目录号 | 产品详情 | 靶点 | |
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T35667 | |||
Napyradiomycin A1is a fungal metabolite originally isolated fromC. rubraand has diverse biological activities.1,2It is active againstS. aureus,M. luteus,B. anthracis,C. bovis, andM. smegmatis(MICs = 1.56-12.5 μg/ml).1Napyradiomycin A1is an estrogen receptor antagonist (IC50= 4.2 μM in rat uterine homogenates).2It also inhibits mitochondrial NADH:ubiquinone oxidoreductase (complex I) and succinate:ubiquinone oxidoreductase (complex II) activities in bovine heart homogenates (IC50s = 20 and 9.7 μM, respectively).3 1.Shiomi, K., Iinuma, H., Hamada, M., et al.Novel antibiotics napyradiomycins. Production, isolation, physico-chemical properties and biological activityJ. Antibiot. (Tokyo)39(4)487-493(1986) 2.Hori, Y., Abe, Y., Shigematsu, N., et al.Napyradiomycins A and B1: Non-steroidal estrogen-receptor antagonists produced by a StreptomycesJ. Antibiot. (Tokyo)46(12)1890-1893(1993) 3.Yamamoto, K., Tashiro, E., Motohashi, K., et al.Napyradiomycin A1, an inhibitor of mitochondrial complexes I and IIJ. Antibiot. (Tokyo)65(4)211-214(2012) | |||
T36456 | |||
12-hydroxy Stearic acid is a hydroxy fatty acid produced by the hydrogenation of ricinoleic acid .1It is a low molecular weight gelator that self-assembles to form organogels.2Administration of paclitaxel in 12-hydroxy stearic acid-containing gel nanocarriers enhances tumor growth suppression in an H22 murine hepatocellular carcinoma model.3Formulations containing 12-hydroxy stearic acid have been used in cosmetic products as emollients. 1.Fameau, A.-L., and Rogers, M.A.The curious case of 12-hydroxystearic acid — the Dr. Jekyll & Mr. Hyde of molecular gelatorsCurr. Opin. Colloid Interface Sci.4568-82(2020) 2.Burkhardt, M., Noirez, L., and Gradzielski, M.Organogels based on 12-hydroxy stearic acid as a leitmotif: Dependence of gelation properties on chemical modificationsJ. Colloid Interface Sci.466369-376(2016) 3.He, W., Lv, Y., Zhao, Y., et al.Core-shell structured gel-nanocarriers for sustained drug release and enhanced antitumor effectInt. J. Pharm.484(1-2)163-171(2015) | |||
T35978 | |||
Benastatin A is a polyketide synthase-derived benastatin that has been found inStreptomycesand has diverse biological activities.1,2,3It inhibits glutathione S-transferase (GST; Ki= 5 μM for the rat liver enzyme).2Benastatin A is active against several bacteria, including methicillin-resistantS. aureus(MRSA; MIC = 3.12 μg/ml). It induces apoptosis and cell cycle arrest at the G1/G0phase in Colon 26 mouse colon cancer cells when used at concentrations of 20 and 16 μM, respectively.3 1.Xu, Z., Schenk, A., and Hertweck, C.Molecular analysis of the benastatin biosynthetic pathway and genetic engineering of altered fatty acid-polyketide hybridsJ. Am. Chem. Soc.129(18)6022-6030(2007) 2.Aoyagi, T., Aoyama, T., Kojima, F., et al.Benastatins A and B, new inhibitors of glutathione S-transferase, produced by Streptomyces sp. MI384-DF12. I. Taxonomy, production, isolation, physico-chemical properties and biological activitiesJ. Antibiot. (Tokyo)45(9)1385-1390(1992) 3.Kakizaki, I., Ookawa, K., Ishikawa, T., et al.Induction of apoptosis and cell cycle arrest in mouse colon 26 cells by benastatin AJpn. J. Cancer Res.91(11)1161-1168(2000) | |||
T35752 | |||
Xanthoquinodin A1 is a fungal metabolite that has been found inHumicolaand has diverse biological activities.1,2It inhibitsE. tenellaschizont formation in BHK-21 cells with a minimum effective concentration (MEC) value of 0.02 μg/ml.1Xanthoquinodin A1 is active againstB. subtilis,M. luteus,S. aureus,A. laidlawii, andB. fragilisin a disc assay when used at a concentration of 1 mg/ml. It is also active againstB. cereus(MIC = 0.44 μM).2Xanthoquinodin A1 is cytotoxic to KB, MCF-7, and NCI H187 cancer cells. 1.Tabata, N., Suzumura, Y., Tomoda, H., et al.Xanthoquinodins, new anticoccidial agents produced by Humicola sp. Production, isolation and physico-chemical and biological propertiesJ. Antibiot. (Tokyo)46(5)749-755(1993) 2.Tantapakul, C., Promgool, T., Kanokmedhakul, K., et al.Bioactive xanthoquinodins and epipolythiodioxopiperazines from Chaetomium globosum 7s-1, an endophytic fungus isolated from Rhapis cochinchinensis (Lour.) MartNat. Prod. Res.34(4)494-502(2020) | |||
