目录号 | 产品详情 | 靶点 | |
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T23324 | Others | ||
NOP receptor antagonist | |||
T37013 | |||
Selective sigma (σ) receptor ligand. Displays high affinity for σ1; also binds at σ2 sites (Ki = 1.5 nM and 50.8 nM respectively). Selective over a range of receptor types including dopaminergic and muscarinic receptors, DAT and SERT. Prezzavento et al (2007) Novel sigma receptor ligands: synthesis and biological profile. J.Med.Chem. 50 951 PMID:17328523 |Prezzavento et al (2008) A new sigma ligand, (±)-PPCC, antagonizes kappa opioid receptor-mediated antinociceptive effect. Life Sci. 82 549 PMID:18261749 |Antonini et al (2009) Anti-amnesic properties of (±)-PPCC, a novel sigma receptor ligand, on cognitive dysfunction induced by selective cholinergic lesion in rats. J.Neurochem. 109 744 PMID:19245662 | |||
T36376 | |||
SB-612111 is a novel and potent human opiate receptor-like orphan receptor (ORL-1) antagonist with a high affinity for hORL-1 (Ki=0.33 nM). SB-612111 exhibits selectivity for μ-, κ- and δ-receptors with Ki values of 57.6 nM, 160.5 nM and 2109 nM, respecticely. SB-612111 effectively antagonizes the pronociceptive action of Nociceptin in an acute pain model[1]. [1]. Paola F Zaratin, et al. Modification of Nociception and Morphine Tolerance by the Selective Opiate Receptor-Like Orphan Receptor Antagonist (-)-cis-1-methyl-7-[[4-(2,6-dichlorophenyl)piperidin-1-yl]methyl]-6,7,8,9-tetrahydro-5H-benzocyclohepten-5-ol (SB-612111).J Pharmacol Exp Ther. 2004 Feb;308(2):454-61. |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-04733 | OPCML Protein, Rat, Recombinant (hFc) | Rat | HEK293 | ||
Opioid-binding Cell Adhesion Molecule (OBCAM), also known as OPCML, is a GPI-anchored cell adhesion molecule in the plasma membrane. This neuron-specific protein consists of three immunoglobulin (Ig)-like domains anchored to the membrane through a glycosylphosphatidylinositol (GPI)-tail. OPCML also belongs to the member of the IgLON family, a subgroup of the immunoglobulin superfamily, consisting of three members, LAMP, OBCAM, and Neurotrimin. These molecules interact homophilically and heterophilically within the family, and OBCAM acts only as heterodimers with LAMP or Neurotrimin and possibly inhibits neurite outgrowth from cerebellar granule cells. The OBCAM has been presumed to play a role as a cell adhesion/recognition molecule. Furthermore, the OPCML protein defects may play an important role in the carcinogenesis of cervical or ovarian cancers, and this gene is regarded as a candidate TSG (tumor suppressor gene).
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TMPY-00893 | OPCML Protein, Human, Recombinant (His) | Human | HEK293 | ||
Opioid-binding Cell Adhesion Molecule (OBCAM), also known as OPCML, is a GPI-anchored cell adhesion molecule in the plasma membrane. This neuron-specific protein consists of three immunoglobulin (Ig)-like domains anchored to the membrane through a glycosylphosphatidylinositol (GPI)-tail. OPCML also belongs to the member of the IgLON family, a subgroup of the immunoglobulin superfamily, consisting of three members, LAMP, OBCAM, and Neurotrimin. These molecules interact homophilically and heterophilically within the family, and OBCAM acts only as heterodimers with LAMP or Neurotrimin and possibly inhibits neurite outgrowth from cerebellar granule cells. The OBCAM has been presumed to play a role as a cell adhesion/recognition molecule. Furthermore, the OPCML protein defects may play an important role in the carcinogenesis of cervical or ovarian cancers, and this gene is regarded as a candidate TSG (tumor suppressor gene).
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TMPY-03818 | OPCML Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Opioid-binding Cell Adhesion Molecule (OBCAM), also known as OPCML, is a GPI-anchored cell adhesion molecule in the plasma membrane. This neuron-specific protein consists of three immunoglobulin (Ig)-like domains anchored to the membrane through a glycosylphosphatidylinositol (GPI)-tail. OPCML also belongs to the member of the IgLON family, a subgroup of the immunoglobulin superfamily, consisting of three members, LAMP, OBCAM, and Neurotrimin. These molecules interact homophilically and heterophilically within the family, and OBCAM acts only as heterodimers with LAMP or Neurotrimin and possibly inhibits neurite outgrowth from cerebellar granule cells. The OBCAM has been presumed to play a role as a cell adhesion/recognition molecule. Furthermore, the OPCML protein defects may play an important role in the carcinogenesis of cervical or ovarian cancers, and this gene is regarded as a candidate TSG (tumor suppressor gene).
