His-[D-2-ME-Trp]-Ala
目录号 : GC34237His-[D-2-ME-Trp]-Ala是生长激素hexarelin的片段。
Sample solution is provided at 25 µL, 10mM.
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- Purity: >99.50%
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His-[D-2-ME-Trp]-Ala is a fragment of the growth hormone hexarelin.
Cas No. | SDF | ||
Canonical SMILES | His-{d-2-Me-Trp}-Ala | ||
分子式 | C21H26N6O4 | 分子量 | 426.47 |
溶解度 | Water : ≥ 50 mg/mL (117.24 mM) | 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 | |||
1 mg | 5 mg | 10 mg | |
1 mM | 2.3448 mL | 11.7242 mL | 23.4483 mL |
5 mM | 0.469 mL | 2.3448 mL | 4.6897 mL |
10 mM | 0.2345 mL | 1.1724 mL | 2.3448 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。
His-Ala-Phe-Lys peptide from Burkholderia arboris possesses antifungal activity
Burkholderia arboris, which belongs to the Burkholderia cepacia complex, has been shown to possess antifungal activity against several plant fungal pathogens; however, the antifungal compounds are yet to be identified. Here, we identified the antifungal compounds produced by B. arboris using genetic and metabolomic approaches. We generated a Tn5 transposon mutation library of 3,000 B. arboris mutants and isolated three mutants with reduced antifungal activity against the plant fungal pathogen Fusarium oxysporum. Among the mutants, the M464 mutant exhibited the weakest antifungal activity. In the M464 genome, the transposon was inserted into the cobA gene, encoding uroporphyrin-III methyltransferase. Deletion of the cobA gene also resulted in reduced antifungal activity, indicating that the cobA gene contributed to the antifungal activity of B. arboris. Furthermore, a comparison of the differential metabolites between wild type B. arboris and the ?cobA mutant showed a significantly decreased level of tetrapeptide His-Ala-Phe-Lys (Hafk) in the ?cobA mutant. Therefore, a Hafk peptide with D-amino acid residues was synthesized and its antifungal activity was evaluated. Notably, the Hafk peptide displayed significant antifungal activity against F. oxysporum and Botrytis cinerea, two plant pathogens that cause destructive fungal diseases. Overall, a novel antifungal compound (Hafk) that can be used for the biocontrol of fungal diseases in plants was identified in B. arboris.
Human "autotomy"
We describe two cases of self-injurious behaviour. One was a man with central post-stroke pain with maximal pain in the tip of the nose, who excavated his ala nasae--in which he subsequently continued to experience phantom pain. The second case a man who, following ophthalmic herpes zoster and possibly mild postherpetic neuralgia. He subsequently scratched his anaesthetic forehead down to the bone, while denying he experienced any pain. We would describe the first case as one of true autotomy; but the second as destruction of an anaesthetic part of the body. The implications for human and animal physiopathology are discussed.
Glycyl-alanyl-histidine protects PC12 cells against hydrogen peroxide toxicity
Background: Peptides with cytoprotective functions, including antioxidants and anti-infectives, could be useful therapeutics. Carnosine, β-alanine-histidine, is a dipeptide with anti-oxidant properties. Tripeptides of Ala-His-Lys, Pro-His-His, or Tyr-His-Tyr are also of interest in this respect.
Results: We synthesized several histidine-containing peptides including glycine or alanine, and tested their cytoprotective effects on hydrogen peroxide toxicity for PC12 cells. Of all these peptides (Gly-His-His, Ala-His-His, Ala-His-Ala, Ala-Ala-His, Ala-Gly-His, Gly-Ala-His (GAH), Ala-His-Gly, His-Ala-Gly, His-His-His, Gly-His-Ala, and Gly-Gly-His), GAH was found to have the strongest cytoprotective activity. GAH decreased lactate dehydrogenase (LDH) leakage, apoptosis, morphological changes, and nuclear membrane permeability changes against hydrogen peroxide toxicity in PC12 cells. The cytoprotective activity of GAH was superior to that of carnosine against hydrogen peroxide toxicity in PC12 cells. GAH also protected PC12 cells against damage caused by actinomycin D and staurosporine. Additionally, it was found that GAH also protected SH-SY5Y and Jurkat cells from damage caused by hydrogen peroxide, as assessed by LDH leakage.
Conclusion: Thus, a novel tripeptide, GAH, has been identified as having broad cytoprotective effects against hydrogen peroxide-induced cell damage.
Detection of ADAM15 in urine from patients with bladder cancer
Cancer is one of the leading causes of death in the United States and Europe. Of the cancers, bladder cancer is the 10th most frequently diagnosed cancer and the 13th most frequently diagnosed cancer in men. There are many studies showing that proteolytic enzymes, e.g. A Disintegrin and Metalloproteinases (ADAMs), play a key role in the development and progression of neoplasms. In this paper, we present the use of chromogenic substrate of ADAM15 for the qualitative determination of specific activity of enzyme in urine of patients with confirmed bladder cancer. In the first step, we optimized the substrate molecule in non-primed positions using combinatorial chemistry. By means of the obtained ABZ-His-Ala-Arg-Gly-ANB-NH2 peptide, we detected ADAM15 activity in urine samples collected from patients diagnosed with bladder cancer. In contrast, we did not observe such activity in urine obtained from healthy volunteers.
[Pt(dien)]2+ migrates intramolecularly from methionine S to imidazole Nepsilon2 in the peptides H-His-Gly-Met-OH and Ac-His-Ala-Ala-Ala-Met-NHPh
The pH- and time-dependent reaction of [Pt(dien)(H2O)]2+ with the methionine- and histidine-containing peptides H-His-Gly-Met-OH and Ac-His-Ala-Ala-Ala-Met-NHPh at 313 K has been investigated by HPLC and NMR spectroscopy. For both peptides, initial relatively rapid formation of the kinetically favoured methionine S-bound complex is followed by slow intramolecular migration of the [Pt(dien)]2+ fragment to imidazole Nepsilon2 (or, in the case of H-His-Gly-Met-OH, to a much lesser extent to the competing imidazole Ndelta1) of the histidine side chain over a period of 500 h. Time-dependent studies for the pentapeptide at pH 8.0 demonstrate that this isomerization can take place by either direct S-->Nepsilon2 migration or by a two-step mechanism involving initial Nepsilon2 coordination of a second [Pt(dien)]2+ fragment and subsequent cleavage of the orginal Pt-S bond in the resulting dinuclear complex. The rate of kappaS/kappaNepsilon2 isomerization is markedly reduced on lowering the pH to 5.1.