目录号 | 产品详情 | 靶点 | |
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T75967 | |||
Bactenecin TFA (Bactenecin, bovine TFA) 是一种从牛嗜中性粒细胞中分离出来的有效的含 12 个氨基酸的环状抗菌肽。Bactenecin TFA 抑制细菌和酵母菌 (bacteria 和 yeast) 的生长,并能杀死真菌红毛癣菌 (fungusTrichophyton rubrum)。Bactenecin TFA 增加了膜的通透性,抑制了假苹果芽孢杆菌 (B. pseudomallei) 的生长和生物膜的形成。 | |||
T83693 | |||
Magainin 2是一种从非洲爪蟾(X. laevis)皮肤中分离出的阳离子肽,具有宿主防御和抗菌活性。该化合物对细菌E. coli、K. pneumoniae、S. epidermidis、S. aureus及真菌C. albicans表现出活性(MICs分别为5、10、10、50和80 µg/ml)。Magainin 2(20 µM)能降低猕猴桃花粉的萌发率和平均管长。在被单纯疱疹病毒1型(HSV-1)或2型(HSV-2)感染的Vero细胞中,它可减少病毒复制(EC50s分别为22.16和19.8 µM),同时不影响细胞活性,其50%细胞毒性浓度值(CC50)大于100 µM。 | |||
T37880 | |||
OPC-167832 is a potent and orally active dprE1 Inhibitor with an IC50 of 0.258 μM. OPC-167832 has antituberculosis activity and can be used for the research of tuberculosis caused by Mycobacterium tuberculosis[1]. OPC-167832 exhibits very low MICs against laboratory strains of M. tuberculosis H37Rv (MIC: 0.0005 μg/ml) and Kurono (MIC: 0.0005 μg/ml) and strains with monoresistance to rifampin (RIF), isoniazid (INH), ethambutol (EMB), streptomycin (STR), and pyrazinamide (PZA) (MIC: 0.00024-0.001 μg/ml). However, OPC-167832 has minimal or no activity against standard strains of nonmycobacterial aerobic and anaerobic bacteria[1].The IC90 values of OPC-167832 against intracellular M. tuberculosis strains H37Rv and Kurono are 0.0048 and 0.0027 μg/ml, respectively. OPC-167832 shows bactericidal activity against intracellular M. tuberculosis at a low concentration, and the bactericidal activity is saturated at concentrations of 0.004 μg/ml or higher[1]. OPC-167832 (oral administration; 0.625-10 mg/kg) exhibits a good pharmacokinetic characteristic. The plasma reaches peak at 0.5 h to 1.0 h (tmax) and is eliminated with a half-life (t1/2) of 1.3 h to 2.1 h OPC-167832 distribution in the lungs is approximately 2 times higher than that in plasma, and the Cmax and AUCt of OPC-167832 in plasma and the lungs shows dose dependency[1].OPC-167832 (oral administration; 0.625-10 mg/kg; 4 weeks) significantly reduces lung CFU compared to the vehicle group. The dose-dependent decrease of lung CFU is observed from 0.625 mg/kg to 2.5 mg/kg. In a M. tuberculosis Kurono-infected ICR female mice model. OPC-167832 combines with DMD, BDQ, or LVX via oral gavage exhibits significantly higher efficacies than each single agent alone[1].[1].OPC-167832 (oral gavage; 2.5 mg/kg; combination with DCMB; 12 weeks) demonstrates the most potent efficacy when compares with DC, DCB. The lung CFU count after 6 weeks of treatment is below the detection limit, and at the end of just 8 weeks of treatment, the bacteria in the lungs of all the evaluated mice had already been eradicate[1]. [1]. Norimitsu Hariguchi, et al. OPC-167832, a Novel Carbostyril Derivative with Potent Antituberculosis Activity as a DprE1 Inhibitor.Antimicrob Agents Chemother. 2020 May 21;64(6):e02020-19. | |||
T35624 | |||
Ajoene is a disulfide that has been found inA. sativumand has diverse biological activities, including antibacterial, anticancer, antiplatelet, and antioxidant properties.1,2,3,4It is active against Gram-positive (MICs = 5-160 µg/ml) and Gram-negative bacteria (MICs = 136-200 µg/ml), as well as yeasts (MICs = 10-20 µg/ml).1Ajoene is cytotoxic to mouse melanoma cells (IC50= 18 µM), as well as human colon, lung, mammary, and pancreatic cancer cells (IC50s = 7-41 µM).2It reduces tumor growth in a B16/BL6 mouse model of melanoma when administered at a dose of 25 mg/kg every other day and decreases the number of lung metastases when administered prior to tumor cell inoculation at doses ranging from 1-25 mg/kg. It inhibits ADP- or collagen-induced platelet aggregation in isolated baboon platelets when used at concentrations ranging from 75 to 150 µg/ml and in platelet-rich plasma isolated from baboons when administered at a dose of 25 mg/kg.3Ajoene (25 mg/kg) prevents thrombus formation on damaged arterial walls in heparinized pigs in anin situmodel of thrombogenesis.5It also reduces high-fat diet-induced hepatic steatosis, histopathological markers of liver damage, thiobarbituric acid reactive substances (TBARS) formation, and protein oxidation in a mouse model of non-alcoholic fatty liver disease (NAFLD).4 