目录号 | 产品详情 | 靶点 | |
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T26744 | |||
BAY-598 R-异构体是BAY589的R-异构体,它可用作参考化合物。它是是赖氨酸N-甲基转移酶(SMYD2)的抑制剂,对SMYD2比蛋白酶激活的受体1(PAR1)具有选择性。 | |||
T75903 | |||
VKGILS-NH2 TFA 是SLIGKV-NH2(PAR2激动剂)的逆序反向对照肽,无影响细胞DNA合成。 | |||
T11369L | Others | ||
GB-110 hydrochloride selectively induces PAR2-mediated intracellular Ca2+ release in HT29 cells with an EC50 of 0.28 μM. GB-110 hydrochloride is a potent, orally active, and nonpeptidic protease activated receptor 2 (PAR2) agonist. | |||
T28017 | |||
Merbarone is a Type II DNA topoisomerase inhibitor. Merbarone inhibits the catalytic activity of human topoisomerase IIalpha by blocking DNA cleavage. Merbarone induces activation of caspase-activated DNase and excision of chromosomal DNA loops from the n | |||
T80094 | |||
Dansyl-Glu-Gly-Arg-Chloromethylketone,一种蛋白酶抑制剂,特异性针对丝氨酸/苏氨酸蛋白酶。此化合物有效抑制活化猪因子IX。 | |||
TP1966 | |||
Cell-permeable peptide cleaved from protease-activated receptor 1 (PAR1) upon receptor activation. Attenuates endothelial cell migration and proliferation (IC50 ~ 20 μM), and induces cell cycle arrest. Promotes activation of caspase-3 and exhibits pro-apo | |||
TMA1012 | Androgen Receptor HIV Protease Autophagy | ||
Ganoderiol F has anti-inflammatory, cytotoxic and anti-HIV activity, it inhibits activity of topoisomerases in vitro, and it inhibits human immunodeficiency virus-1 protease with IC(50) values of 20-40 microM. It induced HO-1 expression, activation of the mitogen-activated protein kinase EKR and up-regulation of cyclin-dependent kinase inhibitor p16 and suppressed lipopolysaccharide (LPS)-induced nitric oxide (NO) production. | |||
T75904 | |||
GYPGQV TFA (PAR 4 (1-6) TFA) 是一种六肽,作为蛋白酶激活受体 4 (PAR4) 片段,能特异性抑制PAR4。 | |||
T35867 | |||
TRAP-6 peptide is a hexapeptide corresponding to residues 42-47 of protease-activated receptor 1 (PAR1). It acts as an agonist of PAR1, inducing platelet aggregation in human platelet-rich plasma ex vivo (EC50 = 0.8 μM). TRAP-6 (0.3 and 0.6 mg/kg) has a triphasic effect on mean arterial blood pressure (MAP) in anesthetized rats with a short decrease, an increase, and then a longer decrease in MAP following intravenous administration. | |||
T60854 | |||
ENMD-1068 hydrochloride 是一种选择性的蛋白酶激活受体 2 (PAR2) 拮抗剂。ENMD-1068 hydrochloride 可通过抑制TGF-β1/Smad 信号转导而减少肝星状细胞的活化和胶原蛋白的表达。ENMD-1068 hydrochloride 还能抑制子宫内膜细胞的增殖,并诱导病灶中上皮细胞的凋亡。ENMD-1068 hydrochloride 可用于子宫内膜异位症、肝纤维化的研究。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPH-00134 | AcMNPV Viral cathepsin Protein (His & SUMO) | AcMNPV | E. coli | ||
Cysteine protease that plays an essential role in host liquefaction to facilitate horizontal transmission of the virus. Accumulates within infected cells as an inactive proenzyme (proV-CATH), which is activated by proteolytic cleavage upon cell death. AcMNPV Viral cathepsin Protein (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 39.9 kDa and the accession number is P25783.
