目录号 | 产品详情 | 靶点 | |
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T24328 | |||
L 680833 is an orally active monocyclic beta-lactam human polymorphonuclear leukocyte elastase inhibitor. | |||
T30303 | |||
BAY8040 is a potent selective human neutrophilic elastase inhibitor with excellent potency and selectivity with promising pharmacokinetic characteristics. | |||
T11525L | Others | ||
GW-311616 hydrochloride is a long duration, orally bioavailable, and selective human neutrophil elastase (HNE) inhibitor (IC50: 22 nM; Ki: 0.31 nM). | |||
T34465 | |||
S 2484 is a chromogranic specific granulocyte elastase substrate. | |||
T62846 | |||
Freselestat quarterhydrate (ONO-6818 quarterhydrate) 是一种有效的、口服具有活力的嗜中性粒细胞弹性蛋白酶 (neutrophil elastase) 抑制剂 (Ki: 12.2 nM)。Freselestat quarterhydrate 对其他蛋白酶(例如胰蛋白酶,蛋白酶3,胰弹性蛋白酶,凝血酶,纤溶酶,胶原酶,组织蛋白酶G 和鼠巨噬细胞弹性蛋白酶)的活性低 100 倍以上,表现出有效的抗炎作用。 | |||
T25781 | |||
MDL 101146 is an orally active neutrophil elastase inhibitor. | |||
T15144 | Others | ||
DMP 777 is an orally active inhibitor of human leukocyte elastase. | |||
T25784L | |||
MDL-101146, (S)- is an effective orally active inhibitor of human neutrophil elastase. | |||
T69790 | |||
GW-475151 inhibits human neutrophil elastase (HNE). | |||
T25782 | |||
MDL 27324 is an inhibitor of human neutrophil elastase. |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPH-03166 | Elastase Protein, Pseudomonas aeruginosa, Recombinant (His & SUMO) | Pseudomonas aeruginosa | E. coli | ||
Cleaves host elastin, collagen, IgG, and several complement components as well as endogenous pro-aminopeptidase. Autocatalyses processing of its pro-peptide. Processes the pro-peptide of pro-chitin-binding protein (cbpD). Involved in the pathogenesis of P.aeruginosa infections.
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TMPH-01773 | ELANE Protein, Human, Recombinant (GST) | Human | E. coli | ||
Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis. Capable of killing E.coli but not S.aureus in vitro; digests outer membrane protein A (ompA) in E.coli and K.pneumoniae.
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TMPH-02584 | CELA3B Protein, Mouse, Recombinant (His & Myc) | Mouse | Yeast | ||
Efficient protease with alanine specificity but only little elastolytic activity.
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TMPJ-00481 | CELA3A Protein, Human, Recombinant (His) | Human | Human Cells | ||
Chymotrypsin-Like Elastase Family Member 3A (CELA3A) is an enzyme that contains one peptidase S1 domain. ELA3A belongs to the peptidase S1 family of the Elastase subfamily. ELA3A is secreted from the pancreas as a zymogen and, like other serine proteases such as trypsin, chymotrypsin and kallikrein, it has a digestive function in the intestine. ELA3A may also function in the intestinal transport and metabolism of cholesterol. ELA3A is efficient protease with alanine specificity but only little elastolytic activity. ELA3A preferentially cleaves proteins after alanine residues.
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TMPH-01093 | CELA2A Protein, Human, Recombinant (E. coli, His) | Human | E. coli | ||
Elastase that enhances insulin signaling and might have a physiologic role in cellular glucose metabolism. Circulates in plasma and reduces platelet hyperactivation, triggers both insulin secretion and degradation, and increases insulin sensitivity.
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TMPH-01094 | CELA2A Protein, Human, Recombinant (His) | Human | Yeast | ||
Elastase that enhances insulin signaling and might have a physiologic role in cellular glucose metabolism. Circulates in plasma and reduces platelet hyperactivation, triggers both insulin secretion and degradation, and increases insulin sensitivity.
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TMPH-02583 | CELA3B Protein, Mouse, Recombinant (E. coli, His & Myc) | Mouse | E. coli | ||
Efficient protease with alanine specificity but only little elastolytic activity.
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TMPH-01097 | CELA3B Protein, Human, Recombinant (His) | Human | E. coli | ||
Efficient protease with alanine specificity but only little elastolytic activity.
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TMPH-01096 | CELA3A Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
Efficient protease with alanine specificity but only little elastolytic activity.
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TMPH-01095 | CELA2B Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
Acts upon elastin.