1.Naganawa, R., Iwata, N., Ishikawa, K., et al.Inhibition of microbial growth by ajoene, a sulfur-containing compound derived from garlicAppl. Environ. Microbiol.62(11)4238-4242(1996) 2.Taylor, P., Noriega, R., Farah, C., et al.Ajoene inhibits both primary tumor growth and metastasis of B16/BL6 melanoma cells in C57BL/6 miceCancer Lett.239(2)298-304(2006) 3.Teranishi, K., Apitz-Castro, R., Robson, S.C., et al.Inhibition of baboon platelet aggregation in vitro and in vivo by the garlic derivative, ajoeneXenotransplantation10(4)374-379(2003) 4.Han, C.Y., Ki, S.H., Kim, Y.W., et al.Ajoene, a stable garlic by-product, inhibits high fat diet-induced hepatic steatosis and oxidative injury through LKB1-dependent AMPK activationAntioxid. Redox Signal.14(2)187-202(2011) 5.Apitz-Castro, R., Badimon, J.J., and Badimon, L.A garlic derivative, ajoene, inhibits platelet deposition on severely damaged vessel wall in an in vivo porcine experimental modelThromb. Res.75(3)243-249(1994) | |||
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). |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPH-00516 | StxA2 Protein, Enterobacteria phage 933W, Recombinant (E189K, His & Myc) | Enterobacteria phage 933W | E. coli | ||
The A subunit is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits. After endocytosis, the A subunit is cleaved by furin in two fragments, A1 and A2: A1 is the catalytically active fragment, and A2 is essential for holotoxin assembly with the B subunits.
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TMPH-00526 | Endolysin Protein, Enterobacteria phage T4, Recombinant (His & SUMO) | Enterobacteria phage T4 | E. coli | ||
Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.
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TMPH-00524 | ATP-dependent DNA helicase dda Protein, Enterobacteria phage T4, Recombinant (His) | Enterobacteria phage T4 | E. coli | ||
DNA helicase that stimulates viral DNA replication and recombination. Plays a role in T4 DNA replication initiation by selecting and activating DNA origins. Acts by dissociating and reassociating with the DNA molecule being unwound. Unwinds DNA as a monomer in a 5'-to-3' direction at a rate of 250 bp/s and can efficiently displace proteins from the DNA.
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TMPH-00529 | UvsY Protein, Enterobacteria phage T4, Recombinant (Avi & His) | Enterobacteria phage T4 | E. coli | ||
Plays a role in viral DNA synthesis by promoting enzymatic activities of UvsX recombinase, by promoting UvsX-ssDNA filament assembly, and by helping UvsX to displace bound gp32 from ssDNA.
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TMPH-00533 | T7 RNA polymerase Protein, Enterobacteria phage T7, Recombinant (His & Myc) | Escherichia phage T7 | E. coli | ||
Highly processive DNA-dependent RNA polymerase that catalyzes the transcription of class II and class III viral genes. Recognizes a specific promoter sequence and enters first into an 'abortive phase' where very short transcripts are synthesized and released before proceeding to the processive transcription of long RNA chains. Unwinds the double-stranded DNA to expose the coding strand for templating. Participates in the initiation of viral DNA replication presumably by making primers accessible to the DNA polymerase, thus facilitating the DNA opening. Plays also a role in viral DNA packaging, probably by pausing the transcription at the right end of concatemer junction to allow packaging complex recruitment and beginning of the packaging process.
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TMPH-00518 | StxB2 Protein, Enterobacteria phage 933W, Recombinant (His & SUMO) | Enterobacteria phage 933W | E. coli | ||
The B subunit is responsible for the binding of the holotoxin to specific receptors on the target cell surface, such as globotriaosylceramide (Gb3) in human intestinal microvilli.
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TMPH-00519 | StxB Protein, Enterobacteria phage H19B, Recombinant (His) | Enterobacteria phage H19B | E. coli | ||
The B subunit is responsible for the binding of the holotoxin to specific receptors on the target cell surface, such as globotriaosylceramide (Gb3) in human intestinal microvilli.