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TMPY-03653 | CTRL Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
CTRL-1, also known as chymotrypsin-like protease, belongs to thepeptidase S1 family. CTRL-1 contains 1peptidase S1 domain. Its expression is increased in preeclampsia (PE). Placental-derived chymotrypsin-like protease is responsible for inducing endothelial inflammatory phenotypic changes possibly by upregulation of cell adhesion molecule expressions, activation of cellular protease, and induction of extracellular regulated kinase phosphorylation. Activated microglia have been observed in various neurodegenerative diseases, including Alzheimer's disease (AD), Parkinson's disease (PD), amyotrophic lateral sclerosis, and multiple sclerosis. Five structurally distinct inhibitors that are known to inhibit chymotrypsin-like proteases were partially protective. They might represent a novel class of drugs with benefit in diseases where overactivity of microglia contributes to the pathogenesis.
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TMPJ-00542 | TPSB2 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Tryptases are Trypsin-like Serine Proteases. β-Tryptases are the main isoenzymes in mast cells. Βtryptases form active tetramers with heparin proteoglycan. In the tetramer, the unique arrangement of the active sites facing a narrow central pore, β-Tryptases are resistant to macromolecule protease inhibitors . When mast cells are activated, β-Tryptases are released and participate in provoking inflammatory conditions . β-Tryptases have been implicated as mediators in the pathogenesis of asthma and other allergic disorders.
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TMPH-02237 | TMPRSS2 Protein, Human, Recombinant (His & Myc) | Human | HEK293 Cells | ||
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.
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TMPH-02236 | TMPRSS2 Protein, Human, Recombinant (E. coli, His) | Human | E. coli | ||
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.
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TMPJ-01116 | HABP2 Protein, Human, Recombinant (His) | Human | HEK293 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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TMPJ-00845 | CTSE Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Cathepsin E (CTSE) is a gastric aspartyl protease that functions as a disulfide-linked homodimer. It is a member of the Peptidase C1 family, and has a specificity similar to that of Pepsin A and Cathepsin D. CTSE is localized to the endoplasmic reticulum and Golgi apparatus, while the mature enzyme is localized to the endosome. It is expressed abundantly in the stomach, the Clara cells of the lung and activated B-lymphocytes, and at lower levels in lymph nodes, skin and spleen. CTSE is an intracellular proteinase that have a role in immune function, activation-induced lymphocyte depletion in the thymus, neuronal degeneration and glial cell activation in the brain. Futhermore, it probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation.
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TMPH-02832 | Serpin A5 Protein, Mouse, Recombinant (His) | Mouse | Baculovirus Insect Cells | ||
Heparin-dependent serine protease inhibitor acting in body fluids and secretions. Inactivates serine proteases by binding irreversibly to their serine activation site. Involved in the regulation of intravascular and extravascular proteolytic activities. Plays hemostatic roles in the blood plasma. Acts as a procoagulant and proinflammatory factor by inhibiting the anticoagulant activated protein C factor as well as the generation of activated protein C factor by the thrombin/thrombomodulin complex. Acts as an anticoagulant factor by inhibiting blood coagulation factors like prothrombin, factor XI, factor Xa, plasma kallikrein and fibrinolytic enzymes such as tissue- and urinary-type plasminogen activators. In seminal plasma, inactivates several serine proteases implicated in the reproductive system. Inhibits the serpin acrosin; indirectly protects component of the male genital tract from being degraded by excessive released acrosin. Inhibits tissue- and urinary-type plasminogen activator, prostate-specific antigen and kallikrein activities; has a control on the sperm motility and fertilization. Inhibits the activated protein C-catalyzed degradation of SEMG1 and SEMG2; regulates the degradation of semenogelin during the process of transfer of spermatozoa from the male reproductive tract into the female tract. In urine, inhibits urinary-type plasminogen activator and kallikrein activities. Inactivates membrane-anchored serine proteases activities such as MPRSS7 and TMPRSS11E. Inhibits urinary-type plasminogen activator-dependent tumor cell invasion and metastasis. May also play a non-inhibitory role in seminal plasma and urine as a hydrophobic hormone carrier by its binding to retinoic acid.
