目录号 | 产品详情 | 靶点 | |
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TN1788 | Amylase | ||
Isookanin 在多种疾病领域有研究价值,包括肿瘤,皮疹,蛇和昆虫叮咬,糖尿病,腹泻。它可作为抗病毒剂对抗 HSV 和水痘带状疱疹病毒。它也具有抗氧化特性。 | |||
T20137 | Others | ||
Dimethoate (L-395) 是一种系统性和接触性杀虫剂,用于控制牛蛴螬和农场动物的某些其他害虫。 | |||
T13633 | Parasite | ||
D-Phenothrin ((-)-trans-Phenothrin) 是一种口服有效的 II 型合成拟除虫菊酯,广泛用于杀死昆虫,蚊子和人类虱子。它还用于兽医,保护农作物和控制动物上的害虫。 | |||
T22295 | Others | ||
cis-3-Hexen-1-ol ((Z)-3-Hexen-1-ol) 是发现于许多新鲜水果和蔬菜中的一种绿色草味化合物,常用作加工食品的附加风味剂,以提供新鲜的绿色品质,也是多种昆虫的引诱剂。 | |||
T16044 | Others | ||
Methoprene (ZR-515) 是一种保幼激素模拟物和一种生物杀虫剂。Methoprene 作为昆虫生长调节剂,干扰昆虫的生命周期并阻止其成熟或繁殖。 | |||
T19940 | AChR | ||
Sulfoxaflor (GF 2032) 是 nAChR1 和 nAChR2 亚型的激动剂,是一种作用于昆虫中枢神经系统的内吸性杀虫剂。 Sulfoxaflor 用于防治吸食汁液的昆虫,如褐飞虱、烟粉虱、桃蚜和棉蚜。 | |||
T20692L | Others | ||
Schistoflrfamide acetate 是从蚱蜢 Schistocerca gregaria 中分离得到的。 Schistoflrfamide acetate 对昆虫乳白色小管腺细胞的基底膜电位产生直接影响。 | |||
TP1413L | |||
Crustacean Cardioactive Peptide Acetate (CCAP acetate) 是 是节肢动物中最保守和普遍存在的神经肽,在昆虫中由腹侧神经索中的保守神经元网络产生。Crustacean Cardioactive Peptide Acetate 是一种环酰胺化九肽激素,常见于昆虫,甲壳类动物和其他节肢动物中。 | |||
T8070 | Others | ||
Nonadecanoic acid 是19 C 长的饱和脂肪酸,是白蚁防御时分泌的主要物质。 | |||
T3202 | Parasite | ||
Fluensulfone (MCW-2) 是一种新型杀线虫剂,可化学防治植物寄生线虫。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPH-02404 | LqhaIT Protein, Leiurus hebraeus, Recombinant (His & SUMO) | Yellow scorpion | E. coli | ||
Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. The dissociation is voltage-dependent. This toxin is active on insects. It is also highly toxic to crustaceans and has a measurable but low toxicity to mice.
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TMPH-02405 | LqqIT1 Protein, Leiurus quinquestriatus quinquestriatus, Recombinant (His & Myc) | Egyptian scorpion | E. coli | ||
Excitatory insect beta-toxins induce a spastic paralysis. They bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. This toxin induces a fast excitatory contraction paralysis on fly larvae. It is active only on insects.
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TMPY-02311 | AGO3 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
Argonaute (Ago) protein family plays a key role in the RNA interference (RNAi) process in different insects including Lepidopteran. AGO3 also coexists and interacts with Armitage in the mitochondrial fraction. Furthermore, AGO3 acts in conjunction with the mitochondria-associated protein Zucchini to control the dynamic subcellular localization of Armitage between mitochondria and nuage in a Slicer-dependent fashion.
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TMPH-00837 | BjaIT Protein, Hottentotta judaicus, Recombinant (His & Myc) | Hottentotta judaicus | E. coli | ||
Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin is active against insects (para/tipE).
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TMPH-00056 | Delta-AITX-Avd1c Protein, Anemonia sulcata, Recombinant (His) | Anemonia sulcata | Yeast | ||
Binds specifically to voltage-gated sodium channels (Nav) (site 3), thereby delaying their inactivation. Has a strong effect on crustaceans and insects (DmNav1) and a weaker effect on mammals. This toxin is highly potent at mammalian Nav1.1/SCN1A (EC(50)=6.01 nM) and Nav1.2/SCN2A (EC(50)=7.88 nM). It has also great activity on Nav1.5/SCN5A (EC(50)=49.05 nM), Nav1.4/SCN4A (EC(50)=109.49 nM) and Nav1.6/SCN8A (EC(50)=about 180 nM) and is less potent on Nav1.3/SCN3A (EC(50)=759.22 nM) (when measured as the increase in the slow component).