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TMPH-00523 | DNA-directed DNA polymerase Protein, Enterobacteria phage RB69, Recombinant (His & Myc) | Escherichia phage RB69 | E. coli | ||
Replicates the viral genomic DNA. This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction for proofreading purpose.
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TMPH-00522 | Recombinase cre Protein, Enterobacteria phage P1, Recombinant (His & Myc) | Escherichia phage P1 | E. coli | ||
Catalyzes site-specific recombination between two 34-base-pair LOXP sites. Its role is to maintain the phage genome as a monomeric unit-copy plasmid in the lysogenic state.
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TMPH-00517 | StxB2 Protein, Enterobacteria phage 933W, Recombinant (His) | Enterobacteria phage 933W | Yeast | ||
The B subunit is responsible for the binding of the holotoxin to specific receptors on the target cell surface, such as globotriaosylceramide (Gb3) in human intestinal microvilli.
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TMPH-00521 | G3P Protein, Enterobacteria phage M13, Recombinant (His) | Enterobacteria phage M13 | Yeast | ||
Plays essential roles both in the penetration of the viral genome into the bacterial host via pilus retraction and in the extrusion process. During the initial step of infection, G3P mediates adsorption of the phage to its primary receptor, the tip of host F-pilus. Subsequent interaction with the host entry receptor tolA induces penetration of the viral DNA into the host cytoplasm. In the extrusion process, G3P mediates the release of the membrane-anchored virion from the cell via its C-terminal domain.
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TMPH-00528 | Recombination and repair protein Protein, Enterobacteria phage T4, Recombinant (His) | Enterobacteria phage T4 | E. coli | ||
Important in genetic recombination, DNA repair, and replication. Possesses pairing and strand-transfer activity. Interacts with dda and gene 32 proteins.
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TMPH-00532 | SSB Protein, Enterobacteria phage T7, Recombinant | Enterobacteria phage T7 | Yeast | ||
Single-stranded DNA-binding protein that participates in viral DNA replication, formation of concatemers, recombination and repair of double-stranded breaks. Coats the lagging-strand ssDNA as the replication fork advances and stimulates the activities of viral DNA polymerase and primase/helicase. Coordinates simultaneous synthesis of leading- and lagging-strands. Together with DNA primase/helicase, promotes pairing of two homologous DNA molecules containing complementary single-stranded regions and mediates homologous DNA strand exchange. Promotes also the formation of joint molecules. Disrupts loops, hairpins and other secondary structures present on ssDNA to reduce and eliminate pausing of viral DNA polymerase at specific sites during elongation.
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TMPH-00525 | DsDNA-binding protein A Protein, Enterobacteria phage T4, Recombinant (His & Myc) | Enterobacteria phage T4 | E. coli | ||
May play a role in transcription of several T4 genes. Binds double-stranded DNA and interacts preferentially with T4 late promoter regions.
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TMPH-00531 | SSB Protein, Enterobacteria phage T7, Recombinant (His & SUMO) | Enterobacteria phage T7 | E. coli | ||
Single-stranded DNA-binding protein that participates in viral DNA replication, formation of concatemers, recombination and repair of double-stranded breaks. Coats the lagging-strand ssDNA as the replication fork advances and stimulates the activities of viral DNA polymerase and primase/helicase. Coordinates simultaneous synthesis of leading- and lagging-strands. Together with DNA primase/helicase, promotes pairing of two homologous DNA molecules containing complementary single-stranded regions and mediates homologous DNA strand exchange. Promotes also the formation of joint molecules. Disrupts loops, hairpins and other secondary structures present on ssDNA to reduce and eliminate pausing of viral DNA polymerase at specific sites during elongation.
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TMPH-00520 | Host-nuclease inhibitor protein gam Protein, Enterobacteria phage lambda, Recombinant (His & Myc) | Escherichia phage lambda | E. coli | ||
Binds to host RecBCD nuclease and inhibits it thereby protecting the viral DNA against recBCD mediated degradation.
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TMPH-00530 | SSB Protein, Enterobacteria phage T4, Recombinant (His & Myc) | Enterobacteria phage T4 | E. coli | ||
Single-stranded DNA-binding protein that participates in viral DNA replication, recombination, and repair (Probable). Coats the lagging-strand ssDNA as the replication fork advances. Stimulates the activities of viral DNA polymerase and DnaB-like SF4 replicative helicase, probably via its interaction with the helicase assembly factor. Together with DnaB-like SF4 replicative helicase and the helicase assembly factor, promotes pairing of two homologous DNA molecules containing complementary single-stranded regions and mediates homologous DNA strand exchange. Promotes also the formation of joint molecules. mRNA specific autogenous translational repressor.