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TMPY-02014 | Coagulation factor VII/F7 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Coagulation factor VII, also known as Serum prothrombin conversion accelerator, Factor VII, F7 and FVII, is a member of the peptidase S1 family. Factor VII is one of the central proteins in the coagulation cascade. It is an enzyme of the serine protease class, and Factor VII (FVII) deficiency is the most frequent among rare congenital bleeding disorders. Factor VII contains two EGF-like domains, one Gla (gamma-carboxy-glutamate) domain and one peptidase S1 domain. The main role of factor VII is to initiate the process of coagulation in conjunction with tissue factor (TF). Tissue factor is found on the outside of blood vessels, normally not exposed to the blood stream. The action of the Factor VII is impeded by tissue factor pathway inhibitor (TFPI), which is released almost immediately after initiation of coagulation. Factor VII is vitamin K dependent and is produced in the liver. Upon vessel injury, tissue factor is exposed to the blood and circulating Factor VII. Once bound to TF, FVII is activated to FVIIa by different proteases, among which are thrombin (factor IIa), factor Xa, IXa, XIIa, and the FVIIa-TF complex itself. Recombinant activated factor VII (rFVIIa) is a haemostatic agent, which was originally developed for the treatment of haemophilia patients with inhibitors against factor FVIII or FIX. FVIIa binds specifically to endothelial protein C receptor (EPCR), a known cellular receptor for protein C and activated protein C, on the endothelium. rFVIIa is a novel hemostatic agent, originally developed for the treatment of hemorrhage in hemophiliacs with inhibitors, which has been successfully used recently in an increasing number of nonhemophilic bleeding conditions.
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TMPY-02831 | Caspase-7 Protein, Human, Recombinant (His) | Human | E. coli | ||
Caspase 7, also known as caspase-7 and MCH3, belongs to the cysteine-aspartic acid protease (caspase) family. Caspases play a role in the signal transduction pathways of apoptosis, necrosis and inflammation. There are two major classes of caspases: initiators and effectors. The initiator isoforms (caspases-1,-4,-5,-8,-9,-10,-11,-12) are activated by, and interact with, upstream adaptor molecules through protein-protein interaction domains known as CARD and DED. Effector caspases (-3,-6,-7) are responsible for cleaving downstream substrates and are sometimes referred to as the executioner caspases. Caspase 7 exists in lung, skeletal muscle, liver, kidney, spleen, heart, and moderately in testis. Caspase 7 cannot be detected in the brain. Caspase 7 functions in the activation cascade of caspases responsible for apoptosis execution. It cleaves and activates sterol regulatory element binding proteins (SREBPs). It proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp- -Gly-217' bond. Overexpression promotes programmed cell death.
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TMPJ-00490 | Serpin A5 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Serpin A5 is a member of the human Serpin superfamily consists of at least 35 members. It is synthesized in the liver and has been detected in saliva, cerebral spinal fluid, amniotic fluid, tears and semen. As a potent inhibitor of the protein C anticoagulant pathway at the levels of both zymogen activation and enzyme inhibition, Serpin A5 additionally inhibits a variety of serine protease including thrombin, factor Xa, several kallekreins and acrosin. It plays a critical role in the processes of blood of blood coagulation and fertilization. Serpin A5 also inhibits urinary plasminogen activator (uPA), a mediator of tumor cell invasion, and regulates tumor growth and metastasis by inhibiting angiogenesis. Furthermore, recent studies have identified PCI as a potent and direct inhibitor of activated HGFA (hepatocyte growth factor activator), suggesting a novel function in the regulation of tissue repair and regeneration. Similar to Serpins C1 and D1, the thrombin inhibitory activity of serpinA5 is enhanced by heparin.
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TMPY-01711 | Serpin B2 Protein, Human, Recombinant (GST) | Human | Baculovirus Insect Cells | ||
Serpins are the largest and most diverse family of serine protease inhibitors which are involved in some fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner.SerpinB2, also known as Plasminogen activator inhibitor 2, Placental plasminogen activator inhibitor, Monocyte Arg-serpin, Urokinase inhibitor and PAI2, is a cytoplasm protein that belongs to the serpin family and Ov-serpin subfamily. SerpinB2 is a major product of activated monocytes and macrophages and is substantially induced during most inflammatory processes. Distinct from its widely described extracellular role as an inhibitor of urokinase plasminogen activator. SerpinB2 has been shown to have an intracellular role as a retinoblastoma protein (Rb)-binding protein that inhibits Rb degradation. SerpinB2 is widely described as an inhibitor of urokinase plasminogen activator. SerpinB2 inhibits urokinase-type plasminogen activator. The monocyte derived SerpinB2 is distinct from the endothelial cell-derived PAI-1. SerpinB2 is a potentially important inducible host factor that significantly promotes HIV-1 replication.
