跳转至内容
Merck
CN

MABS528

Anti-HGPRT Antibody, clone 13H11.1

clone 13H11.1, from mouse

别名:

Hypoxanthine-guanine phosphoribosyltransferase, HGPRT, HGPRTase

登录 查看组织和合同定价。

选择尺寸


关于此项目

UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Conjugate:
unconjugated
Clone:
13H11.1, monoclonal
Application:
WB
Citations:
-
技术服务
需要帮助?我们经验丰富的科学家团队随时乐意为您服务。
让我们为您提供帮助
技术服务
需要帮助?我们经验丰富的科学家团队随时乐意为您服务。
让我们为您提供帮助

biological source

mouse

conjugate

unconjugated

antibody form

purified antibody

antibody product type

primary antibodies

clone

13H11.1, monoclonal

species reactivity

human

technique(s)

western blot: suitable

isotype

IgG2bκ

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Quality Level

Gene Information

human ... HPRT1(3251)

General description

Hypoxanthine-guanine phosphoribosyltransferase (EC:2.4.2.8; UniProt P00492; also known as HGPRT, HGPRTase) is encoded by the HPRT1 (also known as HGPRT, HPRT) gene (Gene ID 3251) in human. HPRT is a purine salvage enzyme that catalyzes the condensation of 5-phosphoribosyl 1-pyrophosphate (PRPP) and hypoxanthine or guanine to form inosine 5-monophosphate (IMP) and guanosine 5-monophosphate (GMP), respectively. PRPP is an essential compound for the de novo pathway of purine synthesis as well as the synthesis of pyrimidine compounds. PRPP concentrations in erythrocyte are markedly increased in individuals with HPRT deficiency. Complete HPRT deficiency leads to Lesch–Nyhan disease (LND) characterized by uric acid overproduction, motor dysfunction, cognitive disability, and self-injurious behavior. Partial deficiency of HPRT activity causes Lesch–Nyhan variant (LNV) characterized by hyperuricemia and variable degree of neurological manifestations, depending on the residual enzyme activity.
~25 kDa observed

Immunogen

Epitope: Internal
GST-tagged human HGPRT recombinant fragment lacking N- and C-terminal regions.

Application

Research Category
Signaling
Research Sub Category
Signaling Neuroscience
This Anti-HGPRT, clone 13H11.1 is validated for use in Western Blotting for the detection of HGPRT.

Physical form

Format: Purified
Protein G Purified
Purified mouse monoclonal IgG2bκ antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Preparation Note

Stable for 1 year at 2-8°C from date of receipt.

Analysis Note

Evaluated by Western Blotting in HeLa cell lysate.

Western Blotting Analysis: 0.5 µg/mL of this antibody detected HGPRT in 10 µg of HeLa cell lysate.

Other Notes

Concentration: Please refer to lot specific datasheet.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

未找到合适的产品?  

试试我们的产品选型工具.

存储类别

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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。

已有该产品?

在文件库中查找您最近购买产品的文档。

访问文档库

相关内容

"Mods – modifications – small alterations can have a big impact on form and function. In the motorsports world, stock vehicles are modified to enhance their performance. Modifications, or mods, to the engine, drive train, intake and exhaust components add up to provide phenomenal performance gains that can be measured as horsepower and torque increases, which yield a competitive advantage, and result in reduced run times. In biology, proteins undergo modifications that alter their function. Some proteins require the modifications in order to perform their function effectively, whether it’s a pro-protein that is cleaved to produce an active enzyme, or a protein that is phosphorylated to facilitate a signaling process. Other proteins, such as histones, undergo modifications that regulate gene expression and alter cellular function. There are several post translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination that impact protein function and activity. As a result, the analysis of proteins and their post-translational modifications are particularly important for the study of normal and disease-associated processes. New antibodies to detect phospho Histidines are now available from EMD Millipore."

A major focus of breast cancer research is to understand the mechanisms responsible for disease progression and drug resistance. Toward that end, it has been found that approximately two thirds of all human breast carcinomas overexpress the Estrogen Receptor α (ERα) protein and it remains the primary pharmacological target for endocrine therapy1,2. The normal cellular function of ERα is as a transcription factor that mediates a wide variety of physiological processes, many of which are dependent upon phosphorylation of the receptor at specific amino acid residues3,4. Indeed, ERα is known to be phosphorylated at a multitude of different sites, yet how these all correlate to disease remains unclear5. Here, we interrogated multiple sites of ERα for phosphorylation status by screening an extensive panel of different breast cancer patient samples and other non-breast cancer tissue microarray (TMA) slide samples to determine their relevance to disease.

我们的科学家团队拥有各种研究领域经验,包括生命科学、材料科学、化学合成、色谱、分析及许多其他领域.

联系客户支持