with an IC50 value of 3.5 μM. RWJ-56110 dihydrochloride shows blockade of thrombin's action with RASMC calcium mobilization (IC50=0.12 μM), as well as with HMVEC (IC50=0.13 μM) and HASMC calcium mobilization (IC50=0.17 μM)[1].RWJ56110 (0.1-10 μM; 24-96 hours) inhibits endothelial cell growth dose-dependently, with half-maximal inhibitory concentration of RWJ56110 is approximately 10 μM[2].RWJ56110 (0.1-10 μM; 6 hours) inhibits DNA synthesis of endothelial cells in a thymidine incorporation assays. Endothelial cells are in fast-growing state (50-60% confluence), RWJ56110 inhibits cell DNA synthesis in a dose-dependent manner, but when cells that are in the quiescent state (100% confluent), the inhibitory effect of PAR-1 antagonists is much less pronounced[2].RWJ56110 (0.1-10 μM; pretreatment for 15 min) inhibits thrombin-induced Erk1/2 activation in a concentration-dependent manner. However, when endothelial cells are stimulated by FBS (final concentration 4%), it reduces partially the activated levels of Erk1/2[2].RWJ56110 (30 μM; 24 hours) has an inhibitory effect on endothelial cell cycle progression. It reduces the percentage of cells in the S phase, while alterations in the percentages of G1 and G2/M cells are less pronounced[2]. Western Blot Analysis[2] Cell Line: Endothelial cells [1]. Andrade-Gordon, et al.Design, synthesis, and biological characterization of a peptide-mimetic antagonist for a tethered-ligand receptor. oc Natl Acad Sci U S A. 1999 Oct 26;96(22):12257-62. [2]. Panagiota Zania, et al. Blockade of angiogenesis by small molecule antagonists to protease-activated receptor-1: association with endothelial cell growth suppression and induction of apoptosis. J Pharmacol Exp Ther. 2006 Jul;318(1):246-54. |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-00541 | LON PROTEASE Protein, E. coli, Recombinant (His) | E. coli | E. coli | ||
Lon protease, an ATP-dependent mitochondrial protease, is important in mitochondrial protein maintenance. Lon protease is a multifunctional enzyme, and its functions include the degradation of damaged proteins and naturally short-lived proteins, ATPase and chaperone-like activities, as well as DNA binding. Lon protease plays a major role in the protein quality control system in mammalian cell mitochondria. It is present in the mitochondrial matrix and degrades oxidized and misfolded proteins, thereby protecting the cell from various extracellular stresses, including oxidative stress. The intellectual disability-associated and thalidomide-binding protein cereblon (CRBN) contains a large, highly conserved Lon domain. The Lon ATP-dependent protease plays an important role in regulating many biological processes in bacteria.
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TMPK-01339 | 3CLpro/3C-like Protease Protein (S144A), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPK-01346 | 3CLpro/3C-like Protease Protein (L50F), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPJ-01431 | SARS-CoV-2 Papain-Like Protease Protein | SARS-CoV-2 | E. coli | ||
Replication of severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) requires proteolytic processing of the replicase polyprotein by two viral cysteine proteases, a chymotrypsin-like protease (3CLpro) and a papain-like protease (PLpro). These proteases are important targets for development of antiviral drugs that would inhibit viral replication and reduce mortality associated with outbreaks of SARS-CoV. PLpro is a cysteine protease located within the non-structural protein 3 (NS3) section of the viral polypeptide. PLPro activity is required to process the viral polyprotein into functional, mature subunits; specifically, PLPro cleaves a site at the amino-terminus of the viral replicase region. In addition to its role in viral protein maturation, PLPro possesses a deubiquitinating and deISGylating activity. In vivo, this protease antagonizes innate immunity by inhibiting IRF3-induced production of type I interferons.