T35771 | |||
Destruxin B2 is a cyclic hexadepsipeptide mycotoxin that has been found in M. anisopliae and has antiviral, insecticidal, and phytotoxic activities.1,2,3 It inhibits secretion of hepatitis B virus surface antigen (HBsAg) by Hep3B cells expressing hepatitis B virus (HBV) DNA (IC50 = 1.3 μM).1 Destruxin B2 is toxic to Sf9 insect cells in an electric cell-substrate impedance sensing (ECIS) test with a 50% inhibitory concentration (ECIS50) value of 92 μM.4 It is also phytotoxic to B. napus leaves.3 |1. Yeh, S.F., Pan, W., Ong, G.-T., et al. Study of structure-activity correlation in destruxins, a class of cyclodepsipeptides possessing suppressive effect on the generation of hepatitis B virus surface antigen in human hepatoma cells. Biochem. Biophys. Res. Commun. 229(1), 65-72 (1996).|2. Male, K.B., Tzeng, Y.-M., Montes, J., et al. Probing inhibitory effects of destruxins from Metarhizium anisopliae using insect cell based impedance spectroscopy: Inhibition vs chemical structure. Analyst 134(7), 1447-1452 (2009).|3. Buchwaldt, L., and Green, H. Phytotoxicity of destruxin B and its possible role in the pathogenesis of Alternaria brassicae. Plant Pathol. 41(1), 55-63 (1992). | |||
T35892 | |||
Q134R, a neuroprotective hydroxyquinoline derivative that suppresses nuclear factor of activated T cell (NFAT) signaling. Q134R can across blood-brain barrier. Q134R has the potential for Alzheimer’s disease (AD) and aging-related disorders research[1]. Q134R (1-10 μM) suppresses NFAT signaling, without inhibiting calcineurin activity. Q134R partially inhibits NFAT activity in primary rat astrocytes, but does not prevent calcineurin-mediated dephosphorylation of a non-NFAT target, either in vivo, or in vitro[1]. Q134R (4 mg/kg; orally gavage; twice per day; for 7 days) treatment improves cognitive function in rodent models of AD‐like pathology[1]. [1]. Pradoldej Sompol, et al. Q134R: Small chemical compound with NFAT inhibitory properties improves behavioral performance and synapse function in mouse models of amyloid pathology. Aging Cell. 2021 Jul;20(7):e13416. | |||
T38280 | |||
C22 dihydro 1-Deoxyceramide (m18:0/22:0) is a very long-chain atypical ceramide containing a 1-deoxysphinganine backbone. 1-Deoxysphingolipids are formed when serine palmitoyltransferase condenses palmitoyl-CoA with alanine instead of serine during sphingolipid synthesis.1,2 C22 dihydro 1-Deoxyceramide (m18:0/22:0) has been found in mouse embryonic fibroblasts (MEFs) following application of 1-deoxysphinganine alkyne or 1-deoxysphinganine-d3.3 It has also been found as the most prevalent dihydro deoxyceramide species in mouse brain, spinal cord, and sciatic nerve at one, three, and six months of age.4 |1. Steiner, R., Saied, E.M., Othman, A., et al. Elucidating the chemical structure of native 1-deoxysphingosine. J. Lipid Res. 57(7), 1194-1203 (2016).|2. Alecu, I., Othman, A., Penno, A., et al. Cytotoxic 1-deoxysphingolipids are metabolized by a cytochrome P450-dependent pathway. J. Lipid Res. 58(1), 60-71 (2017).|3. Alecu, I., Tedeschi, A., Behler, N., et al. Localization of 1-deoxysphingolipids to mitochondria induces mitochondrial dysfunction. J. Lipid. Res. 58(1), 42-59 (2017).|4. Schwartz, N.U., Mileva, I., Gurevich, M., et al. Quantifying 1-deoxydihydroceramides and 1-deoxyceramides in mouse nervous system tissue. Prostaglandins Other Lipid Mediat. 141, 40-48 (2019). | |||
T38284 | |||
