(Z)-10-Hydroxynortriptyline-d3
目录号 : GC67761(Z)-10-Hydroxynortriptyline-d3 是 (Z)-10-Hydroxynortriptyline 的氘代物。(Z)-10-Hydroxynortriptyline 是 Nortriptyline 的代谢物。Nortriptyline 是三环类抗抑郁药，是 Amitriptyline 的主要活性代谢物，用于缓解抑郁症状。
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
(Z)-10-Hydroxynortriptyline-d3 is the deuterium labeled (Z)-10-Hydroxynortriptyline . (Z)-10-Hydroxynortriptyline is a metabolite of Nortriptyline . Nortriptyline is a tricyclic antidepressant and the main active metabolite of Amitriptyline, and is used to relieve the symptoms of depression[1][2].
Stable heavy isotopes of hydrogen, carbon, and other elements have been incorporated into drug molecules, largely as tracers for quantitation during the drug development process. Deuteration has gained attention because of its potential to affect the pharmacokinetic and metabolic profiles of drugs[1].
[1]. Russak EM, et al. Impact of Deuterium Substitution on the Pharmacokinetics of Pharmaceuticals. Ann Pharmacother. 2019 Feb;53(2):211-216.
[2]. Shimoda K, et al. The impact of CYP2C19 and CYP2D6 genotypes on metabolism of amitriptyline in Japanese psychiatric patients. J Clin Psychopharmacol. 2002 Aug;22(4):371-8.
| Cas No. | SDF | Download SDF | |
| 分子式 | C19H18D3NO | 分子量 | 282.39 |
| 溶解度 | 储存条件 | Store at -20°C | |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 3.5412 mL | 17.706 mL | 35.412 mL |
| 5 mM | 0.7082 mL | 3.5412 mL | 7.0824 mL |
| 10 mM | 0.3541 mL | 1.7706 mL | 3.5412 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Cortical Thickness Abnormalities at Different Stages of the Illness Course in Schizophrenia: A Systematic Review and Meta-analysis
JAMA Psychiatry 2022 Jun 1;79(6):560-570.PMID:35476125DOI:10.1001/jamapsychiatry.2022.0799.
Importance: Questions of whether and how cortical thickness (CTh) alterations differ over the course of schizophrenia (SCZ) have yet to be resolved. Objective: To characterize CTh alterations across illness stages in SCZ. Data sources: PubMed, Embase, Web of Science, and Science Direct were screened for CTh studies published before June 15, 2021. Study selection: Original studies comparing whole-brain CTh alterations from healthy controls in individuals at clinical high-risk (CHR), first episode of psychosis (FEP), and long-term illness stages of SCZ were included. Data extraction and synthesis: This preregistered systematic review and meta-analysis followed PRISMA reporting guidelines. Separate and pooled meta-analyses were performed using seed-based d mapping. Meta-regression analyses were conducted. Main outcomes and measures: Cortical thickness differences from healthy control individuals across illness stages. Results: Ten studies comprising 859 individuals with CHR (mean [SD] age, 21.02 [2.66] years; male, 573 [66.7%]), 12 studies including 671 individuals with FEP (mean [SD] age, 22.87 [3.99] years; male, 439 [65.4%]), and 10 studies comprising 579 individuals with long-term SCZ (mean [SD] age, 41.58 [6.95] years; male, 396 [68.4%]) were included. Compared with healthy control individuals, individuals with CHR showed cortical thinning in bilateral medial prefrontal cortex (Z = -1.01; P < .001). Individuals with FEP showed cortical thinning in right lateral superior temporal cortex (Z = -1.34; P < .001), right anterior cingulate cortex (Z = -1.44; P < .001), and right insula (Z = -1.14; P = .002). Individuals with long-term SCZ demonstrated CTh reductions in right insula (Z = -3.25; P < .001), right inferior frontal cortex (Z = -2.19; P < .001), and left (Z = -2.37; P < .001) and right (Z = -1.94; P = .002) temporal pole. There were no significant CTh differences between CHR and FEP. Individuals with long-term SCZ showed greater cortical thinning in right insula (Z = -2.58; P < .001), right inferior frontal cortex (Z = -2.32; P < .001), left lateral temporal cortex (Z = -1.91; P = .002), and right temporal pole (Z = -1.82; P = .002) than individuals with FEP. Combining all studies on SCZ, accelerated age-related CTh reductions were found in bilateral lateral middle temporal cortex and right pars orbitalis in inferior frontal cortex. Conclusions and relevance: The absence of significant differences between FEP and CHR noted in this systematic review and meta-analysis suggests that the onset of psychosis was not associated with robust CTh reduction. The greater cortical thinning in long-term SCZ compared with FEP with accelerated age-related reduction in CTh suggests progressive neuroanatomic alterations following illness onset. Caution in interpretation is needed because heterogeneity in samples and antipsychotic treatment may confound these results.