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TMPK-01343 | 3CLpro/3C-like Protease Protein (A191T), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPK-01335 | 3CLpro/3C-like Protease Protein (E166V), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPK-01336 | 3CLpro/3C-like Protease Protein (L50F, E166V), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPK-01340 | 3CLpro/3C-like Protease Protein (F140A), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPK-01384 | SARS PLpro/papain-like protease Protein (His) | SARS | E. coli | ||
The coronaviral proteases, papain-like protease (PLpro) and 3C-like protease (3CLpro), are attractive antiviral drug targets because they are essential for coronaviral replication. Although the primary function of PLpro and 3CLpro are to process the viral polyprotein in a coordinated manner, PLpro has the additional function of stripping ubiquitin and ISG15 from host-cell proteins to aid coronaviruses in their evasion of the host innate immune responses.
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TMPK-01338 | 3CLpro/3C-like Protease Protein (H172Y), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPK-01341 | 3CLpro/3C-like Protease Protein (P132H), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPK-01337 | 3CLpro/3C-like Protease Protein (Q189K), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPK-01348 | 3CLpro/3C-like Protease Protein, SARS-COV-2, Recombinant (aa 1-306) | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPK-01342 | 3CLpro/3C-like Protease Protein (A191V), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPK-01347 | 3CLpro/3C-like Protease Protein (E166A), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPY-01897 | PRSS3 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Trypsin-3, also known as Trypsin III, brain trypsinogen, Serine protease 3 and PRSS3, is a secreted protein that belongs to the peptidase S1 family. Trypsin-3 / PRSS3 is expressed is in pancreas and brain. It contains one peptidase S1 domain. Trypsin-3 / PRSS3 can degrade intrapancreatic trypsin inhibitors that protect against CP. Genetic variants that cause higher mesotrypsin activity might increase the risk for chronic pancreatitis (CP). A sustained imbalance of pancreatic proteases and their inhibitors seems to be important for the development of CP. The trypsin inhibitor-degrading activity qualified PRSS3 as a candidate for a novel CP susceptibility gene. Trypsin-3 / PRSS3 has been implicated as a putative tumor suppressor gene due to its loss of expression, which is correlated with promoter hypermethylation, in esophageal squamous cell carcinoma and gastric adenocarcinoma.
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TMPK-01344 | 3CLpro/3C-like Protease Protein (L167F), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPK-01345 | 3CLpro/3C-like Protease Protein (L50F, E166A, L167F), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPH-00581 | ATP-dependent Clp protease adapter protein ClpS Protein, E. coli, Recombinant (His) | E. coli | E. coli | ||
Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation.
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TMPK-01352 | SARS-CoV-2 PLpro/papain-like protease Protein (His & Avi) | SARS | E. coli | ||
The coronaviral proteases, papain-like protease (PLpro) and 3C-like protease (3CLpro), are attractive antiviral drug targets because they are essential for coronaviral replication. Although the primary function of PLpro and 3CLpro are to process the viral polyprotein in a coordinated manner, PLpro has the additional function of stripping ubiquitin and ISG15 from host-cell proteins to aid coronaviruses in their evasion of the host innate immune responses.
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TMPY-04997 | Prostasin/PRSS8 Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
Prostasin (Prss8), also known as channel activating protease 1 (CAP1), is a trypsinlike serine peptidase, and plays important roles in epithelial physiology. It is originally purified as an active, soluble enzyme from human seminal fluid and is highly expressed in prostate, lung, kidney, salivary gland and pancreas. Prostasin is expressed as a glycosyl-phosphatidylinositol (GPI)-anchored membrane protein in prostate epithelial cells, and also exists as a secreted proteolytic enzyme possibly via tryptic cleavage of its COOH-terminal hydrophobic domain. Prostasin is found to activate the epithelial sodium channel (ENaC) which is tightly regulated and is critical for maintaining salt and fluid balance in the lung and kidney in both normal and pathological conditions. Accordingly, prostasin has been proposed as a target for therapeutic inhibition in cystic fibrosis. Besides, prostasin inhibits prostate and breast cancer cell invasion in vitro, suggesting a functional role as a suppressor of tumor invasion, as well as a regulator of gene expression during inflammation.