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TMPH-02582 | CELA2A Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Elastase that enhances insulin signaling and might have a physiologic role in cellular glucose metabolism. Circulates in plasma and reduces platelet hyperactivation, triggers both insulin secretion and degradation, and increases insulin sensitivity.
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TMPH-03583 | Extracellular elastase Protein, S. epidermidis, Recombinant (His & Myc) | Staphylococcus epidermidis | E. coli | ||
Protease that has a low substrate specificity. Glucagon is preferentially cleaved between aromatic (Phe) and hydrophobic (Val) amino acids. Hydrolyzes casein and elastin.
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TMPH-03466 | Elastase-1 Protein, Salmo salar, Recombinant (His) | Salmo salar | E. coli | ||
Acts upon elastin.
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TMPH-03271 | Complement factor D Protein, Rat, Recombinant (His & Myc) | Rat | HEK293 | ||
Factor D cleaves factor B when the latter is complexed with factor C3b, activating the C3bbb complex, which then becomes the C3 convertase of the alternate pathway. Its function is homologous to that of C1s in the classical pathway.
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TMPH-03272 | Complement factor D Protein, Rat, Recombinant (His) | Rat | Yeast | ||
Factor D cleaves factor B when the latter is complexed with factor C3b, activating the C3bbb complex, which then becomes the C3 convertase of the alternate pathway. Its function is homologous to that of C1s in the classical pathway.
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TMPY-00915 | Serpin A1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
SerpinA1, also known as Alpha-1 antitrypsin (AAT), is a prototype member of the Serpin superfamily of the serine protease inhibitors. This serine protease inhibitor blocks the protease, neutrophil elastase. Alpha-1 antitrypsin is mainly produced in the liver and acts as an antiprotease. Its principal function is to inactivate neutrophil elastase, preventing tissue damage. SerpinA1 (alpha1-antitrypsin), an acute phase protein and the classical neutrophil elastase inhibitor, is localized within lipid rafts in primary human monocytes in vitro. Its association with monocytes is inhibited by cholesterol depleting/efflux-stimulating agents (nystatin, filipin, MbetaCD (methyl-beta-cyclodextrin) and oxidized low-density lipoprotein (oxLDL) and conversely, enhanced by free cholesterol. Furthermore, SerpinA1/monocyte association per se depletes lipid raft cholesterol as characterized by the activation of extracellular signal-regulated kinase 2, formation of cytosolic lipid droplets, and complete inhibition of oxLDL uptake by monocytes. Previous population studies have suggested that heterozygote status for the AAT gene (SerpinA1) is a risk factor for chronic rhinosinusitis with nasal polyposis (CRSwNP). Alpha-1 antitrypsin deficiency is a recently identified genetic disease that occurs almost as frequently as cystic fibrosis. It is caused by various mutations in the SerpinA1 gene, and has numerous clinical implications. Alpha-1 antitrypsin deficiency is an inherited disease affecting the lung and liver. In the liver, alpha-1 antitrypsin deficiency may manifest as benign neonatal hepatitis syndrome; a small percentage of adults develop liver fibrosis, with progression to cirrhosis and hepatocellular carcinoma. Its most important physiologic functions are the protection of pulmonary tissue from aggressive proteolytic enzymes and regulation of pulmonary immune processes.
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TMPY-02869 | MMP-12 Protein, Human, Recombinant (catalytic domain) | Human | E. coli | ||
Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological processes such as morphogenesis, differentiation, angiogenesis, and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases, and tumor invasion. Macrophage Metalloelastase, also known as Matrix metalloproteinase-12, Macrophage elastase, MMP12, and MMP-12, is a secreted protein that belongs to the peptidase M1A family. MMP12 is a macrophage-secreted elastase that is highly induced in the liver and lung in response to S. mansoni eggs and contains four hemopexin-like domains. MMP12 is a proteolytic enzyme responsible for the cleavage of plasminogen to angiotensin, which has an angiostatic effect. It may be involved in tissue injury and remodeling and has significant elastolytic activity. It may be related to prognosis in breast cancer patients. MMP12 promotes fibrosis by limiting the expression of specific ECM-degrading MMPs. Like MMP12, MMP13 expression is highly dependent on IL-13 and type I I-IL-4 receptor signaling. MMP12 is a potent proinflammatory and oncogenic molecule. MMP12 up-regulation plays a critical role in emphysema to lung cancer transition that is facilitated by inflammation.