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TMPJ-00837 | LAMP1 Protein, Mouse, Recombinant (His) | Mouse | HEK293 Cells | ||
Lysosomal associated membrane protein 1 (LAMP1) is an approximately 120 kDa transmembrane glycoprotein that is a major protein component of lysosomal membranes. Mature mouse LAMP1 consists of a 346 amino acid (aa) intralumenal domain (ECD), a 24 aa transmembrane segment, and a 12 aa cytoplasmic tail. Its lumenal domain is organized into two heavily N-glycosylated regions separated by a Ser/Pro-rich linker that carries a minor amount of O-linked glycosylation. Within the lumenal domain, mouse LAMP1 shares approximately 64% and 82% aa sequence identity with human and rat LAMP1, respectively. The sorting of LAMP1 to lysosomes relies on a tyrosine motif in the cytoplasmic tail. In cytotoxic T cells and mast cells, LAMP1 is expressed in the membranes of intracellular granules that contain effector molecules such as perforin, granzymes, eicosanoids, and histamine. A glycoform of LAMP1 known as M150 is expressed on the surface of activated macrophages where it promotes T cell co-stimulation and a Th1 biased immune response. Exposure of epithelial cells to pathogenic Neisseria bacteria induces the redistribution of LAMP1 to the cell surface where it can be cleaved by the Neisseria IgA1 protease.
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TMPY-00818 | Granzyme H/GZMH Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Granzymes are key components of the immune response that play important roles in eliminating host cells infected by intracellular pathogens. Several granzymes are potent inducers of cell death. A total of eight granzymes (A-G and M) have been identified in the mouse, but only five are known in humans (A, B, H, M, and granzyme 3), and granzyme H appears to be specifically human. Human granzyme H is a neutral serine protease that is expressed predominantly in the lymphokine-activated killer (LAK)/natural?killer (NK) compartment of the immune system. In adenovirus-infected cells in which granzyme B (gzmB) and downstream apoptosis pathways are inhibited, granzyme H directly cleaves the adenovirus DNA-binding protein (DBP), a viral component required for viral DNA replication. This virus demonstrated that gzmH directly induces an important decay in viral DNA replication. Interestingly, gzmH also cleaves the adenovirus 1K assembly protein, a major inhibitor of gzmB, and relieves gzmB inhibition. Granzyme H has a very high amino acid identity (>9%) with many portions of the granzyme B sequence, particularly near the amino terminus of the molecule despite performing a distinct enzymic function.
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TMPH-01664 | OMA1 Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
Metalloprotease that is part of the quality control system in the inner membrane of mitochondria. Activated in response to various mitochondrial stress, leading to the proteolytic cleavage of target proteins, such as OPA1, UQCC3 and DELE1. Following stress conditions that induce loss of mitochondrial membrane potential, mediates cleavage of OPA1 at S1 position, leading to OPA1 inactivation and negative regulation of mitochondrial fusion. Also acts as a regulator of apoptosis: upon BAK and BAX aggregation, mediates cleavage of OPA1, leading to the remodeling of mitochondrial cristae and allowing the release of cytochrome c from mitochondrial cristae. In depolarized mitochondria, may also act as a backup protease for PINK1 by mediating PINK1 cleavage and promoting its subsequent degradation by the proteasome. May also cleave UQCC3 in response to mitochondrial depolarization. Also acts as an activator of the integrated stress response (ISR): in response to mitochondrial stress, mediates cleavage of DELE1 to generate the processed form of DELE1 (S-DELE1), which translocates to the cytosol and activates EIF2AK1/HRI to trigger the ISR. Its role in mitochondrial quality control is essential for regulating lipid metabolism as well as to maintain body temperature and energy expenditure under cold-stress conditions. Binds cardiolipin, possibly regulating its protein turnover. Required for the stability of the respiratory supercomplexes.
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