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TMPJ-00851 | IDE Protein, Human, Recombinant (His) | Human | Human Cells | ||
Insulin-Degrading Enzyme (IDE) is a secreted enzyme that belongs to the peptidase M16 family. IDE is a large zinc-binding protease and cleaves multiple short polypeptides that vary considerably in sequence. IDE plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin, and other peptides, and thereby plays a role in intercellular peptide signaling. IDE degrades amyloid formed by APP and IAPP. IDE may participate in the degradation and clearance of naturally secreted amyloid β-protein by neurons and microglia. IDE, which migrates at 110 kDa during gel electrophoresis under denaturing conditions, has since been shown to have additional substrates, including the signaling peptides glucagon, TGF α and β-endorphin.
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TMPJ-01295 | SENP7 Protein, Human, Recombinant | Human | E. coli | ||
Sentrin-Specific Protease 7 (SENP7) acts as a SUMO-2/3-specific protease. SENP7 is likely to regulate the metabolism of poly-SUMO-2/3 rather than SUMO-1 conjugation in vivo. SENP7 has a restricted substrate specificity, and displaying paralogue-specific isopeptidase activity. The C-terminal catalytic domain of SENP7 depolymerized poly-SUMO-2 chains but does not have activity against poly-SUMO-1 chains. SENP7 also had isopeptidase activity against di-SUMO-2- and SUMO-2-modified RanGAP1 (Ran GTPase-activating protein 1) but had limited activity against SUMO-1-modified RanGAP1.
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TMPY-04928 | TMPRSS11B Protein, Human, Recombinant (His) | Human | HEK293 | ||
TMPRSS11B Protein, Human, Recombinant (His) is expressed in HEK293 with His tag. The predicted molecular weight is 44.3 kDa. Accession number: CAD91168.1
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TMPY-00274 | Enterokinase Protein, Bovine, Recombinant (His) | Bovine | Yeast | ||
Enterokinase Protein, Bovine, Recombinant (His) is expressed in Yeast with His tag. The predicted molecular weight is 27.1 kDa. Accession number: P98072-1
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TMPJ-01278 | SENP8 Protein, Human, Recombinant (His) | Human | E. coli | ||
Sentrin-Specific Protease 8 (SENP8) mediates the reversible covalent modification of proteins by NEDD8. SENP8 catalyzes the full-length NEDD8 to generate its mature form and deconjugation of NEDD8 from targeted proteins such as CUL2 , CUL4A in vivo, or p53. but it does not show activity against ubiquitin or SUMO proteins.
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TMPJ-01320 | BSSP-4 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Brain-Specific Serine Protease 4 (BSSP-4) is a serine protease that preferentially cleaves the synthetic substrate H-D-Leu-Thr-Arg-pNA compared to tosyl-Gly-Pro-Arg-pNA. BSSP-4 is expressed abundantly in the epithelial cells of the airways, including trachea, esophagus and fetal lung, but scarce in adult lung and expressed at low levels in placenta, pancreas, prostate and thyroid gland. BSSP-4 belongs to the peptidase S1 family and related to trypsin, referentially hydrolyzing substrates after arginine and lysine residues. However, BSSP-4 is less susceptible to inhibition by common trypsin inhibitors such as aprotinin, α1-antitrypsin and secretory leukocyte protease inhibitor. BSSP-4 efficiently converts pro-urokinase- type plasminogen activator to its mature, active form.
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TMPJ-01203 | HATL5 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Transmembrane Protease Serine 11B (TMPRSS11B) is a single-pass type II membrane protein member of the peptidase S1 family. TMPRSS11B contains one peptidase S1 domain and one SEA domain. TMPRSS11B is a serine protease that may play some biological role in the host defense system on the mucous membrane independently of or in cooperation with other substances in airway mucous or bronchial secretions.