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TMPY-00672 | Azurocidin/CAP37 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Azurocidin (AZU1), also known as heparin-binding protein (HBP) or cationic antimicrobial protein 37 (CAP37), is an azurophil granule antibiotic protein, with monocyte chemotactic and antibacterial activity. The Azurophil granules, specialized lysosomes of the neutrophil, contain at least 10 proteins implicated in the killing of microorganisms. Azurocidin is a member of the serine protease family that includes Cathepsin G, neutrophil elastase (NE), and proteinase 3 (PR3), however, Azurocidin is not a serine proteinase since the active site serine and histidine residues are replaced. Neutrophils arriving first at sites of inflammation release Azurocidin, which acts in a paracrine fashion on endothelial cells causing the development of intercellular gaps and allowing leukocyte extravasation. It thus be regarded as a reasonable therapeutic target for a variety of inflammatory disease conditions.
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TMPY-01909 | Elafin Protein, Human, Recombinant (His) | Human | HEK293 | ||
Elafin, also known as Elastase-specific inhibitor, Peptidase inhibitor 3, Protease inhibitor WAP3, Skin-derived antileukoproteinase, WAP four-disulfide core domain protein 14, PI3, WAP3 and WFDC14, is a secreted protein that contains one WAP domain. Elafin / PI3 consists of two domains: the transglutaminase substrate domain (cementoin moiety) and the elastase inhibitor domain. The transglutaminase substrate domain at the N-terminus serves as an anchor to localize elafin covalently to specific sites on extracellular matrix proteins. The serine anti-protease Elafin / PI3 is expressed by monocytes, alveolar macrophages, neutrophils, and at mucosal surfaces and possesses antimicrobial activity. It is also known to reduce lipopolysaccharide-induced neutrophil influx into murine alveoli as well as to abrogate lipopolysaccharide-induced production of matrix metalloprotease 9, macrophage inhibitory protein 2, and tumor necrosis factor-alpha by as-yet unidentified mechanisms. Elafin / PI3 is a neutrophil serine protease inhibitor expressed in lung and displaying anti-inflammatory and anti-bacterial properties. Elafin / PI3 is a neutrophil and pancreatic elastase-specific inhibitor of skin. It may prevent elastase-mediated tissue proteolysis. Elafin / PI3 will regulate proteolytic enzymes during menstruation and will contribute to the innate defense against uterine infection.
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TMPH-03177 | RhlR Protein, Pseudomonas aeruginosa, Recombinant (His & Myc & SUMO) | Pseudomonas aeruginosa | E. coli | ||
Necessary for transcriptional activation of the rhlAB genes encoding the rhamnosyltransferase. It also functions as a transcriptional activator of elastase structural gene (lasB). Binds to autoinducer molecules BHL (N-butanoyl-L-homoserine lactone), and HHL (N-hexanoyl-L-homoserine lactone).
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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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TMPY-03436 | Serglycin Protein, Human, Recombinant (His) | Human | HEK293 | ||
SRGN is known as a hematopoietic cell granule proteoglycan. Proteoglycans stored in the secretory granules of various hematopoietic cells has a protease-resistant peptide core, and is vital for neutralizing hydrolytic enzymes. SRGN is associated with the macromolecular complex of granzymes and perforin, which may serve as a mediator of granule-mediated apoptosis. It is required for storage of some proteases in both connective tissue and mucosal mast cells and for storage of granzyme B in T-lymphocytes. SRGN also plays a role in localizing neutrophil elastase in azurophil granules of neutrophils.
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TMPY-00442 | Serpin A1 Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
SerpinA1, also known as Alpha-1 antitrypsin (AAT), is a prototype member of the Serpin superfamily of the serine protease inhibitors. This serine protease inhibitor blocks the protease, neutrophil elastase. Alpha-1 antitrypsin is mainly produced in the liver and acts as an antiprotease. Its principal function is to inactivate neutrophil elastase, preventing tissue damage. SerpinA1 (alpha1-antitrypsin), an acute phase protein and the classical neutrophil elastase inhibitor, is localized within lipid rafts in primary human monocytes in vitro. Its association with monocytes is inhibited by cholesterol depleting/efflux-stimulating agents (nystatin, filipin, MbetaCD (methyl-beta-cyclodextrin) and oxidized low-density lipoprotein (oxLDL) and conversely, enhanced by free cholesterol. Furthermore, SerpinA1/monocyte association per se depletes lipid raft cholesterol as characterized by the activation of extracellular signal-regulated kinase 2, formation of cytosolic lipid droplets, and complete inhibition of oxLDL uptake by monocytes. Previous population studies have suggested that heterozygote status for the AAT gene (SerpinA1) is a risk factor for chronic rhinosinusitis with nasal polyposis (CRSwNP). Alpha-1 antitrypsin deficiency is a recently identified genetic disease that occurs almost as frequently as cystic fibrosis. It is caused by various mutations in the SerpinA1 gene, and has numerous clinical implications. Alpha-1 antitrypsin deficiency is an inherited disease affecting the lung and liver. In the liver, alpha-1 antitrypsin deficiency may manifest as benign neonatal hepatitis syndrome; a small percentage of adults develop liver fibrosis, with progression to cirrhosis and hepatocellular carcinoma. Its most important physiologic functions are the protection of pulmonary tissue from aggressive proteolytic enzymes and regulation of pulmonary immune processes.