C24 dihydro 1-Deoxyceramide (m18:0/24:0) is a very long-chain atypical ceramide containing a 1-deoxysphinganine backbone. 1-Deoxysphingolipids are formed when serine palmitoyltransferase condenses palmitoyl-CoA with alanine instead of serine during sphingolipid synthesis.1,2 C24 dihydro 1-Deoxyceramide (m18:0/24:0) has been found in mouse embryonic fibroblasts (MEFs) following application of 1-deoxysphinganine alkyne or 1-deoxysphinganine-d3.3 It has also been found in mouse brain, spinal cord, and sciatic nerve at one, three, and six months of age.4 |1. Steiner, R., Saied, E.M., Othman, A., et al. Elucidating the chemical structure of native 1-deoxysphingosine. J. Lipid Res. 57(7), 1194-1203 (2016).|2. Alecu, I., Othman, A., Penno, A., et al. Cytotoxic 1-deoxysphingolipids are metabolized by a cytochrome P450-dependent pathway. J. Lipid Res. 58(1), 60-71 (2017).|3. Alecu, I., Tedeschi, A., Behler, N., et al. Localization of 1-deoxysphingolipids to mitochondria induces mitochondrial dysfunction. J. Lipid. Res. 58(1), 42-59 (2017).|4. Schwartz, N.U., Mileva, I., Gurevich, M., et al. Quantifying 1-deoxydihydroceramides and 1-deoxyceramides in mouse nervous system tissue. Prostaglandins Other Lipid Mediat. 141, 40-48 (2019). | |||
T37736 | |||
Quorum sensing is a regulatory process used by bacteria for controlling gene expression in response to increasing cell density.[1] This regulatory process manifests itself with a variety of phenotypes including biofilm formation and virulence factor production.[2] Coordinated gene expression is achieved by the production, release, and detection of small diffusible signal molecules called autoinducers. The N-acylated homoserine lactones (AHLs) comprise one such class of autoinducers, each of which generally consists of a fatty acid coupled with homoserine lactone (HSL). AHLs vary in acyl group length (C4-C18), in the substitution of C3 (hydrogen, hydroxyl, or oxo group) and in the presence or absence of one or more carbon-carbon double bonds in the fatty acid chain. These differences confer signal specificity through the affinity of transcriptional regulators of the LuxR family.[3] C16:1-Δ9-(L)-HSL is a long-chain AHL that functions as a quorum sensing signaling molecule in strains of S. meliloti.[4],[5],[6],[7] Regulating bacterial quorum sensing signaling can be used to inhibit pathogenesis and thus, represents a new approach to antimicrobial therapy in the treatment of infectious diseases.[8] Reference:[1]. González, J.E., and Keshavan, N.D. Messing with bacterial quorum sensing. Microbiol. Mol. Biol. Rev. 70(4), 859-875 (2006).[2]. Gould, T.A., Herman, J., Krank, J., et al. Specificity of acyl-homoserine lactone syntheses examined by mass spectrometry. J. Bacteriol. 188(2), 773-783 (2006).[3]. Penalver, C.G.N., Morin, D., Cantet, F., et al. Methylobacterium extorquens AM1 produces a novel type of acyl-homoserine lactone with a double unsaturated side chain under methylotrophic growth conditions. FEBS Lett. 580(2), 561-567 (2006).[4]. Teplitski, M., Eberhard, A., Gronquist, M.R., et al. Chemical identification of N-acyl homoserine lactone quorum-sensing signals produced by Sinorhizobium meliloti strains in defined medium. Archives of Microbiology 180, 494-497 (2003).[5]. Gao, M., Chen, H., Eberhard, A., et al. sinI- and expR-dependent quorum sensing in Sinorhizobium meliloti. Journal of Bacteriology 187(23), 7931-7944 (2005).[6]. Marketon, M.M., Glenn, S.A., Eberhard, A., et al. Quorum sensing controls exopolysaccharide production in Sinorhizobium meliloti. Journal of Bacteriology 185(1), 325-331 (2003).[7]. Marketon, M., Gronquist, M.R., Eberhard, A., et al. Characterization of the Sinorhizobium meliloti sinR/sinI locus and the production of novel N-Acyl homoserine lactones. Journal of Bacteriology 184(20), 5686-5695 (2002).[8]. Cegelski, L., Marshall, G.R., Eldridge, G.R., et al. The biology and future prospects of antivirulence therapies. Nat. Rev. Microbiol. 6(1), 17-27 (2008). | |||
T37741 | |||
