目录号 | 产品详情 | 靶点 | |
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T4455 | Others Endogenous Metabolite Antibacterial | ||
DL-3-Phenyllactic acid (3-Phenyllactic acid) 是广谱抗菌化合物,对细菌和真菌具有活性。 | |||
T10797 | Antifungal | ||
Chlormidazole hydrochloride (Clomidazole hydrochloride) 是一种抗真菌剂,抑制多种真菌和部分革兰氏阳性球菌,可治疗指甲和皮肤的真菌和细菌感染。 | |||
T5746 | Apoptosis Anti-infection Antibacterial Antifungal | ||
Dictamine (Dectamine) 显示抗胆碱酯酶、抗炎、致突变、抗菌和抗真菌活性。 它具有在人子宫颈、结肠和口腔癌细胞中发挥细胞毒性的能力。 | |||
TP1186 | Others | ||
Cyclo(Phe-Pro) (A-64863) 是创伤弧菌的群体感应分子,能够与 RIG-I 的特异性相互作用,阻碍 RIG-I 的多泛素化,并抑制 IRF-3 的激活和 I 型干扰素的产生。它提高 HCV 和流感病毒的易感性。 | |||
T35366 | Others | ||
4-Nitroquinoline 1-oxide (4-NQO) 是一种化学致癌物,可通过形成大量嘌呤加合物来诱导细菌、真菌和动物的突变。 | |||
T74756 | Antifungal | ||
SDH-IN-2 是一种有效的琥珀酸脱氢酶 (SDH) 抑制剂,IC50 为 0.55 μg/mL。SDH-IN-2 具有抗真菌活性,抑制植物病原真菌的平均 EC50 值为 3.82-9.81 μg/mL | |||
T12248 | Antibacterial Antibiotic Antifungal | ||
Nourseothricin sulfate (Streptothricin sulfate) 是广谱抗生素,可破坏革兰氏阴性菌的外膜,并且是Fonsecaea pedrosoi 的主要选择性标记物。它抑制原核细胞中蛋白质的生物合成,并强烈抑制真核生物,还可作为多种生物的选择性标记物。 | |||
T37069 | Antifungal | ||
Pyribencarb,一种苯甲酰胺类杀菌剂,针对多种植物病原真菌展现出广谱活性。作为细胞色素b的强效Qo抑制剂,Pyribencarb 对灰霉病菌(Botrytis cinerea)和菌核病菌(Sclerotinia sclerotiorum)特别有效。 | |||
T5S0814 | Antibacterial | ||
Berberine hydrogen sulphate (Umbellatine Sulfate) 是一种从几种植物中提取的生物碱,对多种微生物具有抗菌活性,包括革兰氏阳性和革兰氏阴性细菌、真菌和原生动物。 | |||
T0583 | Endogenous Metabolite | ||
meso-Erythritol (Phycitol) 是一种天然存在于各种食物 (如梨,西瓜等)的糖醇,其甜度为蔗糖的 60-80%,是一种经过批准的低热量甜味剂。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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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. Cathelicidin-6 Protein, Bovine, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 16.2 kDa and the accession number is P54228.
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TMPH-00761 | Cutinase Protein, Fusarium solani subsp. Cucurbitae, Recombinant | Neocosmosporum cucurbitae | E. coli | ||
Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle. Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of the fungal infection. Cutinase Protein, Fusarium solani subsp. Cucurbitae, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 22.4 kDa and the accession number is Q99174.
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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. Thanatin Protein, Podisus maculiventris, Recombinant (His & KSI) is expressed in E. coli expression system with N-6xHis-KSI tag. The predicted molecular weight is 17.8 kDa and the accession number is P55788.
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TMPH-00424 | Cutinase Protein, Colletotrichum capsici, Recombinant (His & SUMO) | Colletotrichum capsici | E. coli | ||
Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle. Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of the fungal infection. Cutinase Protein, Colletotrichum capsici, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 35.0 kDa and the accession number is P10951.