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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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TMPY-02373 | Serglycin Protein, Human, Recombinant (His & Myc) | Human | HEK293 | ||
SRGN is known as a hematopoietic cell granule proteoglycan. Proteoglycans stored in the secretory granules of various hematopoietic cells has a protease-resistant peptide core, and is vital for neutralizing hydrolytic enzymes. SRGN is associated with the macromolecular complex of granzymes and perforin, which may serve as a mediator of granule-mediated apoptosis. It is required for storage of some proteases in both connective tissue and mucosal mast cells and for storage of granzyme B in T-lymphocytes. SRGN also plays a role in localizing neutrophil elastase in azurophil granules of neutrophils.
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TMPH-03176 | LasA Protein, Pseudomonas aeruginosa, Recombinant (His & SUMO) | Pseudomonas aeruginosa | E. coli | ||
Involved in proteolysis and elastolysis (degradation of the host protein elastin). Has staphylolytic activity (degrades pentaglycine cross-links in cell wall peptidogylcan), preferring Gly-Gly-|-X substrates where X is Ala or Gly. Enhances the elastolytic but not proteolytic activity of elastase (lasB) and elastolytic activity of other proteases. Degradation of host elastin is likely to contribute to the pathogenicity of P.aeruginosa. While either His-317 or His-356 can abstract a proton in the hydrolysis reaction, the same residue performs both functions in a given catalytic cycle, with the other stabilizing the catalytic intermediate.
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TMPH-03580 | Zinc metalloproteinase aureolysin Protein, S. aureus, Recombinant (His & Myc) | Staphylococcus aureus | E. coli | ||
Plays an essential role in immune evasion by helping bacteria to resist complement-mediated killing by neutrophils. Inhibits the deposition of host C3b on bacterial surfaces and the release of the chemoattractant C5a by cleaving the central complement protein C3. The cleavage site renders the C3b molecule vulnerable to proteolytic degradation by host regulators. Cleaves and inactivates host SERPINA1, which is an endogenous protease inhibitor essential for controlling neutrophil serine protease elastase. Plays also an essential role in the cleavage and subsequent activation of the serine protease SspA which is involved in colonization and infection of human tissues.
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TMPJ-00234 | AMBP Protein, Human, Recombinant (His) | Human | Human Cells | ||
Protein AMBP belongs to the calycin superfamily and Lipocalin family. AMBP can be cleaved into three chains: α-1-microglobulin, inter-α-trypsin inhibitor light chain and trypstatin. AMBP is expressed by the liver and secreted in plasma. α-1-microglobulin occurs in many physiological fluids including the plasma, urine, and cerebrospinal fluid. Inter-α-trypsin inhibitor is present in the plasma and urine. α-1-microglobulin occurs as a monomer and also in complexes with IgA and albumin, Inter-α-trypsin inhibitor inhibits trypsin, plasmin and lysosomal granulocytic elastase. Trypstatin act as a trypsin inhibitor, exists in a monomer forms and also occurs as a complex with tryptase in mast cells.
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TMPJ-00505 | Serpin A1 Protein, Human, Recombinant (aa 25-418, His) | Human | Human Cells | ||
Serpin A1 is a prototype member of the Serpin superfamily of the serine protease inhibitors. As one of the most abundant proteinase inhibitors in the circulation, it is synthesized in hepatocytes, and to a lesser extent, in macrophages as well as intestinal epithelial cell lines and secreted as the abundant proteinase inhibitor in the circulation whose targets include elastase, plasmin, thrombin, trypsin, chymotrypsin, and plasminogen activator. Point mutations in the native SerpinA1 variants result in Serpin A1 deficiency, and consequently lead to several clinical complications such as pulmonary emphysema, juvenile hepatitis, cirrhosis, and hepatocellular carcinoma. For example, the Z variants (Glu342 to Lys) forms intracellular inclusion bodies, is not secreted, and leads to a severe SerpinA1 deficiency. Accordingly, Serpin A1 deficiency in circulation is associated with emphysema or liver disease.