Comparative review on left-handed Z-DNA
Front Biosci (Landmark Ed) 2021 Apr 30;26(5):29-35.PMID:34027648DOI:10.52586/4922.
Being polymorphic, deoxyribonucleic acid is worthy of raise a variety of structure like right-handed B to left-handed Z conformation. In left-handed contour of DNA consecutive nucleotides substitute between syn-arrangement and anti-arrangement, through the chain. 2D gel electrophoresis comprising d(PCpG)n of topo isomers of a plasmid inserts d(pCpG)n, in this 'n' ranges among 8 to 21, indicate the change of B-Z DNA. The high denseness of salt is required for conversion of B configuration d(CG)n toward Z configuration. The rate of B to Z transition is measured by "Cytosine Analogues" and "Fluorescence Spectroscopy". h-ZαADAR1 that a Z-DNA's binding domain, binds and stabilizes one part in Z configuration and therefore the remaining half in B deoxyribonucleic acid configuration. At halfway point, it creates B-Z junction. "Stacking" is the main reason for the B-Z DNA junction construction. Upregulation of ADAM-12, related with Z-DNA is said to a cause for cancer, arthritis, and hypertrophy. Z-DNA forming sequence (ZFS) conjointly generates massive - scale deletion in cells from mammals.
H2A.Z's 'social' network: functional partners of an enigmatic histone variant
Trends Biochem Sci 2022 Nov;47(11):909-920.PMID:35606214DOI:10.1016/j.tibs.2022.04.014.
The histone variant H2A.Z has been extensively studied to understand its manifold DNA-based functions. In the past years, researchers identified its specific binding partners, the 'H2A.Z interactome', that convey H2A.Z-dependent chromatin changes. Here, we summarize the latest findings regarding vertebrate H2A.Z-associated factors and focus on their roles in gene activation and repression, cell cycle regulation, (neuro)development, and tumorigenesis. Additionally, we demonstrate how protein-protein interactions and post-translational histone modifications can fine-tune the complex interplay of H2A.Z-regulated gene expression. Last, we review the most recent results on interactors of the two isoforms H2A.Z.1 and H2A.Z.2.1, which differ in only three amino acids, and focus on cancer-associated mutations of H2A and H2A.Z, which reveal fascinating insights into the functional importance of such minuscule changes.
[Protein Z]
Pol Merkur Lekarski 2003 Dec;15(90):574-6.PMID:15058266doi
Protein Z (PZ) is a 6.2 kDa vitamin K-dependent protein, synthesized in the liver. The gene for human PZ is localized to chromosome 13 at band 34 q. The structure of PZ is very similar to that of factors VII, IX, X and protein C. Very low plasma levels of protein Z were observed under oral anticoagulant treatment. The cause of this phenomenon might be increased protein Z binding on the surface of endothelial cells. Protein Z is consumed during coagulopathy. About 60% of humans suffering from a bleeding tendency of unknown origin presented with decreased plasma levels of protein Z. PZ forms a Ca(2+)-dependent complex with activated factor X (Xa) on phospholipid surfaces, that leads to the inhibition of factor Xa and decrease in thrombin generation. Inhibition of factor Xa may be caused directly by protein Z or indirectly by the activity of protein Z-dependent protease inhibitor (ZPI). ZPI is a 72 kDa member of the serpin family of proteinase inhibitors, synthesized in the liver. ZPI circulates in plasma in complex with protein Z. ZPI in the presence of Ca2+ and phospholipids inhibits factor Xa. The presence of protein Z enhances this process by more than 1000 times. ZPI also inhibits activated factor XI in the absence of protein Z, Ca2+ or phospholipids. Protein Z deficiency may induce bleeding as well as prothrombotic tendencies and might occur as an inherited disorder. Protein Z deficiency may aggravate mild bleeding tendency in subjects with diagnosed borderline decrease in von Willebrand factor and factor VII activity. Patients presenting with factor V Leiden mutation and low protein Z levels show earlier onset and higher frequency of thromboembolic events comparing to patients with normal protein Z levels.
Some thoughts on choosing a Z-plasty: the Z made simple
Plast Reconstr Surg 2000 Sep;106(3):665-71.PMID:10987477DOI:10.1097/00006534-200009030-00024.
The Z-plasty and its variations are techniques commonly performed in plastic surgery. However, there are few descriptions and comparisons of the various types of Z-plasty. This article examines the mechanics of the Z-plasty and its variations. Understanding the geometry of the different variations will allow selection of the most appropriate Z-plasty for contracture release.