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TMPH-00527 | Fibritin Protein, Enterobacteria phage T4, Recombinant (His & SUMO) | Enterobacteria phage T4 | E. coli | ||
Chaperone involved in tail fiber assembly and retraction. Acts as a chaperone helping to attach the long tail fibers to the virus during the assembly process. During phage assembly, twelve fibritin molecules attach to the phage neck via gp13: six molecules forming the collar and six molecules forming the whiskers.
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TMPY-00541 | LON PROTEASE Protein, E. coli, Recombinant (His) | E. coli | E. coli | ||
Lon protease, an ATP-dependent mitochondrial protease, is important in mitochondrial protein maintenance. Lon protease is a multifunctional enzyme, and its functions include the degradation of damaged proteins and naturally short-lived proteins, ATPase and chaperone-like activities, as well as DNA binding. Lon protease plays a major role in the protein quality control system in mammalian cell mitochondria. It is present in the mitochondrial matrix and degrades oxidized and misfolded proteins, thereby protecting the cell from various extracellular stresses, including oxidative stress. The intellectual disability-associated and thalidomide-binding protein cereblon (CRBN) contains a large, highly conserved Lon domain. The Lon ATP-dependent protease plays an important role in regulating many biological processes in bacteria.
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TMPY-02971 | CLEC10A Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
CLEC10A, also known as the macrophage galactose-type calcium-type lectins (MGLs; CD301) constitute a unique class of C-type lectins because of their specificity for galactose and its structural homologues. MGLs/CD301 is a type II transmembrane glycoproteins and is expressed on macrophages and related cells of myeloid origins, particularly immature dendritic cells (DCs). There are 2 homologues: MGL1 and MGL2 (CD301a and CD301b) in mice. MGL1/CD301a induces both the production and secretion of interleukin (IL)-10. MGL1/CD301a plays a protective role against colitis by effectively inducing IL-10 production by colonic lamina propria macrophages in response to invading commensal bacteria.
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TMPY-02204 | LBP Protein, Human, Recombinant (His) | Human | HEK293 | ||
Lipopolysaccharide binding protein ( LBP ) is a glycoprotein that is synthesized principally by hepatocytes. LBP is a trace plasma protein that binds to the lipid A moiety of bacterial lipopolysaccharides ( LPSs ). LBP binds directly to the outer membrane of Gram-negative bacteria and purified aggregates of extracted endotoxin and catalyzes the delivery of endotoxin to the membrane ( mCD14, GPI-Linked ) and soluble ( sCD14 ) forms of CD14, thereby markedly increasing host cell sensitivity to endotoxin. LBP efficiently catalyzes the transfer of individual molecules of endotoxin to (s)CD14 only when LBP–endotoxin aggregates are formed in the presence of albumin. In the presence of EDTA, LBP binding promotes further disaggregation of endotoxin. LBP binding does not have such drastic effects under more physiological conditions, but may still induce more subtle topological rearrangements of endotoxin.
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TMPY-00638 | Interferon alpha B/IFNA8 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Interferon alpha-B, also known as IFNA8, belongs to the alpha/beta interferon family. Interferons are proteins made and released by host cells in response to the presence of pathogens such as viruses, bacteria, parasites, or tumor cells. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. They also allow for communication between cells to trigger the protective defenses of the immune system that eradicate pathogens or tumors. Interferons also activate immune cells, such as natural killer cells and macrophages. They increase recognition of infection or tumor cells by up-regulating antigen presentation to T lymphocytes. They also increase the ability of uninfected host cells to resist new infections by virus. Certain symptoms, such as aching muscles and fever, are related to the production of IFNs during infection. Produced by macrophages, IFN-alpha has antiviral activities.
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TMPY-02904 | TLR4 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
TLR4, also known as TLR-4, is a member of the Toll-like receptor (TLR) family, which plays a fundamental role in pathogen recognition and activation of innate immunity. TLRs are highly conserved from Drosophila to humans and share structural and functional similarities. They recognize pathogen-associated molecular patterns (PAMPs) that are expressed on infectious agents, and mediate the production of cytokines necessary for the development of effective immunity. TLR4 is most abundantly expressed in placenta, and in myelomonocytic subpopulation of the leukocytes. TLR 4 has also been designated as CD284 (cluster of differentiation 284). It has been implicated in signal transduction events induced by lipopolysaccharide (LPS) found in most gram-negative bacteria. TLR4 Cooperates with LY96 and CD14 to mediate the innate immune response to bacterial lipopolysaccharide (LPS). It acts via MYD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. It is also involved in LPS-independent inflammatory responses triggered by Ni(2+).