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TMPY-04985 | TMPRSS11D Protein, Human, Recombinant (His) | Human | HEK293 | ||
TMPRSS11D (HAT) belongs to the large type II transmembrane serine protease (TTSP) family, participating in various biological and physiological processes. TMPRSS11D protein expression in tumorous tissues were correlated with NSCLC patients' clinical characteristics and overall survival. Both TMPRSS11D mRNA and protein expression levels were significantly higher in NSCLC tumorous tissues than in adjacent normal tissues. High TMPRSS11D protein expression was associated with high TNM stages, and high TMPRSS11D protein expression is an independent prognostic marker in NSCLC.
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TMPH-02553 | BSSP-4 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
BSSP-4 Protein, Mouse, Recombinant (His) is expressed in E. coli.
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TMPY-00905 | Prostasin/PRSS8 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Prostasin (Prss8), also known as channel activating protease 1 (CAP1), is a trypsinlike serine peptidase, and plays important roles in epithelial physiology. It is originally purified as an active, soluble enzyme from human seminal fluid and is highly expressed in prostate, lung, kidney, salivary gland and pancreas. Prostasin is expressed as a glycosyl-phosphatidylinositol (GPI)-anchored membrane protein in prostate epithelial cells, and also exists as a secreted proteolytic enzyme possibly via tryptic cleavage of its COOH-terminal hydrophobic domain. Prostasin is found to activate the epithelial sodium channel (ENaC) which is tightly regulated and is critical for maintaining salt and fluid balance in the lung and kidney in both normal and pathological conditions. Accordingly, prostasin has been proposed as a target for therapeutic inhibition in cystic fibrosis. Besides, prostasin inhibits prostate and breast cancer cell invasion in vitro, suggesting a functional role as a suppressor of tumor invasion, as well as a regulator of gene expression during inflammation.
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TMPH-02644 | Enteropeptidase Protein, Mouse, Recombinant (His & SUMO) | Mouse | E. coli | ||
Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A). It catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases.
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TMPJ-01083 | Serpin E2 Protein, Mouse, Recombinant (His) | Mouse | Human Cells | ||
Serpin E2 is a member of the Serpin superfamily. It is differentially expressed during neuronal differentiation and is able to transform human embryonic kidney cells into neuronlike cells. Its over-expression in mice leads to progressive neuronal and motor dysfunction in these animals. It is also over-expressed in the majority of pancreatic carcinoma as well as gastric and colorectal cancer samples whereas it is weakly expressed in all normal pancreas and chronic pancreatitis tissue samples. Serpin E2 is a potent inhibitor of thrombin, trypsin, urokinase, plasmin and plasminogen activators. It plays an important role in controlling male fertility because its knockout male mice show a marked impairment in fertility from the onset of sexual maturity and its abnormal expression is found in the semen of men with seminal dysfunction.
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TMPJ-01383 | Serpin A10 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Serpin A10 is a secreted protein that belongs to the serpin family. It is predominantly expressed in the liver and secreted in the plasma. Its phosphorylation sites are present in the extracelllular medium. It inhibits factors Xa and XIa of the coagulation cascade in the presence of protein Z, calcium, and phospholipid. Mutations in SERPINA10 are associated with venous thrombosis.
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TMPH-00334 | Candidapepsin-6 Protein, Candida albicans, Recombinant (His) | Candida albicans | E. coli | ||
Candidapepsin-6 Protein, Candida albicans, Recombinant (His) is expressed in E. coli with N-terminal 6xHis tag. The predicted molecular weight is 39.8 kDa. Accession number: P43095
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TMPH-02643 | Enteropeptidase Protein, Mouse, Recombinant (His & Myc) | Mouse | HEK293 | ||
Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A). It catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases.
