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Phenelzine-d5 (sulfate) Sale

(Synonyms: 硫酸苯乙肼 d5 (硫酸盐)) 目录号 : GC46200

An internal standard for the quantification of phenelzine

Phenelzine-d5 (sulfate) Chemical Structure

Cas No.:1219798-40-9

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500μg
¥2,141.00
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1mg
¥4,078.00
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产品描述

Phenelzine-d5 (sulfate) is intended for use as an internal standard for the quantification of phenelzine by GC- or LC-MS. Phenelzine is an inhibitor of monoamine oxidase (MAO; IC50 = 0.9 μM using rat brain mitochondrial preparations).1 It potentiates the effects of tryptamine on isolated rat fundus (EC50 = 90 nM) and increases tryptamine toxicity in mice with LD50 values of 85 and 500 mg/kg in the presence and absence of phenelzine, respectively. Phenelzine (20 mg/kg) increases GABA, dopamine, serotonin , and norepinephrine levels in the hippocampus and cortex of socially isolated rats and rats treated with the NMDA receptor antagonist (+)-MK-801 .2 It also increases 5-HT levels in the ventral horn of the spinal cord, improves gross motor ability in a rotarod test, and increases locomotor activity in an open field test in mice with experimental autoimmune encephalomyelitis when administered at a dose of 30 mg/kg.3

Chemical Properties

Cas No. 1219798-40-9 SDF
别名 硫酸苯乙肼 d5 (硫酸盐)
Canonical SMILES NNCCC1=C([2H])C([2H])=C([2H])C([2H])=C1[2H].O=S(O)(O)=O
分子式 C8H7D5N2 • H2SO4 分子量 239.3
溶解度 DMSO: soluble,Methanol: soluble,Water: soluble 储存条件 Store at -20°C
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溶解性数据

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1 mM 4.1789 mL 20.8943 mL 41.7885 mL
5 mM 0.8358 mL 4.1789 mL 8.3577 mL
10 mM 0.4179 mL 2.0894 mL 4.1789 mL
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Research Update

Sulfated glycans in inflammation

Eur J Med Chem 2015 Mar 6;92:353-69.PMID:25576741DOI:10.1016/j.ejmech.2015.01.002.

Sulfated glycans such as glycosaminoglycans on proteoglycans are key players in both molecular and cellular events of inflammation. They participate in leukocyte rolling along the endothelial surface of inflamed sites; chemokine regulation and its consequential functions in leukocyte guidance, migration and activation; leukocyte transendothelial migration; and structural assembly of the subendothelial basement membrane responsible to control tissue entry of cells. Due to these and other functions, exogenous sulfated glycans of various structures and origins can be used to interventionally down-regulate inflammation processes. In this review article, discussion is given primarily on the anti-inflammatory functions of mammalian heparins, heparan sulfate, chondroitin sulfate, dermatan sulfate and related compounds as well as the holothurian fucosylated chondroitin sulfate and the brown algal fucoidans. Understanding the underlying mechanisms of action of these sulfated glycans in inflammation, helps research programs involved in developing new carbohydrate-based drugs aimed to combat acute and chronic inflammatory disorders.

Sulfated plant peptide hormones

J Exp Bot 2019 Aug 19;70(16):4267-4277.PMID:31231771DOI:10.1093/jxb/erz292.

Sulfated peptides are plant hormones that are active at nanomolar concentrations. The sulfation at one or more tyrosine residues is catalysed by tyrosylprotein sulfotransferase (TPST), which is encoded by a single-copy gene. The sulfate group is provided by the co-substrate 3´-phosphoadenosine 5´-phosphosulfate (PAPS), which links synthesis of sulfated signaling peptides to sulfur metabolism. The precursor proteins share a conserved DY-motif that is implicated in specifying tyrosine sulfation. Several sulfated peptides undergo additional modification such as hydroxylation of proline and glycosylation of hydroxyproline. The modifications render the secreted signaling molecules active and stable. Several sulfated signaling peptides have been shown to be perceived by leucine-rich repeat receptor-like kinases (LRR-RLKs) but have signaling pathways that, for the most part, are yet to be elucidated. Sulfated peptide hormones regulate growth and a wide variety of developmental processes, and intricately modulate immunity to pathogens. While basic research on sulfated peptides has made steady progress, their potential in agricultural and pharmaceutical applications has yet to be explored.

Sulfation pathways from red to green

J Biol Chem 2019 Aug 16;294(33):12293-12312.PMID:31270211DOI:10.1074/jbc.REV119.007422.

Sulfur is present in the amino acids cysteine and methionine and in a large range of essential coenzymes and cofactors and is therefore essential for all organisms. It is also a constituent of sulfate esters in proteins, carbohydrates, and numerous cellular metabolites. The sulfation and desulfation reactions modifying a variety of different substrates are commonly known as sulfation pathways. Although relatively little is known about the function of most sulfated metabolites, the synthesis of activated sulfate used in sulfation pathways is essential in both animal and plant kingdoms. In humans, mutations in the genes encoding the sulfation pathway enzymes underlie a number of developmental aberrations, and in flies and worms, their loss-of-function is fatal. In plants, a lower capacity for synthesizing activated sulfate for sulfation reactions results in dwarfism, and a complete loss of activated sulfate synthesis is also lethal. Here, we review the similarities and differences in sulfation pathways and associated processes in animals and plants, and we point out how they diverge from bacteria and yeast. We highlight the open questions concerning localization, regulation, and importance of sulfation pathways in both kingdoms and the ways in which findings from these "red" and "green" experimental systems may help reciprocally address questions specific to each of the systems.

[Production and application of 3-phosphoadenosine-5- phosphosulfate]

Sheng Wu Gong Cheng Xue Bao 2019 Jul 25;35(7):1222-1233.PMID:31328479DOI:10.13345/j.cjb.180527.

Sulfated compounds are widely present in cytoplasm, on cell surface, and in extracellular matrix. These compounds play important roles in cell development, differentiation, immune response, detoxication, and cell signal transduction. 3-Phosphoadenosine-5-phosphosulfate (PAPS) is the universal sulfate group donor for the biosynthesis of sulfated compounds. Up to now, the synthesis of PAPS is still too expensive for industrial applications. This review focuses on the recent progress of PAPS production and summaries the application of PAPS, particularly in the production of glucosinolate, heparin, condroitin sulfate, and oxamniquine production.

Multi-faceted substrate specificity of heparanase

Matrix Biol 2013 Jun 24;32(5):223-7.PMID:23499529DOI:10.1016/j.matbio.2013.02.006.

Heparan sulfate is a highly sulfated polysaccharide abundantly present in the extracellular matrix. Heparan sulfate consists of a disaccharide repeating unit of glucosamine and glucuronic and iduronic acid residues. The functions of heparan sulfate are largely dictated by its size as well as the sulfation patterns. Heparanase is an enzyme that cleaves heparan sulfate polysaccharide into smaller fragments, regulating the functions of heparan sulfate. Understanding the substrate specificity plays a critical role in dissecting the biological functions of heparanase and heparan sulfate. The prevailing view is that heparanase recognizes specific sulfation patterns in heparan sulfate. However, emerging evidence suggests that heparanase is capable of varying its substrate specificities depending on the saccharide structures around the cleavage site. The plastic substrate specificity suggests a complex role of heparanase in regulating the structures of heparan sulfate in matrix biology.