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TMPY-00663 | Alkaline Phosphatase/ALPL Protein, Human, Recombinant (His) | Human | HEK293 | ||
Alkaline phosphatase (ALPL) is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids. The process of removing the phosphate group is called dephosphorylation. As the name suggests, alkaline phosphatases are most effective in an alkaline environment. It is sometimes used synonymously as basic phosphatase. Alkaline phosphatases (APs) are ubiquitous in many species, from bacteria to human. Four genes encode AP isoenzymes in humans and rodents. Three AP genes are expressed in a tissue-specific manner (i.e., placental, embryonic, and intestinal AP isoenzymes). Expression of the fourth AP gene is nonspecific to a single tissue and is especially abundant in bone, liver, and kidney. This isoenzyme is also called tissue-nonspecific alkaline phosphatase (TNAP). The enzyme tissue non-specific alkaline phosphatase (TNAP) belongs to the ectophosphatase family. TNAP is present in large amounts in bone in which it plays a role in mineralization.
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TMPY-02794 | TLR2 Protein, Human, Recombinant (aa 1-587, His) | Human | Baculovirus-Insect Cells | ||
TLR2, also known as CD282, is a member of the Toll-like receptor (TLR) family. TLRs are highly conserved from Drosophila to humans and share structural and functional similarities. They play a fundamental role in pathogen recognition and activation of innate immunity. They recognize pathogen-associated molecular patterns (PAMPs) that are expressed on infectious agents, and mediate the production of cytokines necessary for the development of effective immunity. The various TLRs exhibit different patterns of expression. TLR2 contains 14 LRR (leucine-rich) repeats and 1 TIR domain. TLR2 gene is expressed most abundantly in peripheral blood leukocytes, and mediates host response to Gram-positive bacteria and yeast via stimulation of NF-kappaB. CD282 cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. It also cooperates with TLR1 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. CD282 acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. It may also promote apoptosis in response to lipoproteins.
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TMPY-04578 | Interferon alpha 1/IFNA1 Protein, Human, Recombinant (His) | Human | Yeast | ||
IFNA1, also known as IFN-alpha and IFNA, belongs to the alpha/beta interferon family. Interferons(IFNs) are proteins made and released by host cells in response to the presence of pathogens such as viruses, bacteria, parasites, or tumor cells. They belong to the large class of glycoproteins known as cytokines. IFNs stimulate the production of two enzymes: a protein kinase and an oligoadenylate synthetase. They allow for communication between cells to trigger the protective defenses of the immune system that eradicate pathogens or tumors. IFNs can activate immune cells, such as natural killer cells and macrophages; they increase recognition of infection or tumor cells by up-regulating antigen presentation to T lymphocytes, and they also increase the ability of uninfected host cells to resist new infection by the virus. Leukocyte interferon is produced predominantly by B lymphocytes. Immune interferon is produced by mitogen- or antigen-stimulated T lymphocytes. IFNA1 is produced by macrophages and has antiviral activities.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-01845 | IL-10 Protein, Human, Recombinant (His) | Human | HEK293 | ||
IL-10 is an anti-inflammatory cytokine that belongs to the IL-10 family. It is produced by a variety of cell lines, including T-cells, macrophages, mast cells, and other cell types, while it is produced primarily by monocytes and to a lesser extent by lymphocytes. IL-10 is mainly expressed in monocytes and Type 2 T helper cells (TH2), mast cells, CD4+CD25+Foxp3+ regulatory T cells, and also in a certain subset of activated T cells and B cells. IL-10 has pleiotropic effects in immunoregulation and inflammation. It down-regulates the expression of Th1 cytokines, MHC class II Ags, and costimulatory molecules on macrophages. It also enhances B cell survival, proliferation, and antibody production. IL-10 can block NF-kappa B activity and is involved in the regulation of the JAK-STAT signaling pathway. Knockout studies in mice suggested the function of this cytokine as an essential immunoregulator in the intestinal tract. The importance of interleukin 10 for counteracting excessive immunity in the human body is revealed by the fact that patients with Crohn's disease react favorably towards treatment with bacteria producing recombinant IL-10. IL-10 inhibits the synthesis of some cytokines, including IFN-gamma, IL-2, IL-3, TNF, and GM-CSF produced by activated macrophages and by helper T-cells. It also displays a potent ability to suppress the antigen-presentation capacity of antigen-presenting cells. However, it is also stimulatory towards certain T cells and mast cells and stimulates B cell maturation and antibody production.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-01357 | S100A9 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
S100 protein is a family of low molecular weight protein found in vertebrates characterized by two EF-hand calcium-binding motifs. There are at least 21 different S100 proteins, and the name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are disulfide-linked homodimer, and is normally present in cells derived from the neural crest, chondrocytes, macrophages, dendritic cells, etc. S100 proteins have been implicated in a variety of intracellular and extracellular functions. They are involved in regulation of protein phosphorylation, transcription factors, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response. Protein S100-A9, also known as S100 calciumbinding protein A9, S100A9, and CAGB, is a member of the S-100 family. S100A9 is expressed by macrophages in acutely inflammed tissues and in chronic inflammation. It is also expressed in epithelial cells constitutively or induced during dermatoses. S100A9 is a calcium-binding protein. It has anti-microbial activity towards bacteria and fungi. The anti-microbial and proapoptotic activity of S100A9 is inhibited by zinc ions. S100A9 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide (LPS). It promotes tubulin polymerization when unphosphorylated. It also promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A9 plays a role as a proinflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.