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TMPY-02117 | Marapsin Protein, Human, Recombinant (His) | Human | HEK293 | ||
The name "Pancreasin" because it is transcribed strongly in the pancreas. This secreted, tryptic serine protease, also known as Marapsin or PRSS27 (Protease, serine, 27), is a member of the peptidase S1 family. Pancreasin is inhibited by benzamidine and leupeptin but resists several classic inhibitors of trypsin. Marapsin was constitutively expressed in nonkeratinizing stratified squamous epithelia of human esophagus, tonsil, cervix, larynx, and cornea. In fact, marapsin was the second most strongly up-regulated protease in psoriatic lesions, where expression was localized to the upper region of the hyperplastic epidermis. Similarly, in the hyperproliferative epithelium of regenerating murine skin wounds, marapsin localized to the suprabasal layers, where keratinocytes undergo squamous differentiation. Marapsin's restricted expression, localization, and cytokine-inducible expression suggest a role in the terminal differentiation of keratinocytes in hyperproliferating squamous epithelia.
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TMPJ-01336 | SENP2 Protein, Human, Recombinant | Human | E. coli | ||
SENP2 is an enzyme that belongs to the peptidase C48 family. SENP2 is a protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO1, SUMO2 and SUMO3 to their mature forms and deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins. SUMO1 is a small ubiquitin-like protein that can be covalently conjugated to other proteins. It has been implicated as a down-regulator of CTNNB1 levels and may therefore be a modulator of the Wnt pathway.
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TMPH-00332 | Candidapepsin-2 Protein, Candida albicans (strain WO-1), Recombinant (His) | Candida albicans | E. coli | ||
Candidapepsin-2 Protein, Candida albicans (strain WO-1), Recombinant (His) is expressed in E. coli with N-terminal 6xHis tag. The predicted molecular weight is 42.3 kDa. Accession number: C4YMJ3
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TMPH-00333 | Candidapepsin-2 Protein, Candida albicans, Recombinant (His) | Candida albicans | E. coli | ||
Candidapepsin-2 Protein, Candida albicans, Recombinant (His) is expressed in E. coli with N-terminal 10xHis tag. The predicted molecular weight is 42.4 kDa. Accession number: P0CS83
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TMPJ-01069 | Serpin A1e Protein, Mouse, Recombinant (His) | Mouse | Human Cells | ||
Alpha-1-antitrypsin 1-5(SERPIN A1) is a secreted protein and belongs to the serpin family. Serpins bind the protease active site resulting in a major conformational rearrangement that traps the enzyme in a covalent acyl-enzyme intermediate. Mouse SERPIN A1 is a serine protease inhibitor whose targets include elastase,plasmin, thrombin, trypsin, chymotrypsin, and plasminogen activator. Defects in this gene can cause emphysema orliver disease. Several transcript variants encoding the same protein have been found for this gene.
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TMPJ-01282 | Serpin B12 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Serpin B12 is a member of the serpin family. Serpins are the largest and most diverse family of serine protease inhibitors. Most serpins are secreted and attain physiologic concentrations in the blood and extracellular fluids. Serpin B12 is expressed in many tissues, including brain, bone marrow, lymph node, heart, lung, liver, pancreas, testis, ovary, and intestine. Serpins are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner. SerpinB12 inhibits trypsin and plasmin, but not thrombin, coagulation factor Xa, or urokinase-type plasminogen activator.
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TMPH-02035 | ASPRV1 Protein, Human, Recombinant (His & Myc) | Human | in vitro E. coli expression system | ||
ASPRV1 Protein, Human, Recombinant (His & Myc) is expressed in in vitro E. coli expression system.
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TMPH-01315 | CASR Protein, Human, Recombinant (GST) | Human | E. coli | ||
G-protein-coupled receptor that senses changes in the extracellular concentration of calcium ions and plays a key role in maintaining calcium homeostasis. Senses fluctuations in the circulating calcium concentration and modulates the production of parathyroid hormone (PTH) in parathyroid glands. The activity of this receptor is mediated by a G-protein that activates a phosphatidylinositol-calcium second messenger system. The G-protein-coupled receptor activity is activated by a co-agonist mechanism: aromatic amino acids, such as Trp or Phe, act concertedly with divalent cations, such as calcium or magnesium, to achieve full receptor activation.