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TMPJ-00737 | PDYN Protein, Human, Recombinant (His) | Human | Human Cells | ||
Proenkephalin-B(PDYN), belongs to the opioid neuropeptide precursor family. The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing. Leu-enkephalins, which is a type of Proenkephalin-B, compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress. Dynorphin peptides differentially regulate the kappa opioid receptor. Dynorphin A has a typical opiod activity, it is 700 times more potent than Leu-enkephalin.
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TMPH-00055 | Alpha-toxin Amm8 Protein, Androctonus mauritanicus, Recombinant (His & Myc) | Androctonus mauritanicus | Baculovirus | ||
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 toxin principally slows the inactivation process of TTX-sensitive sodium channels. It discriminates neuronal versus muscular sodium channel, as it is more potent on rat brain Nav1.2/SCN2A (EC(50)=29 nM) than on rat skeletal muscle Nav1.4/SCN4A (EC(50)=416 nM). It also shows a weak activity on Nav1.7/SCN9A (EC(50)=1.76 uM). In vivo, the toxin produces pain hypersensibility to mechanical and thermal stimuli.(PubMed:23685008). It also exhibits potent analgesic activity (when injected intraperitoneally), increasing hot plate and tail flick withdrawal latencies in a dose-dependent fashion. This paradoxical analgesic action, is significantly suppressed by opioid receptor antagonists, suggesting a pain-induced analgesia mechanism that involves an endogenous opioid system. This led to hypothesis that pain relief induced by peripheral administration of Amm VIII may result from sensitization of primary afferent neurons and subsequent activation of an opioid-dependent noxious inhibitory control.
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TMPJ-00513 | LTF Protein, Human, Recombinant (His) | Human | Human Cells | ||
Lactotransferrin is a member of the transferrin family that transfer iron to the cells and control the level of free iron in the blood and external secretions. Lactotransferrin is a secreted protein and contains two transferrin-like domains. Lactotransferrin can be cleaved into the following four chains: Kaliocin-1, Lactoferroxin-A, Lactoferroxin-B, and Lactoferroxin-C. Lactoferroxin A, Lactoferroxin B, and Lactoferroxin C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while Lactoferroxin B and Lactoferroxin C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors. LTF has antimicrobial activity (bacteriocide, fungicide) and is part of the innate defense, mainly at mucoses.
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TMPY-04121 | NAGA Protein, Human, Recombinant (His) | Human | HEK293 | ||
NAGA (Alpha-N-Acetylgalactosaminidase) is a Protein Coding gene. NAGA encodes the lysosomal enzyme alpha-N-acetylgalactosaminidase, which cleaves alpha-N-acetylgalactosaminyl moieties from glycoconjugates. It belongs to the glycosyl hydrolase 27 family. The antinociceptive effect of NAGA may involve the participation of endogenous opioid peptides and endogenous catecholamines. Normal alpha-NAGA is synthesized as a 52 kDa precursor which matures to a 49 kDa species through phosphorylation and carbohydrate trimming. Mutations in gene encoding alpha-NAGA cause a wide range of diseases, characterized by mild to severe clinical features. NAGA is widely expressed in the placenta, appendix, and other tissues. Diseases associated with NAGA include Kanzaki Disease and Schindler Disease, Type I.
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TMPY-01800 | NEGR1 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Neuronal Growth Regulator 1, NEGR1, also known as neurotractin, or KILON, belongs to the immunoglobulin superfamily, IgLON family. This GPI-linked cell surface glycoprotein NEGR1 is composed of three Ig-like domains and belongs to the IgLON subgroup of neural IgSF members. It is expressed in two isoforms with apparent molecular masses of 50 and 37 kD, termed L-form and S-form, respectively. NEGR1/Neurotractin participates in the regulation of neurite outgrowth in the developing brain and is expressed on the neurites of primary hippocampal neurons. Neurotractin/KILON is a trans-neural growth-promoting factor for outgrowing axons following hippocampal denervation. KILON (kindred of IgLON) and opioid-binding cell adhesion molecule, together with the limbic system-associated membrane protein and neurotrophin, belong to the IgLON subgroup of immunoglobulin superfamily. The alteration of the modulatory function of KILON/NEGR1 for the number of dendritic synapses concomitant with changes in its localization and detergent solubility during neuronal culture development. In addition to its reported role in the brain, NEGR1 is also expressed in subcutaneous adipose tissue and acts as a central 'hub' in an obesity-related transcript network.