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TMPY-05064 | IL-10 Protein, Mouse, Recombinant | Mouse | E. coli | ||
IL-10 is an anti-inflammatory cytokine that belongs to the IL-10 family. It is produced by a variety of cell lines, including T-cells, macrophages, mast cells, and other cell types, while it is produced primarily by monocytes and to a lesser extent by lymphocytes. IL-10 is mainly expressed in monocytes and Type 2 T helper cells (TH2), mast cells, CD4+CD25+Foxp3+ regulatory T cells, and also in a certain subset of activated T cells and B cells. IL-10 has pleiotropic effects in immunoregulation and inflammation. It down-regulates the expression of Th1 cytokines, MHC class II Ags, and costimulatory molecules on macrophages. It also enhances B cell survival, proliferation, and antibody production. IL-10 can block NF-kappa B activity and is involved in the regulation of the JAK-STAT signaling pathway. Knockout studies in mice suggested the function of this cytokine as an essential immunoregulator in the intestinal tract. The importance of interleukin 10 for counteracting excessive immunity in the human body is revealed by the fact that patients with Crohn's disease react favorably towards treatment with bacteria producing recombinant IL-10. IL-10 inhibits the synthesis of some cytokines, including IFN-gamma, IL-2, IL-3, TNF, and GM-CSF produced by activated macrophages and by helper T-cells. It also displays a potent ability to suppress the antigen-presentation capacity of antigen-presenting cells. However, it is also stimulatory towards certain T cells and mast cells and stimulates B cell maturation and antibody production.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-03547 | IL-10 Protein, Human, Recombinant | Human | E. coli | ||
IL-10 is an anti-inflammatory cytokine that belongs to the IL-10 family. It is produced by a variety of cell lines, including T-cells, macrophages, mast cells, and other cell types, while it is produced primarily by monocytes and to a lesser extent by lymphocytes. IL-10 is mainly expressed in monocytes and Type 2 T helper cells (TH2), mast cells, CD4+CD25+Foxp3+ regulatory T cells, and also in a certain subset of activated T cells and B cells. IL-10 has pleiotropic effects in immunoregulation and inflammation. It down-regulates the expression of Th1 cytokines, MHC class II Ags, and costimulatory molecules on macrophages. It also enhances B cell survival, proliferation, and antibody production. IL-10 can block NF-kappa B activity and is involved in the regulation of the JAK-STAT signaling pathway. Knockout studies in mice suggested the function of this cytokine as an essential immunoregulator in the intestinal tract. The importance of interleukin 10 for counteracting excessive immunity in the human body is revealed by the fact that patients with Crohn's disease react favorably towards treatment with bacteria producing recombinant IL-10. IL-10 inhibits the synthesis of some cytokines, including IFN-gamma, IL-2, IL-3, TNF, and GM-CSF produced by activated macrophages and by helper T-cells. It also displays a potent ability to suppress the antigen-presentation capacity of antigen-presenting cells. However, it is also stimulatory towards certain T cells and mast cells and stimulates B cell maturation and antibody production.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPH-02821 | GP2 Protein, Mouse, Recombinant (E. coli, His) | Mouse | E. coli | ||
Functions as an intestinal M-cells transcytotic receptor specific of type-I-piliated bacteria that participate in the mucosal immune response toward these bacteria. At the apical membrane of M-cells binds fimH, a protein of the bacteria type I pilus tip. Internalizes bound bacteria, like E.coli and S.typhimurium, from the lumen of the intestine and delivers them, through M-cells, to the underlying organized lymphoid follicles where they are captured by antigen-presenting dendritic cells to ellicit a mucosal immune response.