Quorum sensing is a regulatory system used by bacteria for controlling gene expression in response to increasing cell density.[1] This regulatory process manifests itself with a variety of phenotypes including biofilm formation and virulence factor production.[2] Coordinated gene expression is achieved by the production, release, and detection of small diffusible signal molecules called autoinducers. The N-acylated homoserine lactones (AHLs) comprise one such class of autoinducers, each of which generally consists of a fatty acid coupled with homoserine lactone (HSL). Regulation of bacterial quorum sensing signaling systems to inhibit pathogenesis represents a new approach to antimicrobial therapy in the treatment of infectious diseases.[3] AHLs vary in acyl group length (C4-C18), in the substitution of C3 (hydrogen, hydroxyl, or oxo group), and in the presence or absence of one or more carbon-carbon double bonds in the fatty acid chain. These differences confer signal specificity through the affinity of transcriptional regulators of the LuxR family.[4] C16-HSL is one of a number of lipophilic, long acyl side-chain bearing AHLs, including its monounsaturated analog C16:1-(L)-HSL, produced by the LuxI AHL synthase homolog SinI involved in quorum-sensing signaling in S. meliloti, a nitrogen-fixing bacterial symbiont of certain legumes.[5],[6] C16-HSL is the most abundant AHL produced by the proteobacterium R. capsulatus and activates genetic exchange between R. capsulatus cells.[7] N-Hexadecanoyl-L-homoserine lactone and other hydrophobic AHLs tend to localize in relatively lipophilic cellular environments of bacteria and cannot diffuse freely through the cell membrane. The long-chain N-acylhomoserine lactones may be exported from cells by efflux pumps or may be transported between communicating cells by way of extracellular outer membrane vesicles.[8],[9]Reference:[1]. González, J.E., and Keshavan, N.D. Messing with bacterial quorum sensing Microbiol. Mol. Biol. Rev. 70(4), 859-875 (2006).[2]. Gould, T.A., Herman, J., Krank, J., et al. Specificity of acyl-homoserine lactone syntheses examined by mass spectrometry Journal of Bacteriology 188(2), 773-783 (2006).[3]. Cegelski, L., Marshall, G.R., Eldridge, G.R., et al. The biology and future prospects of antivirulence therapies Nature Reviews.Microbiology 6(1), 17-27 (2008).[4]. Penalver, C.G.N., Morin, D., Cantet, F., et al. Methylobacterium extorquens AM1 produces a novel type of acyl-homoserine lactone with a double unsaturated side chain under methylotrophic growth conditions FEBS Letters 580, 561-567 (2006).[5]. Gao, M., Chen, H., Eberhard, A., et al. sinI- and expR-dependent quorum sensing in Sinorhizobium meliloti Journal of Bacteriology 187(23), 7931-7944 (2005).[6]. Teplitski, M., Eberhard, A., Gronquist, M.R., et al. Chemical identification of N-acyl homoserine lactone quorum-sensing signals produced by Sinorhizobium meliloti strains in defined medium Archives of Microbiology 180, 494-497 (2003).[7]. Schaefer, A.L., Taylor, T.A., Beatty, J.T., et al. Long-chain acyl-homoserine lactone quorum-sensing regulation of Rhodobacter capsulatus gene transfer agent production Journal of Bacteriology 184(23), 6515-6521 (2002).[8]. Pearson, J.P., Van Delden, C., and Iglewski, B.H. Active efflux and diffusion are involved in transport of Pseudomonas aeruginosa cell-to-cell signals Journal of Bacteriology 181(4), 1203-1210 (1999).[9]. Mashburn-Warren, L., and Whiteley, M. Special delivery: Vesicle trafficking in prokaryotes Molecular Microbiology 61(4), 839-846 (2006). |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-02483 | ATP citrate lyase/ACLY Protein, Human, Recombinant (His) | Human | Baculovirus Insect Cells | ||
ATP citrate lyase, also known as Acly or Acl, is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. The enzyme is composed of two polymer chains which are polypeptides in human. ATP citrate lyase is responsible for catalyzing the conversion of citrate and CoA into acetyl-CoA and oxaloacetate, along with the hydrolysis of ATP. A definitive role for ATP citrate lyase in tumorigenesis has emerged from ATP citrate lyase RNAi and chemical inhibitor studies, showing that ATP citrate lyase inhibition limits tumor cell proliferation and survival and induces differentiation in vitro. In vivo, it reduces tumor growth leading to a cytostatic effect and induces differentiation.
