目录号 | 产品详情 | 靶点 | |
---|---|---|---|
T36828 | |||
(9Z)-Tricosene is a pheromone released by insects, including D. melanogaster, M. domestica (house fly), and A. mellifera L. (honey bee). In Drosophila, it induces aggregation behavior and is an oviposition guidance cue for females. Due to its aggregation-inducing activity, it is used as a bait pesticide to attract insects to traps. The mechanism of action in Drosophila is the activation of antennal basiconic Or7a receptors. It is also highly produced by honey bees during the waggle dance, which is a complex communication process used to alert nest-mates of the location and profitability of a food source. When injected into a hive, (9Z)-tricosene induced foraging behavior. | |||
TN3910 | Apoptosis ATPase Glucocorticoid Receptor Potassium Channel Sodium Channel Endogenous Metabolite Autophagy | ||
Ecdysone 是存在于昆虫和草药中的主要类固醇激素,可以激活盐皮质激素受体并诱导细胞凋亡。Ecdysone 的活性代谢物 20-羟基蜕皮激素在协调发育过渡和体内稳态睡眠调节中起重要作用。 | |||
T83165 | |||
Adipokinetic Hormone (Apis mellifera ligustica, Bombyx mori, Heliothis zea, Manduca sexta) 是昆虫肽类激素,能强烈诱导促脂肪/高海藻素反应,但不具备糖原动员功能,亦不能在脂肪体内有效储存及利用糖原。 | |||
T73614 | |||
Tyrosine decarboxylase (TDC; TyrDC),即酪氨酸脱羧酶,广泛存在于植物、昆虫和不同微生物中,常用于生化研究。Tyrosine decarboxylase 是一种5'-磷酸吡哆醛 (PLP) 依赖性脱羧酶,可以催化酪氨酸中羧基的去除,产生酪胺和二氧化碳。 | |||
T37922 | |||
Unsaturated, long-chain hydrocarbons are found on the cuticles of insects and can act as pheromones. In mature Drosophila melanogaster, certain cuticular hydrocarbons are sexually dimorphic: males synthesize 23- and 25-C monoenes and females produce 27- and 29-C dienes. Each of these lipids plays specific roles in regulating male sexual behavior, with dienes stimulating courtship. 7(Z),11(Z)-Pentacosadiene is a 25-C hydrocarbon that is found in low abundance on cuticles of mature Drosophila females. Depletion of a female-specific elongase (eloF), which leads to an increase in 7(Z),11(Z)-pentacosadiene along with a parallel decrease in 7,11-nonacosadiene, significantly reduces copulation in Drosophila. This raises the possibility that 7(Z),11(Z)-pentacosadiene may act as an anti-aphrodisiac. | |||
T37924 | |||
7(Z)-Tricosene is an unsaturated cuticular hydrocarbon that acts as a pheromone in some insects, including Drosophila. While it is present in both sexes of some Drosophila species, it is abundant in males, but not females, of D. melanogaster and D. sechellia. In these species, 7(Z)-tricosene prevents or reduces male courtship behavior and increases female sexual receptivity. It is absent from virgin D. melanogaster females, but is transferred from males to females during mating. In addition, mating induces the synthesis of 7(Z)-tricosene by D. melanogaster females, so that it acts as an anti-aphrodisiac in mated females. 7(Z)-Tricosene is also a minor component of labial gland secretion and cuticle of Bombus spp. |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
---|---|---|---|---|---|
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.
|
|||||
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.
|
|||||
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.
|
|||||
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).
|
|||||
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).
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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
|