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TMPH-02820 | GP2 Protein, Mouse, Recombinant (His) | Mouse | Yeast | ||
Functions as an intestinal M-cells transcytotic receptor specific of type-I-piliated bacteria that participate in the mucosal immune response toward these bacteria. At the apical membrane of M-cells binds fimH, a protein of the bacteria type I pilus tip. Internalizes bound bacteria, like E.coli and S.typhimurium, from the lumen of the intestine and delivers them, through M-cells, to the underlying organized lymphoid follicles where they are captured by antigen-presenting dendritic cells to ellicit a mucosal immune response.
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TMPH-03145 | Thanatin Protein, Podisus maculiventris, Recombinant (His & KSI) | Podisus maculiventris | E. coli | ||
Insect defense peptide with a broad spectrum of activity against Gram-positive and Gram-negative bacteria and fungi. No activity against S.aureus. Stops respiration in bacteria but does not permeabilize their inner membranes.
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TMPH-02544 | DEFB4 Protein, Mouse, Recombinant (His & SUMO) | Mouse | E. coli | ||
Exhibits antimicrobial activity against Gram-negative bacteria and Gram-positive bacteria. May act as a ligand for C-C chemokine receptor CCR6. Can bind to mouse (but not human) CCR6 and induce chemotactic activity of CCR6-expressing cells.
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TMPH-00325 | S-layer Protein, Campylobacter fetus, Recombinant (His & Myc) | Campylobacter fetus | E. coli | ||
The S-layer is a paracrystalline mono-layered assembly of proteins which coats the surface of bacteria. This protein is critical for virulence.
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TMPJ-00726 | NEO Protein, K. pneumoniae, Recombinant | Klebsiella pneumoniae | E. coli | ||
Aminoglycoside 3'-phosphotransferase (APH(3')), also known as aminoglycoside kinase, is an aminoglycoside-modifying enzyme and widely presented in resistant bacteria. These ATP-dependent enzymes phosphorylate the 3'-hydroxyl of a variety of aminoglycosides including kanamycins, neomycins, paromomycins, neamine, ribostamycin, geneticin, and paromamine. These phosphorylated aminoglycosides fail to bind to their respective ribosomal binding sites with high affinity; hence resistance is conferred to the drugs that are phosphorylated. APH(3') is primarily found in certain species of gram-positive bacteria.
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TMPH-00063 | Defensin-1 Protein, Apis mellifera, Recombinant (His) | Apis mellifera | E. coli | ||
Found in royal jelly and in hemolymph, potent antibacterial protein against Gram-positive bacteria at low concentration.
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TMPH-02381 | slpA Protein, Lactobacillus acidophilus, Recombinant (His & Myc) | Lactobacillus acidophilus | E. coli | ||
The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of bacteria.
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TMPH-00230 | Cathelicidin-6 Protein, Bovine, Recombinant (His & SUMO) | Bovine | E. coli | ||
Exerts a potent antimicrobial activity against Gram-negative and Gram-positive bacteria, including methicillin-resistant Staphylococcus aureus, and fungi.
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TMPH-00598 | Colicin-E5 Protein, E. coli, Recombinant (His & SUMO) | E. coli | in vitro E. coli expression system | ||
Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria. This colicin is an endonuclease.
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TMPH-00061 | Defensin-1 Protein, Apis mellifera carnica, Recombinant (His & KSI) | Apis mellifera carnica | E. coli | ||
Found in royal jelly and in hemolymph, potent antibacterial protein against Gram-positive bacteria at low concentration.
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TMPH-03716 | Invasin Protein, Yersinia enterocolitica, Recombinant (His & SUMO) | Yersinia enterocolitica | E. coli | ||
Invasin is a protein that allows enteric bacteria to penetrate cultured mammalian cells. The entry of invasin in the cell is mediated by binding several beta-1 chain integrins.
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TMPH-00596 | Colicin-E1 Protein, E. coli, Recombinant (Cell-Free, His & Myc) | E. coli | in vitro E. coli expression system | ||
This colicin is a channel-forming colicin. This class of transmembrane toxins depolarize the cytoplasmic membrane, leading to dissipation of cellular energy.; Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria.
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TMPH-00597 | Colicin-E1 Protein, E. coli, Recombinant (His & Myc) | E. coli | E. coli | ||
This colicin is a channel-forming colicin. This class of transmembrane toxins depolarize the cytoplasmic membrane, leading to dissipation of cellular energy.; Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria.
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TMPH-01772 | DEFA1 Protein, Human, Recombinant (GST) | Human | E. coli | ||
Defensin 1 and defensin 2 have antibacterial, fungicide and antiviral activities. Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane.
