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安全信息

HPA021241

Sigma-Aldrich

抗 PHGDH 兔抗

enhanced validation

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution, Ab1

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别名:
抗 3-PGDH, 抗 D-3-磷酸甘油酸脱氢酶
UNSPSC代码:
12352203
人类蛋白质图谱编号:
NACRES:
NA.43

生物来源

rabbit

质量水平

偶联物

unconjugated

抗体形式

affinity isolated antibody

抗体产品类型

primary antibodies

克隆

polyclonal

产品线

Prestige Antibodies® Powered by Atlas Antibodies

形式

buffered aqueous glycerol solution

种属反应性

mouse, rat, human

增强验证

orthogonal RNAseq
independent
Learn more about Antibody Enhanced Validation

技术

immunoblotting: 0.04-0.4 μg/mL
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:500-1:1000

免疫原序列

LEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGALLRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDM

UniProt登记号

应用

research pathology

运输

wet ice

储存温度

−20°C

靶向翻译后修饰

unmodified

基因信息

human ... PHGDH(26227)

一般描述

基因 PHGDH(D-3-磷酸甘油酸脱氢酶)定位于人类染色体 1p。

免疫原

D-3-磷酸甘油酸脱氢酶重组蛋白表位标签 (PrEST)

应用

兔抗PHGDH抗体属Prestige抗体,经人类蛋白质图谱(HPA)计划开发和验证。每种抗体都通过针对数百种正常和疾病组织的免疫组织化学进行测试。通过单击图像库链接,可以在人类蛋白质图谱(HPA)站点上查看这些图像。还采用免疫荧光和蛋白质印迹法对抗体进行检测。想要查看有关Prestige 抗体和HPA的方案和其他实用信息,请访问 sigma.com/prestige

生化/生理作用

PHGDH(D-3-磷酸甘油醛脱氢酶)主要可以催化丝氨酸合成途径的初始步骤,将3-磷酸甘油酸转化为3-磷酸羟基丙酮酸。它在雌激素受体阴性乳腺癌、黑素瘤和宫颈癌中上调。PHGDH突变与Neu-Laxova 综合征有关。PHGDH水平下调导致先天性小头畸形、精神运动迟缓和癫痫发作。

特点和优势

Prestige抗体®是经过高度表征和广泛验证的抗体,同时还有一个优点是其每个靶标的所有可用表征数据都可以通过位于此页面顶部产品名称下方的人类蛋白质图谱门户进行访问。Prestige抗体对其他蛋白质的独特性和低交叉反应性®是通过严密的抗原区域选择、亲和纯化和严格的选择来实现的。针对每一个Prestige Antibody都存在有对应的Prestige抗原对照,并可在链接区域内找到。

每个Prestige Antibody都是按照以下方法进行测试的:
  • 44例正常人类组织以及20例最常见癌症类型组织的IHC组织阵列。
  • 364个人类重组蛋白片段的蛋白阵列。

联系

Corresponding Antigen APREST73826

外形

磷酸盐缓冲盐溶液,pH 7.2,含 40% 甘油和 0.02% 叠氮化钠

法律信息

Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany

免责声明

除非我们的产品目录或产品附带的其他公司文档另有说明,否则我们的产品仅供研究使用,不得用于任何其他目的,包括但不限于未经授权的商业用途、体外诊断用途、离体或体内治疗用途或任何类型的消费或应用于人类或动物。

WGK

WGK 1

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

常规特殊物品

分析证书(COA)

输入产品批号来搜索 分析证书(COA) 。批号可以在产品标签上"批“ (Lot或Batch)字后找到。

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Quentin Spillier et al.
Pharmaceuticals (Basel, Switzerland), 13(2) (2020-01-26)
For many years now, targeting deregulation within cancer cells' metabolism has appeared as a promising strategy for the development of more specific and efficient cancer treatments. Recently, numerous reports highlighted the crucial role of the serine synthetic pathway, and particularly
D M Brown et al.
Scientific reports, 6, 28693-28693 (2016-06-29)
We aimed to identify novel molecular mechanisms for muscle growth during administration of anabolic agents. Growing pigs (Duroc/(Landrace/Large-White)) were administered Ractopamine (a beta-adrenergic agonist; BA; 20 ppm in feed) or Reporcin (recombinant growth hormone; GH; 10 mg/48 hours injected) and compared to a
Katherine R Mattaini et al.
Cancer & metabolism, 3, 5-5 (2015-05-01)
The gene encoding the serine biosynthesis pathway enzyme PHGDH is located in a region of focal genomic copy number gain in human cancers. Cells with PHGDH amplification are dependent on enzyme expression for proliferation. However, dependence on increased PHGDH expression
Yang Ou et al.
The Journal of biological chemistry, 290(1), 457-466 (2014-11-19)
Although p53 is frequently mutated in human cancers, about 80% of human melanomas retain wild-type p53. Here we report that PHGDH, the key metabolic enzyme that catalyzes the rate-limiting step of the serine biosynthesis pathway, is a target of p53
Katherine R Mattaini et al.
BMC cancer, 19(1), 723-723 (2019-07-25)
Copy number gain of the D-3-phosphoglycerate dehydrogenase (PHGDH) gene, which encodes the first enzyme in serine biosynthesis, is found in some human cancers including a subset of melanomas. In order to study the effect of increased PHGDH expression in tissues

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