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TMPH-00290 | Odorant-binding Protein, Bovine, Recombinant | Bovine | E. coli | ||
This protein binds a wide variety of chemical odorants. Odorant-binding Protein, Bovine, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 18.5 kDa and the accession number is P07435.
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TMPH-00291 | Odorant-binding Protein, Bovine, Recombinant (His & SUMOstar) | Bovine | P. pastoris (Yeast) | ||
This protein binds a wide variety of chemical odorants. Odorant-binding Protein, Bovine, Recombinant (His & SUMOstar) is expressed in yeast with N-6xHis-sumostar tag. The predicted molecular weight is 34.5 kDa and the accession number is P07435.
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TMPK-01370 | GRP-10 proform Protein, Canine, Recombinant (hFc) | Canine | HEK293 Cells | ||
Gastrin-releasing peptide (GRP) is a neuropeptide with growth-stimulatory and tumorigenic properties, and neuropeptides have previously been suggested to play a role in the complex cascade of chemical activity associated with periodontal inflammation.
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TMPH-03120 | OBP Protein, Pig, Recombinant (His & Myc) | Sus scrofa (Pig) | E. coli | ||
This protein is found in nasal epithelium and it binds a wide variety of chemical odorants. OBP Protein, Pig, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 25.2 kDa and the accession number is P81245.
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TMPY-05066 | IVD Protein, Mouse, Recombinant (His) | Mouse | Baculovirus Insect Cells | ||
IVD (Isovaleryl-CoA Dehydrogenase) is a Protein Coding gene. IVD is a mitochondrial matrix enzyme that catalyzes the third step in leucine catabolism. IVD plays an essential role in processing proteins obtained from the diet. The body breaks down proteins from food into smaller parts called amino acids. Amino acids can be further processed to provide energy for growth and development. Isovaleryl-CoA dehydrogenase helps process a particular amino acid called leucine. Specifically, isovaleryl-CoA dehydrogenase is responsible for the third step in the breakdown of leucine. This step is a chemical reaction that converts a molecule called isovaleryl-CoA to another molecule, 3-methylcrotonyl-CoA. Additional chemical reactions convert 3-methylcrotonyl-CoA into molecules that are used for energy.
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TMPJ-00872 | MGMT Protein, Human, Recombinant (His) | Human | E. coli | ||
MGMT belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. MGMT involved in the cellular defense against the biological effects of O6-methylguanine in DNA. Repairs alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the O-6 position to a cysteine residue in the enzyme. MGMT catalyzes the chemical reaction: DNA (containing 6-O-methylguanine) and proteinL-cysteine into DNA (without 6-O-methylguanine) and protein S-methyl-L-cysteine.
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TMPJ-00297 | SHPK Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Sedoheptulokinase (SHPK) belongs to the FGGY kinase family, and is mainly located in cytoplasm. SHPK is strongly expressed in liver, kidney and pancreas. It is expressed at lower levels in placenta and heart, and very weakly expressed in lung and brain. SHPK catalyzes the chemical reaction: ATP + sedoheptulose = ADP + sedoheptulose 7-phosphatecan, It can transform sedoheptulose to sedoheptulose 7-phosphate in the condition of ATP, and acts as a modulator of macrophage activation through control of glucose metabolism. In addition, It also can be down-regulated by LPS.
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TMPJ-00565 | Mucin-15/MUC15 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Mucin-15 is a single-pass type I membrane protein member of the Mucin family. Mucins are a family of high molecular weight, heavily glycosylated proteins (glycoconjugates) produced by epithelial tissues in most metazoans. A key characteristic of Mucins is their ability to form gels. Therefore they are a key component in most gel-like secretions, serving functions from lubrication to cell signalling to forming chemical barriers. Mucin-15 is expressed in many tissues. Mucin-15 is highly glycosylated (N- and O-linked carbohydrates). Mucin-15 may play a role in the cell adhesion to the extracellular matrix.
