目录号 | 产品详情 | 靶点 | |
---|---|---|---|
T7740 | Protease-activated Receptor | ||
Protease-Activated Receptor-4 diTFA 是蛋白酶激活受体 4 (PAR4) 激动剂。 | |||
T7513 | Protease-activated Receptor | ||
Protease-Activated Receptor-2, amide (SLIGKV-NH2) 是 PAR2 的激动剂,IC50为 10.4 M。 | |||
T38836L | Protease-activated Receptor | ||
Protease-Activated Receptor-1, PAR-1 Agonist acetate 是一种选择性蛋白酶激活受体 1 (PAR-1) 激动剂肽。 它对应于 PAR1 栓系配体,可以选择性地模拟凝血酶通过该受体的作用。 | |||
TP1046 | Protease-activated Receptor | ||
SLIGRL-NH2 (Protease-Activated Receptor-2 Activating Peptide) 为一种蛋白酶激活受体-2 (PAR-2) 激动剂,具有诱导非组胺能性瘙痒的功能。 | |||
T10925L | Others | ||
Cysteine Protease inhibitor hydrochloride 是一种半胱氨酸蛋白酶(cysteine protease)抑制剂。 | |||
T39729 | |||
HIV Protease Substrate 1 is a fluorogenic compound that offers insights into the enzymatic activity of HIV protease, making it a valuable tool for studying this aspect. | |||
T8936 | Others | ||
Proteinase K (proteinase K for tritirachium album) 是一种非特异性丝氨酸蛋白酶,可用于蛋白消化。它在有 SDS 或尿素存在的情况下,在很大 pH 值 (4-12)、盐浓度和温度单位内均有活性。 | |||
T10924 | Cysteine Protease | ||
Cysteine protease inhibitor-2 是半胱氨酸蛋白酶抑制剂。 | |||
T10925 | Others | ||
Cysteine protease inhibitors are inhibitors of cysteine proteases. Target: Cysteine Protease | |||
T39503 | |||
Hepatitis Virus C NS3 Protease Inhibitor 2 is a peptide inhibitor derived from a product that targets the NS3 protease of the hepatitis C virus (HCV). Its inhibitory activity against the NS3 protease is characterized by a Ki value of 41 nM. |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
---|---|---|---|---|---|
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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
|
|||||
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
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
TMPH-02553 | BSSP-4 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
BSSP-4 Protein, Mouse, Recombinant (His) is expressed in E. coli.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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
|
|||||
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
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
TMPH-00717 | Protease 7 Protein, E. coli, Recombinant (His) | E. coli | E. coli | ||
Protease that can cleave T7 RNA polymerase, ferric enterobactin receptor protein (FEP), antimicrobial peptide protamine and other proteins. This protease has a specificity for paired basic residues.
|
|||||
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.
|