9001-64-3|苹果酸脱氢酶|Malate dehydrogenase|-范德生物科技公司

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苹果酸脱氢酶
NMR and HPLC COA下载 MSDS下载
Names：
Malate dehydrogenase
CAS号：
9001-64-3
MDL Number：
MF(分子式)： NULL MW(分子量)： 0
EINECS:232-622-5 Reaxys Number:
Pubchem ID:318694880 Brand:BIOFOUNT

苹果酸脱氢酶(9001-64-3,Malate dehydrogenase)在所有生物体中均存在，是生物糖代谢过程中的关键酶之一，能催化苹果酸与草酰乙酸之间的可逆转换。

货品编码	规格	纯度	价格 (¥)	现价(¥)	特价(¥)	库存描述	数量	总计 (¥)
SS4087-5KU	5KU	酶活: 30KU/ML	¥ 560.00	¥ 560.00		3-5days	- +	¥ 0.00

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中文别名	苹果酸脱氢酶(9001-64-3,Malate dehydrogenase);人重组肝细胞生长因子;苹果酸脱氢酶（悬浮液）;苹果酸脱氢酶(猪心);苹果酸脱氢酶(微生物)
英文别名	Malate dehydrogenase(9001-64-3);EC 1.1.1.37
CAS号	9001-64-3
SMILES	No data available
Inchi	No data available
InchiKey	No data available
分子式 Formula	NULL
分子量 Molecular Weight	0
闪点 FP	No data available
熔点 Melting point	No data available
沸点 Boiling point	No data available
Polarizability极化度	No data available
密度 Density	No data available
蒸汽压 Vapor Pressure	No data available
溶解度Solubility	No data available
性状	混浊液体
储藏条件 Storage conditions	2-8°C

苹果酸脱氢酶(9001-64-3,Malate dehydrogenase)实验注意事项：
1.使用9001-64-3实验前需戴好防护眼镜，穿戴防护服和口罩，佩戴手套，避免与皮肤接触。
2.使用9001-64-3实验过程中如遇到有毒或者刺激性物质及有害物质产生，必要时实验操作需要手套箱内完成以免对实验人员造成伤害。
3.取样品9001-64-3的移液枪头需及时更换，必要时为避免交叉污染尽可能选择滤芯吸头。
4.称量药品时选用称量纸，并无风处取药和称量以免扬撒，试剂的容器使用前务必确保干净，并消毒。
5.取药品9001-64-3时尽量采用多个药勺分别使用，使用后清洗干净。
6.实验后产生的废弃物需分类存储，并交于专业生物废气物处理公司处理，以免造成环境污染。
大规格定制：定制产品请将信息发送至sales@bio-fount.com。

Malate dehydrogenase(9001-64-3) Experimental considerations:
1. Wear protective glasses, protective clothing and masks, gloves, and avoid contact with the skin during the experiment.
2. The waste generated after the experiment needs to be stored separately, and handed over to a professional biological waste gas treatment company to avoid environmental pollution.

Tag:苹果酸脱氢酶(9001-64-3,Malate dehydrogenase),苹果酸脱氢酶悬浮液,苹果酸脱氢酶的活性,苹果酸脱氢酶的储存条件,苹果酸脱氢酶的使用注意事项,苹果酸脱氢酶的MSDS,苹果酸脱氢酶的生产厂家,苹果酸脱氢酶的价格,苹果酸脱氢酶的作用

产品说明	苹果酸脱氢酶(9001-64-3,Malate dehydrogenase)仅用于科研实验使用，苹果酸脱氢酶的活性、9001-64-3的其他参数见主页
Introduction	Malate dehydrogenase (9001-64-3,苹果酸脱氢酶) is only used in scientific research experiments. Please refer to the homepage for the activity of malate dehydrogenase and other parameters of 9001-64-3
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警示图
危险性
危险性警示	Not Available
安全声明	H303吞入可能有害+H313皮肤接触可能有害+H333吸入可能对身体有害
安全防护	P264处理后彻底清洗+P280戴防护手套/穿防护服/戴防护眼罩/戴防护面具+P305如果进入眼睛+P351用水小心冲洗几分钟+P338取出隐形眼镜（如果有）并且易于操作,继续冲洗+P337如果眼睛刺激持续+P313获得医疗建议/护理
备注	避免吸入，误食以及与皮肤接触

1.Diglycolic acid, the toxic metabolite of diethylene glycol, chelates calcium and produces renal mitochondrial dysfunction in vitro.

2.The α-Crystallin Domain Containing Genes: Identification, Phylogeny and Expression Profiling in Abiotic Stress, Phytohormone Response and Development in Tomato (Solanum lycopersicum).

3.Research on root responses to Pb and Zn combined stress of Carex putuoshan.

