目录号 | 产品详情 | 靶点 | |
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T2P2937 | Others Antibacterial | ||
Nonacosane 是从Baphia massaiensis 分离的,是一种由 29 个碳原子组成的直链烷烃,具有植物代谢物和挥发油成分的作用。 | |||
T4998L | Others | ||
Cefpodoxime (free acid) 是一种口服的第三代头孢菌素抗生素。除铜绿假单胞菌、肠球菌和脆弱拟杆菌外,它对大多数革兰氏阳性和革兰氏阴性微生物均有效。 | |||
T1008 | Antibacterial Antibiotic | ||
Cephalexin (Cephacillin) 是一种强口服活性的头孢菌素抗生素。它通过破坏细菌细胞壁的生长来杀死革兰氏阳性和一些革兰氏阴性细菌。它可研究肺炎、链球菌性咽喉炎、细菌性心内膜炎等。 | |||
T5006 | Antibacterial Antibiotic | ||
Flucloxacillin sodium (floxacillin sodium) 是一种高活性抗生素,抑制革兰氏阳性和革兰氏阴性菌。 | |||
T73997 | |||
Anti gram-positive/negative bacteria agent 1 是一种含有基于MECAM的人工铁载体的抗生素化合物。 | |||
T6582 | Antibacterial Antibiotic | ||
Mezlocillin Sodium (Baycipen) 是一种青霉素 β-内酰胺类抗生素,用于治疗由易感染微生物引起的细菌感染。 | |||
T14391 | Antibacterial Antibiotic | ||
Azidamfenicol 抑制核糖体肽基转移酶,Ki 为 22 µM。Azidamfenicol 是一种广谱氯霉素类抗生素。 | |||
T24729 | Antibacterial | ||
Roseoflavin 是天然色素,起初分离自Streptomyces davawensis。Roseoflavin 是核黄素和黄素单核苷酸的抗代谢类似物,显示出抗菌活性。 | |||
T83705 | |||
BING是一种来源于日本稻田鱼(O. laptipes)的抗菌肽,由液泡蛋白质分选相关蛋白13D样(Vps13D)衍生而来。对包括耐甲氧西林的金黄色葡萄球菌(MRSA; MICs = 4-64 µg/ml)在内的各种革兰氏阴性和革兰氏阳性细菌都有活性。与氨苄西林、阿莫西林和新霉素共同使用时,对抗铜绿假单胞菌(P. aeruginosa)表现出协同效应,并能抑制大肠杆菌(E. coli)对卡那霉素和氨苄西林的抗药性发展。在体内,BING提高了被鳗弧菌(E. tarda)感染的O. laptipes的生存率。 | |||
T19858 | DHFR Antibacterial | ||
Brodimoprim 是甲氧苄啶的一种类似物,是口服有效的二氢叶酸还原酶抑制剂,对广谱革兰氏阴性和革兰氏阳性细菌具有高度的抑制作用。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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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-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-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-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-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-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-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-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-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-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-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-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-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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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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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-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-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-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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TMPH-02289 | FAU Protein, Human, Recombinant (GST) | Human | E. coli | ||
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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-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-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-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-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-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-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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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-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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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-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-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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