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TMPH-00760 | Cutinase Protein, Fusarium solani subsp. Cucurbitae, Recombinant (His) | Neocosmosporum cucurbitae | P. pastoris (Yeast) | ||
Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle. Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of the fungal infection. Cutinase Protein, Fusarium solani subsp. Cucurbitae, Recombinant (His) is expressed in yeast with C-6xHis tag. The predicted molecular weight is 23.7 kDa and the accession number is Q99174.
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TMPK-00255 | CD209/DC-SIGN Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
C-type lectin CD209/DC-SIGN and CD209L/L-SIGN proteins are distinct cell adhesion and pathogen recognition receptors that mediate cellular interactions and recognize a wide range of pathogens, including viruses such as SARS, SARS-CoV-2, bacteria, fungi and parasites. Pathogens exploit CD209 family proteins to promote infection and evade the immune recognition system.
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TMPH-01632 | MRC1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Mediates the endocytosis of glycoproteins by macrophages. Binds both sulfated and non-sulfated polysaccharide chains.; (Microbial infection) Acts as phagocytic receptor for bacteria, fungi and other pathogens.; (Microbial infection) Acts as a receptor for Dengue virus envelope protein E.; (Microbial infection) Interacts with Hepatitis B virus envelope protein. MRC1 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 69.9 kDa and the accession number is P22897.
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TMPJ-00133 | MBL2 Protein, Mouse, Recombinant | Mouse | HEK293 Cells | ||
Mannose-binding Lectin (MBL) is an acute phase protein bearing to the family of collectins produced by the liver as a monomer that forms a triple helix. Once released in serum, it further polymerizes forming dimers to octamers. The degree of serum polymerization is critical for the biological activity of MBL. MBL has higher affinity to microbial polysaccharides or their glycoconjugates. MBL was shown earlier to bind cell surfaces of bacteria, fungi, protozoa and viruses and acts as an acute-phase plasma protein (APP) during infection and inflammation. MBL activates the lectin-complement pathway, promotes opsonophagocytosis and modulates inflammation.
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TMPJ-01034 | TIM Protein, Human, Recombinant (His) | Human | E. coli | ||
Triose-phosphate isomerase, also named Triose-phosphate isomerase, TPI and TIM, is an enzyme that catalyzes the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. TPI has been found in nearly every organism searched for the enzyme, including animals such as mammals and insects as well as in fungi, plants, and bacteria. However, some bacteria that do not perform glycolysis, like ureaplasmas, lack TPI. TPI plays an important role in glycolysis and is essential for efficient energy production. TPI deficiency is an autosomal recessive disorder and the most severe clinical disorder of glycolysis. Triose phosphate isomerase deficiency is associated with neonatal jaundice, chronic hemolytic anemia, progressive neuromuscular dysfunction, cardiomyopathy and increased susceptibility to infection and characterized by chronic hemolytic anemia.
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TMPY-02599 | MDH1 Protein, Rat, Recombinant (His) | Rat | E. coli | ||
Malate dehydrogenases 1(MDH1 / MDHA) is a soluble form of malate dehydrogenases. Malate dehydrogenases (MDH) is a group of multimeric enzymes consisting of identical subunits usually organized as either dimer or tetramers with subunit molecular weights of 30-35 kDa. MDH has been isolated from different sources including archaea, eubacteria, fungi, plants, and mammals. MDH catalyzes the NAD/NADH-dependent interconversion of the substrates malate and oxaloacetate. This reaction plays a key part in the malate/aspartate shuttle across the mitochondrial membrane, and in the tricarboxylic acid cycle within the mitochondrial matrix. The enzymes share a common catalytic mechanism and their kinetic properties are similar, which demonstrates a high degree of structural similarity. The three-dimensional structures and elements essential for catalysis are conserved between mitochondrial and cytoplasmic forms of MDH in eukaryotic cells even though these isoenzymes are only marginally related at the level of the primary structure.