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TMPY-02163 | PGLYRP1 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Peptidoglycan recognition protein 1, also known as Peptidoglycan recognition protein short, PGRP-S, PGLYRP1, PGLYRP, PGRP and TNFSF3L, is a secreted protein that belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. PGLYRP1 / PGLYRP is highly expressed in bone marrow. It is weakly expressed in kidney, liver, small intestine, spleen, thymus, peripheral leukocyte, lung, fetal spleen and neutrophils. PGLYRP1 / PGLYRP is a pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. It has bactericidal activity towards Gram-positive bacteria. PGLYRP1 / PGLYRP may kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. It binds also to Gram-negative bacteria, and has bacteriostatic activity towards Gram-negative bacteria. Peptidoglycan recognition proteins (PGRPs or PGLYRPs) are innate immunity proteins that are conserved from insects to mammals, recognize bacterial peptidoglycan, and function in antibacterial immunity and inflammation. Mammals have four PGRPs: PGLYRP1, PGLYRP2, PGLYRP3, and PGLYRP4. They are secreted proteins expressed in polymorphonuclear leukocytes (PGLYRP1), liver (PGLYRP2), or on body surfaces, mucous membranes, and in secretions (saliva, sweat) (PGLYRP3 and PGLYRP4). All PGRPs recognize bacterial peptidoglycan. The PGRPs likely play a role both in antibacterial defenses and several inflammatory diseases. They modulate local inflammatory responses in tissues (such as arthritic joints) and there is evidence for association of PGRPs with inflammatory diseases, such as psoriasis.
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TMPH-00620 | F41 fimbrial Protein, E. coli, Recombinant (His & Myc) | E. coli | E. coli | ||
Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs.
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TMPH-02389 | Hepcidin Protein, Larimichthys crocea, Recombinant | Larimichthys crocea | E. coli | ||
Seems to act as a signaling molecule involved in the maintenance of iron homeostasis. Seems to be required in conjunction with HFE to regulate both intestinal iron absorption and iron storage in macrophages.; Has very strong antibacterial activity against the marine Gram-negative bacteria V.alginolyticus (MIC=24 uM), V.fluvialis, V.harveyis (MIC=12 uM) and V.parahaemolyticus (MIC=6 uM). Has antibacterial activity against the Gram-negative bacteria A.hydrophila (MIC=6 uM), E.coli (MIC=24 uM), and E.coli BL21(DE3)plysS (MIC=6 uM), and the Gram-positive bacteria B.cereus (MIC=24 uM), B.subtilis (MIC=6 uM), C.glutamicum (MIC=3 uM), M.luteus (MIC=3 uM), M.lysodeikticus, S.aureus (MIC=6 uM) and S.epidermis (MIC=12 uM). Possesses antifungal activity against A.niger (MIC=24 uM), F.graminearum (MIC24 uM) and F.solani (MIC=24 uM), but lacks antifungal activity against the yeasts P.pastoris GS115 and C.albicans.
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TMPH-03010 | EsxB Protein, Mycobacterium tuberculosis, Recombinant (His) | Mycobacterium tuberculosis | Yeast | ||
A secreted protein. Acts as a strong host T-cell antigen. Involved in translocation of bacteria from the host (human) phagolysosome to the host cytoplasm. Might serve as a chaperone to prevent uncontrolled membrane lysis by its partner EsxA.
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TMPH-00065 | MRJP1 Protein, Apis mellifera, Recombinant (GST) | Apis mellifera | E. coli | ||
Induces the differentiation of honeybee larvae into queens through an Egfr-mediated signaling pathway. Promotes body size increase by activating p70 S6 kinase, stimulates ovary development by augmenting the titer of vitellogenin (Vg) and juvenile hormone, and reduces developmental time by increasing the activity of mitogen-activated protein kinase and inducing the 20-hydroxyecdysone protein (20E). Most abundant protein found in the royal jelly which is the food of the queen honey bee larva. The royal jelly determines the development of the young larvae and is responsible for the high reproductive ability of the honeybee queen.; Has antibacterial activity against the Gram-positive bacteria S.aureus ATCC 6535, S.saprophyticus and B.subtilis CCT2471, and the Gram-negative bacteria E.coli CCT1371, E.cloacae ATCC 23355, K.pneumoniae ATCC 13883 and P.aeruginosa ATCC 27853, and antifungal activity against C.albicans. Lack cytolytic activity and does not induce rat peritoneal mast cell degranulation.; Has antibacterial activity against the Gram-positive bacteria S.aureus ATCC 6535, S.saprophyticus and B.subtilis CCT2471, and the Gram-negative bacteria E.coli CCT1371, E.cloacae ATCC 23355, K.pneumoniae ATCC 13883 and P.aeruginosa ATCC 27853, and antifungal activity against C.albicans. Lack cytolytic activity and does not induce rat peritoneal mast cell degranulation.; Lacks antibacterial and antifungal activity. Lacks cytolytic activity and does not induce rat peritoneal mast cell degranulation.
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