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TMPJ-00727 | PGK1 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Phosphoglycerate kinase 1(PGK1) is an enzyme. It is mainly expressed in spermatogonia and Localized on the principle piece in the sperm. Its expression significantly decreased in the testis of elderly men. PGK1 involved in a critical energy-producing process known as glycolysis. It helps carry out a chemical reaction that converts a molecule called 1,3-diphosphoglycerate, which is produced during the breakdown of glucose, to another molecule called 3-phosphoglycerate during glycolysis. PGK1 may also act as a cofactor for polymerase alpha. The protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions.
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TMPH-02669 | GJA1 Protein, Mouse, Recombinant (His & Myc) | Mouse | Baculovirus Insect Cells | ||
Gap junction protein that acts as a regulator of bladder capacity. A gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. Negative regulator of bladder functional capacity: acts by enhancing intercellular electrical and chemical transmission, thus sensitizing bladder muscles to cholinergic neural stimuli and causing them to contract. May play a role in cell growth inhibition through the regulation of NOV expression and localization. Plays an essential role in gap junction communication in the ventricles.; Connexin 43 is possibly the ATP-induced pore of mouse macrophages.
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TMPJ-00554 | Vinculin Protein, Human, Recombinant | Human | E. coli | ||
Vinculin is a focal adhesion and cytoskeletal protein that distributed mainly at cell-cell junctions and cell-extracellular matrix (ECM) adhesion that belongs to the Vinculin/α-Catenin family. Vinculin is an Actin-binding protein and component of the Actin-Linking Functional module that senses and feels the mechanical properties of the extracellular environment. Vinculin is also a key factor that couples, transmits, transduces, and regulates mechanical force between the cytoskeleton and adhesion receptors. Vinculin generally forms two structural states, an open (active) and closed (inactive) state, which are controlled by conformational interaction(s) between the head and tail domains. Vinculin is involved in the mechano-chemical signal transmission of cells by binding to a variety of focal adhesion or cytoskeletal proteins, and plays important roles in cell adhesion, extension, motion, proliferation and survival.
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TMPY-02452 | CMBL Protein, Human, Recombinant (His) | Human | E. coli | ||
Carboxymethylenebutenolidase (CMBL), also known as 4-carboxymethylenebut-2-en-4-olide lactonohydrolase, maleylacetate enol- lactonase, dienelactone hydrolase, and carboxymethylene butenolide hydrolase, is a hydrolase specially belonging to the family of hydrolases. It maily acts on carboxylic ester bonds. CMBL is a human homolog of Pseudomonas dienelactone hydrolase involved in the bacterial halocatechol degradation pathway. The ubiquitous expression of human CMBL gene transcript in various tissues was observed. CMBL was demonstrated to be the primary olmesartan medoxomil (OM) bioactivating enzyme in the liver and intestine. The recombinant human CMBL expressed in mammalian cells was clearly shown to activate OM. The recombinant CMBL also converted other prodrugs having the same ester structure as OM, faropenem medoxomil and lenampicillin, to their active metabolites. CMBL exhibited a unique sensitivity to chemical inhibitors, thus, being distinguishable from other known esterases.
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TMPY-03962 | AFM Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Afamin is an 87 kDa glycoprotein with five predicted N-glycosylation sites. Afamin's glycan abundance contributes to conformational and chemical inhomogeneity presenting great challenges for molecular structure determination. Afamin, a human plasma glycoprotein and putative transporter of hydrophobic molecules, has been shown to act as extracellular chaperone for poorly soluble, acylated Wnt proteins, forming a stable, soluble complex with functioning Wnt proteins. The 2.1-Å crystal structure of glycosylated human afamin reveals an almost exclusively hydrophobic binding cleft capable of harboring large hydrophobic moieties. Afamin plays a role in anti-apoptotic cellular processes related to oxidative stress and is associated with insulin resistance and other features of metabolic syndrome. Afamin may serve as a new early biomarker for pathological glucose metabolism during pregnancy. And first trimester screening for pre-eclampsia could be provided by a combination of afamin and placental bed vascularization. Moreover, the combination of first trimester serum afamin levels with BMI could provide a possible screening for gestational diabetes mellitus.