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TMPJ-00452 | Serpin A1a Protein, Mouse, Recombinant (His) | Mouse | Human Cells | ||
Serpin A1a is also known as alpha-1-antitrypsin, is a member of the serpin superfamily of serine proteinase inhibitors that are involved in the regulation of a number of proteolytic processes. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin.
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TMPJ-01116 | HABP2 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Hyaluronan-binding protein 2(HABP2) is an extracellular serine protease which binds hyaluronic acid. It secreted as an inactive single-chain precursor and is then activated to a heterodimeric form, which consists of a 50 kDa heavy and a 27 kDa light chain linked by a disulfide bond. HABP2 is involved in cell adhesion, it can cleave the alpha-chain at multiple sites and the beta-chain between 'Lys-53' and 'Lys-54' , but not the gamma-chain of fibrinogen. As a result of this, it does not initiate the formation of the fibrin clot and does not cause the fibrinolysis directly. It does not cleave prothrombin and plasminogen but converts the inactive single chain urinary plasminogen activator to the active two chain form, activates coagulation factor VII.
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TMPY-01580 | PRSS2 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Trypsin-2, also known as Trypsin II, Anionic trypsinogen, Serine protease 2, PRSS2 and TRY2, is a secreted protein that belongs to the trypsin serine protease family including Trypsin, PRSS1, PRSS2 and PRSS3. It consists of a signal peptide (residues 1-15), a pro region (residues 16-23), and a proteolytically active mature chain (residues 24-247). PRSS2 contains one peptidase S1 domain. It is secreted into the duodenum, hydrolysing peptides into their smaller building blocks, which is necessary for the uptake of protein in the food. It is secreted by the pancreas in the form of inactive zymogen, trypsinogen and cleaved to its active form in the small intestine when the pancreas is stimulated by cholecystokinin through the common activation mechanism.
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TMPJ-01253 | Serpin A3N Protein, Mouse, Recombinant (His) | Mouse | Human Cells | ||
Serine protease inhibitor A3N(Serpin A3N) is a serine protease inhibitor that is structurally related to α1 antichymotrypsin encoded by the SERPINA3 gene. Serpin A3N is highly expressed in brain, testis, lung, thymus, and spleen. It is expressed with low levels in bone marrow, kidney and skeletal muscle. Serpin A3N secreted by Sertoli cells may regulate the activity of locally produced Granzyme B. Granzyme B inhibition by Serpin A3N may therefore regulate Granzyme Bmediated killing by cytotoxic lymphocytes, providing a means to disable cellmediated immune responses.
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TMPH-02581 | Chymase 1 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion.
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TMPH-01057 | Caspase-8 Protein, Human, Recombinant (His) | Human | E. coli | ||
Thiol protease that plays a key role in programmed cell death by acting as a molecular switch for apoptosis, necroptosis and pyroptosis, and is required to prevent tissue damage during embryonic development and adulthood. Initiator protease that induces extrinsic apoptosis by mediating cleavage and activation of effector caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Cleaves and activates effector caspases CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. Binding to the adapter molecule FADD recruits it to either receptor TNFRSF6/FAS mediated or TNFRSF1A. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. In addition to extrinsic apoptosis, also acts as a negative regulator of necroptosis: acts by cleaving RIPK1 at 'Asp-324', which is crucial to inhibit RIPK1 kinase activity, limiting TNF-induced apoptosis, necroptosis and inflammatory response. Also able to initiate pyroptosis by mediating cleavage and activation of gasdermin-D (GSDMD): GSDMD cleavage promoting release of the N-terminal moiety (Gasdermin-D, N-terminal) that binds to membranes and forms pores, triggering pyroptosis. Initiates pyroptosis following inactivation of MAP3K7/TAK1. Also acts as a regulator of innate immunity by mediating cleavage and inactivation of N4BP1 downstream of TLR3 or TLR4, thereby promoting cytokine production. May participate in the Granzyme B (GZMB) cell death pathways. Cleaves PARP1.; Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex.; Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex.; Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex. Acts as an inhibitor of the caspase cascade.; Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex.
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