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TMPY-05305 | alanyl-tRNA synthetase Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
Alanyl-tRNA synthetase (AARS) belongs to the family of ligases, specifically those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. This enzyme participates in alanine and aspartate metabolism and aminoacyl-tRNA biosynthesis. Alanyl-tRNA synthetase (AlaRS) catalyzes synthesis of Ala-tRNA (Ala) and hydrolysis of mis-acylated Ser- and Gly-tRNA (Ala) at 2 different catalytic sites. Their role is not confined to catalyze the attachment of amino acids to transfer RNAs and thereby establish the rules of genetic code by virtue of matching the nucleotide triplet of anticodon with cognate amino acid. Under apoptotic conditions in cell culture, the full-length enzyme is secreted, and the two cytokine activities can be generated by leukocyte elastase, an extracellular protease. Secretion of this tRNA synthetase may contribute to apoptosis both by arresting translation and producing needed cytokines. This protein could be an attractive target of drugs against bacterial, fungal and parasitic infections.
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TMPY-02441 | alanyl-tRNA synthetase Protein, Mouse, Recombinant (His) | Mouse | Baculovirus-Insect Cells | ||
Alanyl-tRNA synthetase (AARS) belongs to the family of ligases, specifically those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. This enzyme participates in alanine and aspartate metabolism and aminoacyl-tRNA biosynthesis. Alanyl-tRNA synthetase (AlaRS) catalyzes synthesis of Ala-tRNA (Ala) and hydrolysis of mis-acylated Ser- and Gly-tRNA (Ala) at 2 different catalytic sites. Their role is not confined to catalyze the attachment of amino acids to transfer RNAs and thereby establish the rules of genetic code by virtue of matching the nucleotide triplet of anticodon with cognate amino acid. Under apoptotic conditions in cell culture, the full-length enzyme is secreted, and the two cytokine activities can be generated by leukocyte elastase, an extracellular protease. Secretion of this tRNA synthetase may contribute to apoptosis both by arresting translation and producing needed cytokines. This protein could be an attractive target of drugs against bacterial, fungal and parasitic infections.
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TMPH-03119 | SERPINB1 Protein, Pig, Recombinant (His & Myc) | Sus scrofa (Pig) | E. coli | ||
Neutrophil serine protease inhibitor that plays an essential role in the regulation of the innate immune response, inflammation and cellular homeostasis. Acts primarily to protect the cell from proteases released in the cytoplasm during stress or infection. These proteases are important in killing microbes but when released from granules, these potent enzymes also destroy host proteins and contribute to mortality. Regulates the activity of the neutrophil proteases elastase, cathepsin G, proteinase-3, chymase, chymotrypsin, and kallikrein-3. Acts also as a potent intracellular inhibitor of GZMH by directly blocking its proteolytic activity. During inflammation, limits the activity of inflammatory caspases CASP1, CASP4 and CASP5 by suppressing their caspase-recruitment domain (CARD) oligomerization and enzymatic activation. When secreted, promotes the proliferation of beta-cells via its protease inhibitory function.; May be cleaved leading to a loss of its anti-protease activity and to the appearance of an endonuclease activity. However no catalytic site was identified.
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TMPY-01249 | Cathepsin V Protein, Human, Recombinant (His) | Human | HEK293 | ||
Cathepsin V (CTSV), also known as Cathepsin L2, CTSL2, and CATL2, is a member of the peptidase C1 family. It is predominantly expressed in the thymus and testis. Cathepsin V is also expressed in corneal epithelium, and to a lesser extent in conjuctival epithelium and skin. It is a lysosomal cysteine proteinase that may play an important role in corneal physiology. It has about 75% protein sequence identity to murine cathepsin L. The fold of this enzyme is similar to the fold adopted by other members of the papain superfamily of cysteine proteases. Cathepsin V has been recently described as highly homologous to Cathepsin L and exclusively expressed in human thymus and testis. Cathepsin V is the dominant cysteine protease in cortical human thymic epithelial cells, while Cathepsin L and Cathepsin S seem to be restricted to dendritic and macrophage-like cells. Active Cathepsin V in thymic lysosomal preparations was demonstrated by active-site labeling. Recombinant Cathepsin V was capable of converting Ii into CLIP efficiently, suggesting that it is the protease that controls the generation of alphabeta-CLIP complexes in the human thymus. Cathepsin V is the third elastolytic cysteine protease which exhibits the most potent elastase activity yet described among human proteases and that it is present in atherosclerotic plaque specimens. Cathepsin L2 may play a specialized role in the thymus and testis. Expression analysis of cathepsin L2 in human tumors revealed a widespread expression in colorectal and breast carcinomas but not in normal colon or mammary gland or in peritumoral tissues. Cathepsin L2 was also expressed by colorectal and breast cancer cell lines as well as by some tumors of diverse origin, including ovarian and renal carcinomas.
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