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TMPY-01913 | NEGR1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Neuronal Growth Regulator 1, NEGR1, also known as neurotractin, or KILON, belongs to the immunoglobulin superfamily, IgLON family. This GPI-linked cell surface glycoprotein NEGR1 is composed of three Ig-like domains and belongs to the IgLON subgroup of neural IgSF members. It is expressed in two isoforms with apparent molecular masses of 50 and 37 kD, termed L-form and S-form, respectively. NEGR1/Neurotractin participates in the regulation of neurite outgrowth in the developing brain and is expressed on the neurites of primary hippocampal neurons. Neurotractin/KILON is a trans-neural growth-promoting factor for outgrowing axons following hippocampal denervation. KILON (kindred of IgLON) and opioid-binding cell adhesion molecule, together with the limbic system-associated membrane protein and neurotrophin, belong to the IgLON subgroup of immunoglobulin superfamily. The alteration of the modulatory function of KILON/NEGR1 for the number of dendritic synapses concomitant with changes in its localization and detergent solubility during neuronal culture development. In addition to its reported role in the brain, NEGR1 is also expressed in subcutaneous adipose tissue and acts as a central 'hub' in an obesity-related transcript network.
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TMPY-02188 | Lactoferrin/LTF Protein, Human, Recombinant (His) | Human | HEK293 | ||
Lactotransferrin, also known as Lactoferrin, Talalactoferrin, and LTF, is a secreted protein that belongs to the transferrin family. Transferrins are iron binding transport proteins that can bind two Fe3+ions in association with the binding of an anion, usually bicarbonate. Lactotransferrin has antimicrobial activity which depends on the extracellular cation concentration. Lactoferroxins A, B, and C have opioid antagonist activity. Lactoferrin A shows a preference for mu-receptors, while lactoferricin B and lactoferricin C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors. Lactoferrin / LTF is a globular glycoprotein that is widely represented in various secretory fluids, such as milk, saliva, tears, and nasal secretions. Lactoferrin / LTF is also present in secondary granules of PMN and is secreted by some acinar cells. Lactoferrin / LTF can be purified from milk or produced recombinantly. Human colostrum has the highest concentration, followed by human milk, then cow milk. Lactoferrin / LTF is one of the components of the immune system of the body; it has antimicrobial activity (bacteriocide, fungicide) and is part of the innate defense, mainly at mucose. In particular, lactoferrin provides an antibacterial activity to human infants. Lactoferrin interacts with DNA and RNA, polysaccharides and heparin, and shows some of its biological functions in complexes with these ligands.
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TMPY-02728 | Lactoferrin/LTF Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Lactotransferrin, also known as Lactoferrin, Talalactoferrin, and LTF, is a secreted protein that belongs to the transferrin family. Transferrins are iron binding transport proteins that can bind two Fe3+ions in association with the binding of an anion, usually bicarbonate. Lactotransferrin has antimicrobial activity which depends on the extracellular cation concentration. Lactoferroxins A, B, and C have opioid antagonist activity. Lactoferrin A shows a preference for mu-receptors, while lactoferricin B and lactoferricin C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors. Lactoferrin / LTF is a globular glycoprotein that is widely represented in various secretory fluids, such as milk, saliva, tears, and nasal secretions. Lactoferrin / LTF is also present in secondary granules of PMN and is secreted by some acinar cells. Lactoferrin / LTF can be purified from milk or produced recombinantly. Human colostrum has the highest concentration, followed by human milk, then cow milk. Lactoferrin / LTF is one of the components of the immune system of the body; it has antimicrobial activity (bacteriocide, fungicide) and is part of the innate defense, mainly at mucose. In particular, lactoferrin provides an antibacterial activity to human infants. Lactoferrin interacts with DNA and RNA, polysaccharides and heparin, and shows some of its biological functions in complexes with these ligands.
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