目录号 | 产品详情 | 靶点 | |
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T74004 | |||
Carboxyaminoimidazole ribotide (CAIR) 为大肠杆菌代谢产物,用于检测大肠杆菌 PurE 活性位点的特征以及合成真菌嘌呤的从头合成。 | |||
T38104 | |||
Deoxyfusapyrone is an α-pyrone fungal metabolite originally isolated from F. semitectum and has antifungal activity. It is active against C. neoformans, A. fumigatus, A. niger, and A. flavus human mycoses (MICs = 1.56-6.25 μg/ml). Deoxyfusapyrone is also active against a variety of filamentous fungi, but not yeast or the bacterium B. megaterium, in a disc assay. | |||
T80281 | Parasite | ||
Melimine是一种合成的抗菌肽,由蜂毒肽和鱼精蛋白融合而成。该化合物对P. aeruginosa和S. aureus表现出抗菌活性,且具有针对细菌、真菌和原生动物的广谱抗菌性能。 | |||
T73607 | |||
UDP-xylose是一种从Cryptococcus laurentii(NRRL Y-1401)提取的天然产物。它作为糖供体,在植物、脊椎动物和真菌中参与糖蛋白、多糖及多种代谢物和寡糖的合成。 | |||
T75176 | |||
Antifungal agent 53 (A03) 是一种有效的白色念珠菌 CYP51抑制剂,具有抗真菌活性。Antifungal agent 53 阻止真菌生物膜的形成。Antifungal agent 53 也显示出良好的安全性。 | |||
T10330 | Antibacterial | ||
Antibiotic-5d 是一种合成的抗菌化合物,对各种革兰氏阳性和革兰氏阴性细菌、真菌和酵母表现出中等的抗菌活性。 | |||
TN6952 | |||
Hexadecane (n-Hexadecane) 可作为真菌的碳源,与厌氧生物生物降解有关。Hexadecane 在豚鼠皮肤实验中抑制皮肤过度角质化。 | |||
T79989 | Antibiotic | ||
Funiculosin为一种中性亲脂性抗生素,能够抑制DNA及RNA病毒,并具备抗真菌活性。在初级鸡胚成纤维细胞中,Funiculosin可有效抑制致病真菌引发的感染。 | |||
T75475 | |||
Chaetosemin J,一种对植物病原真菌(如灰霉病菌、番茄交链孢菌、稻瘟病菌和赤霉素)具有抑制活性的抗真菌代谢产物,MIC值在12.5-25 μM范围内。 | |||
T9802 | |||
Penconazole 是一种典型的三唑类杀菌剂 (fungicide),主要用于苹果、葡萄、蔬菜等的白粉病防治。Penconazole 抑制真菌甾醇生物合成。Penconazole 降低大鼠大脑和小脑AChE 活性。 |
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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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-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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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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