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Neurotensin (8-13) (trifluoroacetate salt) Sale

目录号 : GC44386

A neuropeptide

Neurotensin (8-13) (trifluoroacetate salt) Chemical Structure

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1mg
¥1,456.00
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Sample solution is provided at 25 µL, 10mM.

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产品描述

Neurotensin (8-13) is a neuropeptide that corresponds to the C-terminal residues 8-13 of neurotensin that binds to rat synaptic membranes with a Ki value of 13 nM. It induces contraction of guinea pig ileum (EC50 = 25 nM) and induces contraction of rat fundus equipotently to full length neurotensin (EC50s = 1.29 and 1.58 nM, respectively). In vivo, neurotensin (8-13) has antinociceptive effects in a mouse tail pressure test (ED50 = 50 nmol per animal). It induces extracellular dopamine release in the prefrontal cortex in rats. Neurotensin (8-13) also decreases diastolic blood pressure in a dose-dependent manner in normotensive rats without affecting heart rate.

Chemical Properties

Cas No. SDF
Canonical SMILES [H]N[C@@H](CCCNC(N)=N)C(N[C@@H](CCCNC(N)=N)C(N1CCC[C@H]1C(N[C@H](C(N[C@]([C@H](CC)C)([H])C(N[C@@H](CC(C)C)C(O)=O)=O)=O)CC2=CC=C(O)C=C2)=O)=O)=O.FC(F)(C(O)=O)F
分子式 C38H64N12O8•XCF3COOH 分子量 817
溶解度 Water: 1 mg/ml 储存条件 Store at -20°C
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溶解性数据

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1 mg 5 mg 10 mg
1 mM 1.224 mL 6.12 mL 12.2399 mL
5 mM 0.2448 mL 1.224 mL 2.448 mL
10 mM 0.1224 mL 0.612 mL 1.224 mL
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Research Update

Peptide characterization with a sulfoethyl aspartamide column

J Chromatogr 1988 Jun 29;443:63-71.PMID:2844842DOI:10.1016/s0021-9673(00)94783-6

A strong cation-exchange (SCX) high-performance liquid chromatography column (sulfoethyl aspartamide, 200 x 4.6 mm) was used to analyze more than 50 peptides, ranging in length from 5 to 20 residues. These data show that the elution positions of the peptides increase monotonically with the number of positively charged residues. [A 60-min linear gradient of 0 to 100% eluent B at 1 ml/min was used, where eluent A is 5 mM phosphate (pH 3.0)-acetonitrile (75:25) and eluent B is eluent A + 0.5 M sodium chloride.] A comparison of SCX with a standard C18 reversed-phase (RP) column [60-min linear gradient of 0 to 60% B at 1 ml/min, where eluent A is 0.1% trifluoroacetic acid (TFA), and eluent B is 0.095% TFA-acetonitrile (10:90)] further demonstrates the utility of SCX in peptide characterization. SCX separated an (Arg)3-containing peptide from the Arg-deleted peptide while RP could not. In addition, SCX and RP resolved the methionine oxidation products of ACTH (4-10) (RP: Met [O] less than Met [O2] less than Met; SCX; Met [O] less than Met less than Met [O2]), suggesting a mixed-mode mechanism for the ion-exchange system. Finally, SCX separated the sulfated and non-sulfated forms of cholecystokinin (26-33) and Leu-enkephalin as well as the N-terminal acetylated forms of Neurotensin \(8-13\) and angiotensinogen (1-14) from the respective unmodified peptides.