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TMPY-03728 | CCL28 Protein, Human, Recombinant (His) | Human | E. coli | ||
CCL28 chemokine is expressed by epithelial cells of various mucosal tissues. This chemokine binds to CCR3 and CCR10 receptors and plays an essential role in the IgA antibody secreting cells (IgA-ASC) homing to mucosal surfaces and lactating mammary gland as well. Besides, CCL28 has been shown to exert a potent antimicrobial activity against both Gram-negative and Gram-positive bacteria and fungi. The potent antimicrobial function of CCL28 combined with its wide distribution in mucosal tissues and secretions suggest that this protein plays an important role in innate immune protection of the epithelial surfaces. CCL28 is a human chemokine constitutively expressed by epithelial cells in diverse mucosal tissues and is known to attract a variety of immune cell types including T-cell subsets and eosinophils. Elevated levels of CCL28 have been found in the airways of individuals with asthma, and previous studies have indicated that CCL28 plays a vital role in the acute development of post-viral asthma. CCL28 presents a novel target for the development of alternative asthma therapeutics. The dental decay of children leads to the secretion of chemokine CCL28, which promotes the secretion of sIgA in saliva. CC chemokine ligand28 (CCL28) has been reported as a severity marker in atopic dermatitis.
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TMPY-01290 | CHIT1 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Chitotriosidase, also known as Chitinase-1 and CHIT1, is a member of the glycosyl hydrolase 18 family and Chitinase class II subfamily. It is a member of the mammalian chitinase family, structurally homologous to chitinases from other species, is synthesized and secreted by specifically activated macrophages. Chitotriosidase is a polymer of N-acetylglucosamine. Serum and plasma chitotriosidase activity is usually measured as the first step in diagnosis of Gaucher disease. Monitoring chitotriosidase activity is widely used during treatment of this pathology by enzyme replacement therapy. Its elevated plasma level reflects gradual intralysosomal accumulation in Gaucher cells (lipid-loaded macrophages). Macrophages overloaded by the enzyme accumulated in lysosomal material (lipids) were shown to secrete chitotriosidase; its increased expression was noted in several lysosomal storage diseases and atherosclerosis. In addition to lipid storage disorders, where Chit activity has longer been used as a marker of disease activity and therapeutic response, elevation of plasma Chit may occur in hematological disorders with storage of erythrocyte membrane breakdown products as thalassemia and different systemic infectious diseases sustained by fungi and other pathogens. Recently, increased Chit activity was demonstrated in CNS from patients with different neurological disorders. Chitotriosidase is believed to play a role in mechanisms of immunity and protection against chitin-containing pathogens.
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TMPY-01855 | Serpin A10 Protein, Mouse, Recombinant (His) | Mouse | HEK293 Cells | ||
Protein Z-dependent protease inhibitor, also known as PZ-dependent protease inhibitor, SERPINA1 and ZPI, is a secreted protein that belongs to the serpin family. It is expressed by the liver and secreted in plasma. SERPINA1 / Serpin-A1 inhibits factor Xa activity in the presence of protein Z, calcium and phospholipid. Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The acronym serpin was originally coined because many serpins inhibit chymotrypsin-like serine proteases (serine protease inhibitors). Over 1 serpins have now been identified, these include 36 human proteins, as well as molecules in plants, fungi, bacteria, archaea and certain viruses. Serpins are the largest and most diverse family of protease inhibitors. Most serpins control proteolytic cascades, certain serpins do not inhibit enzymes, but instead perform diverse functions such as storage (ovalbumin, in egg white), hormone carriage proteins (thyroxine-binding globulin, cortisol-binding globulin) and tumor suppressor genes (maspin). Most inhibitory serpins target chymotrypsin-like serine proteases. These enzymes are defined by the presence of a nucleophilic serine residue in their catalytic site. Some serpins inhibit other classes of protease. A number of such serpins have been shown to target cysteine proteases. These enzymes differ from serine proteases in that they are defined by the presence of a nucleophilic cysteine residue, rather than a serine residue, in their catalytic site.
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