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TMPY-04070 | Citrate Synthase Protein, Human, Recombinant (His) | Human | Baculovirus Insect Cells | ||
Chondroitin sulphate (CS) glycosaminoglycan chains on cell and extracellular matrix proteoglycans (PGs) can no longer be regarded as merely hydrodynamic space fillers. Overwhelming evidence over recent years indicates that sulphation motif sequences within the CS chain structure are a source of significant biological information to cells and their surrounding environment. CS sulphation motifs have been shown to interact with a wide variety of bioactive molecules, e.g. cytokines, growth factors, chemokines, morphogenetic proteins, enzymes and enzyme inhibitors, as well as structural components within the extracellular milieu. They are therefore capable of modulating a panoply of signalling pathways, thus controlling diverse cellular behaviours including proliferation, differentiation, migration and matrix synthesis. Chondroitin sulfate (CS) is a sulfated glycosaminoglycan composed of a long chain of repeating disaccharide units that are attached to core proteins, resulting in CS proteoglycans (CSPGs). In the mature brain, CS is concentrated in perineuronal nets (PNNs), which are extracellular structures that surround synapses and regulate synaptic plasticity. In addition, CS is rapidly synthesized after CNS injury to create a physical and chemical barrier that inhibits axon growth.
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TMPY-01742 | Acetylcholinesterase Protein, Mouse, Recombinant (His) | Mouse | HEK293 Cells | ||
Acetylcholinesterase, also known as ACHE, is an enzyme that degrades (through its hydrolytic activity) the neurotransmitter acetylcholine, producing choline and an acetate group. Acetylcholinesterase plays a crucial role in nerve impulse transmission at cholinergic synapses by rapid hydrolysis of the neurotransmitter acetylcholine (ACh). ACHE appears to be a potential therapeutic target at muscle injuries including organophosphate myopathy. It is an externally oriented membrane-bound enzyme and its main physiological role is termination of chemical transmission at cholinergic synapses and secretory organs by rapid hydrolysis of the neurotransmitter acetylcholine (ACh). ACHE plays important roles in the cholinergic system, and its dysregulation is involved in a variety of human diseases. ACHE was significantly down-regulated in the cancerous tissues of 69.2% of hepatocellular carcinoma (HCC) patients, and the low ACHE expression in HCC was correlated with tumor aggressiveness, an elevated risk of postoperative recurrence, and a low survival rate. Both the recombinant ACHE protein and the enhanced expression of ACHE significantly inhibited HCC cell growth in vitro and tumorigenicity in vivo. ACHE as a tumor growth suppressor in regulating cell proliferation, the relevant signaling pathways, and the drug sensitivity of HCC cells. Thus, ACHE is a promising independent prognostic predictor for HCC recurrence and the survival of HCC patients. ACHE is responsible for the hydrolysis of acetylcholine in the nervous system. It is inhibited by organophosphate and carbamate pesticides. However, this enzyme is only slightly inhibited by organophosphorothionates.
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TMPY-01679 | LCN1 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Lipocalin-1, also known as Von Ebner gland protein, VEG protein, Tear Prealbumin, VEGP, Tear lipocalin, and LCN1 is a secreted protein that belongs to the calycin superfamily and Lipocalin family. Human Lipocalin-1 / VEGP was originally described as a major protein of human tear fluid, which was thought to be tear specific. Lipocalin-1 / VEGP is identical to lingual von Ebner's gland protein and is also produced in the prostate, nasal mucosa, and tracheal mucosa. Homologous proteins have been found in the rat, pig, and probably dog and horse. Lipocalin-1 / VEGP is an unusual lipocalin member, because of its high promiscuity for relative insoluble lipids and binding characteristics that differ from other members. Lipocalin-1 / VEGP acts as the principal lipid-binding protein in tear fluid, a more general physiological function has to be proposed due to its wide distribution and properties. Lipocalin-1 / VEGP would be ideally suited for scavenging of lipophilic, potentially harmful substances and thus might act as a general protection factor of epithelia. Lipocalin-1 / LCN1 could play a role in taste reception. It could be necessary for the concentration and delivery of sapid molecules in the gustatory system. Lipocalin-1 / LCN1 can bind various ligands, with chemical structures ranging from lipids and retinoids to the macrocyclic antibiotic rifampicin and even to microbial siderophores. It exhibits an extremely wide ligand pocket.
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