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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-01306 | DNMT2 Protein, Human, Recombinant (GST) | Human | Baculovirus-Insect Cells | ||
DNMT2, also known as tRNA (cytosine-5-)-methyltransferase, DNA methyltransferase homolog HsaIIP, and TRDMT1, is a member of the DNA methyltransferase family of enzymes. DNMT2 enzymes have been widely conserved during evolution and contain all of the signature motifs of DNA (cytosine-5)-methyltransferases. It contains all 10 sequence motifs that are conserved among m(5)C MTases, including the consensus S:-adenosyl-L-methionine-binding motifs and the active site ProCys dipeptide, and its structure is very similar to prokaryotic DNA methyltransferases. DNMT2 has close homologs in plants, insects and Schizosaccharomyces pombe, but no related sequence can be found in the genomes of Saccharomyces cerevisiae or Caenorhabditis elegans. While the biological function of DNMT2 is not yet known, the strong binding to DNA suggests that DNMT2 may mark specific sequences in the genome by binding to DNA through the specific target-recognizing motif. However, the DNA methyltransferase activity of these proteins is comparatively weak and their biochemical and functional properties remain enigmatic. Recent evidence now shows that Dnmt2 has a novel tRNA methyltransferase activity, raising the possibility that the biological roles of these proteins might be broader than previously thought.
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TMPY-02181 | PLA2G12B Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Group XIIB secretory phospholipase A2-like protein, also known as Group XIII secretory phospholipase A2-like protein, GXIII sPLA2-like, sPLA2-GXIIB, GXIIB, PLA2G13 and PLA2G12B, is a secreted protein that belongs to the phospholipase A2 family. PLA2G12B / PLA2G13 is strongly expressed in liver, small intestine and kidney. Mammalian secretory phospholipase A2s ( sPLA2s ) form a family of structurally related enzymes that are involved in a variety of physiological and pathological processes via the release of arachidonic acid from membrane phospholipids or the binding to specific membrane receptors. Phospholipases A2 / PLA2 are enzymes that release fatty acids from the second carbon group of glycerol. This particular phospholipase specifically recognizes the sn-2 acyl bond of phospholipids and catalytically hydrolyzes the bond releasing arachidonic acid and lysophospholipids. Phospholipases A2 / PLA2 are commonly found in mammalian tissues as well as insect and snake venom. Venom from both snakes and insects is largely composed of melittin, which is a stimulant of Phospholipases A2 / PLA2. Due to the increased presence and activity of Phospholipases A2 / PLA2 resulting from a snake or insect bite, arachidonic acid is released from the phospholipid membrane disproportionately. As a result, inflammation and pain occur at the site.
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TMPY-02162 | Phospholipase A2 IIE/PLA2G2E Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Group IIE secretory phospholipase A2, also known as GIIE sPLA2, sPLA2-IIE, Phosphatidylcholine 2-acylhydrolase 2E and PLA2G2E is a secreted protein that belongs to the phospholipase A2 family. Mammalian secretory phospholipase A2s (sPLA2s) form a family of structurally related enzymes that are involved in a variety of physiological and pathological processes via the release of arachidonic acid from membrane phospholipids or the binding to specific membrane receptors. Phospholipases A2 / PLA2 are enzymes that release fatty acids from the second carbon group of glycerol. This particular phospholipase specifically recognizes the sn-2 acyl bond of phospholipids and catalytically hydrolyzes the bond releasing arachidonic acid and lysophospholipids. Phospholipases A2 / PLA2 are commonly found in mammalian tissues as well as insect and snake venom. Venom from both snakes and insects is largely composed of melittin, which is a stimulant of Phospholipases A2 / PLA2. Due to the increased presence and activity of Phospholipases A2 / PLA2 resulting from a snake or insect bite, arachidonic acid is released from the phospholipid membrane disproportionately. As a result, inflammation and pain occur at the site. PLA2G2E catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Has a preference for arachidonic-containing phospholipids.
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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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TMPY-01468 | Neuraminidase Protein, C.perfringens, Recombinant (His) | C.perfringens | E. coli | ||
Clostridium perfringens / C. perfringens (formerly known as C. welchii) is a Gram-positive, rod-shaped, anaerobic, spore-forming bacterium of the genus Clostridium. C. perfringens is ubiquitous in nature and can be found as a normal component of decaying vegetation, marine sediment, the intestinal tract of humans and other vertebrates, insects, and soil. C. perfringens is commonly encountered in infections as a benign component of the normal flora. In this case, its role in disease is minor. Infections due to C. perfringens show evidence of tissue necrosis, bacteremia, emphysematous cholecystitis, and gas gangrene, which is also known as clostridial myonecrosis. NA, also called sialidases, specifically catalyze the hydrolysis removal of terminal sialic acid residues from viral and cellular glycoconjugates. C. Perfringens neuraminidase catalyzes the hydrolysis of alpha-(2->3)-, alpha-(2->6)-, glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates, but has little activity against the α2-8 glycosidic linkages. The function of the neuraminidase is to release sialic acids for use as carbon and energy sources for the non-pathogenic bacterium, while in pathogenic microorganisms, sialidases have been suggested to be pathogenic factors
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