4.Reactive Oxygen Species Production in Cardiac Mitochondria After Complex I Inhibition: Modulation by Substrate-Dependent Regulation of the NADH/NAD+ Ratio.

1.Diglycolic acid, the toxic metabolite of diethylene glycol, chelates calcium and produces renal mitochondrial dysfunction in vitro.
Conrad T1,2, Landry GM2, Aw TY3, Nichols R2, McMartin KE2. Clin Toxicol (Phila). 2016 Mar 22:1-11. [Epub ahead of print]
CONTEXT: Diethylene glycol (DEG) has caused many cases of acute kidney injury and deaths worldwide. Diglycolic acid (DGA) is the metabolite responsible for the renal toxicity, but its toxic mechanism remains unclear.

2.The α-Crystallin Domain Containing Genes: Identification, Phylogeny and Expression Profiling in Abiotic Stress, Phytohormone Response and Development in Tomato (Solanum lycopersicum).
Paul A1, Rao S1, Mathur S1. Front Plant Sci. 2016 Mar 31;7:426. doi: 10.3389/fpls.2016.00426. eCollection 2016.
The α-crystallin domain (ACD) is an ancient domain conserved among all kingdoms. Plant ACD proteins have roles in abiotic stresses, transcriptional regulation, inhibiting virus movement, and DNA demethylation. An exhaustive in-silico analysis using Hidden Markov Model-based conserved motif search of the tomato proteome yielded a total of 50 ACD proteins that belonged to four groups, sub-divided further into 18 classes. One of these groups belongs to the small heat shock protein (sHSP) class of proteins, molecular chaperones implicated in heat tolerance. Both tandem and segmental duplication events appear to have shaped the expansion of this gene family with purifying selection being the primary driving force for evolution. The expression profiling of the Acd genes in two different heat stress regimes suggested that their transcripts are differentially regulated with roles in acclimation and adaptive response during recovery. The co-expression of various genes in response to different abiotic stresses (heat, low temperature, dehydration, salinity, and oxidative stress) and phytohormones (abscisic acid and salicylic acid) suggested possible cross-talk between various members to combat a myriad of stresses.

3.Research on root responses to Pb and Zn combined stress of Carex putuoshan.
Hu YL, Tan JL, Wang CL, Yang ZB, Yang YX, Chen Z, Lin LJ, Wang YJ, Sun G, Zhu XM, Shao JR1, Zhou ML. Protein Pept Lett. 2016 Mar 22. [Epub ahead of print]
Pb hyper-accumulated Carex putuoshan was taken as experimental material and subjected to combined stress of Pb and Zn. The differential expression of proteins in their roots were analyzed by Proteomic Approach. The protein that was directly involved in the cellular defense under the Pb and Zn combined stress was separated, and expression of those genes was analyzed with Carex Evergold as control. The results were obtained by MALDI-TOF/MS analysis. After applying Pb and Zn combined stress, the expression of 9 protein spots (including 7 different proteins, 2 identical proteins, 1 unknown protein) in Carex putuoshan root was found to be significantly up-regulated. Five proteins were obtained from the 9 proteins related to carbohydrate metabolism, including malate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, frutose-1,6-bisphosphate aldolase, enolase, and 6- phosphogluconate dehydrogenase. Two proteins were related to protein biosynthesis, including isoflavone reductase and phytochelatin synthase (PCS).

4.Reactive Oxygen Species Production in Cardiac Mitochondria After Complex I Inhibition: Modulation by Substrate-Dependent Regulation of the NADH/NAD+ Ratio.
Korge P1, Calmettes G1, Weiss JN2. Free Radic Biol Med. 2016 Apr 8. pii: S0891-5849(16)30022-3. doi: 10.1016/j.freeradbiomed.2016.04.002. [Epub ahead of print]
Reactive oxygen species (ROS) production by isolated complex I is steeply dependent on the NADH/NAD+ ratio. We used alamethicin-permeabilized mitochondria to study the substrate-dependence of matrix NADH and ROS production when complex I is inhibited by piericidin or rotenone. When complex I was inhibited in the presence of malate/glutamate, membrane permeabilization accelerated O2 consumption and ROS production due to a rapid increase in NADH generation that was not limited by matrix NAD(H) efflux. In the presence of inhibitor, both malate and glutamate were required to generate a high enough NADH/NAD+ ratio to support ROS production through the coordinated activity of malate dehydrogenase (MDH) and aspartate aminotransferase (AST). With malate and glutamate present, the rate of ROS production was closely related to local NADH generation, whereas in the absence of substrates, ROS production was accelerated by increase in added [NADH]. With malate alone, oxaloacetate accumulation limited NADH production by MDH unless glutamate was also added to promote oxaloacetate removal via AST.

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