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Merck
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Key Documents

HPA020376

Sigma-Aldrich

Anti-PSPH antibody produced in rabbit

enhanced validation

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

别名:

Anti-L-3-phosphoserine phosphatase, Anti-O-phosphoserine phosphohydrolase, Anti-PSP, Anti-PSPase, Anti-Phosphoserine phosphatase

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About This Item

分類程式碼代碼:
12352203
人類蛋白質圖譜編號:
NACRES:
NA.41

生物源

rabbit

共軛

unconjugated

抗體表格

affinity isolated antibody

抗體產品種類

primary antibodies

無性繁殖

polyclonal

產品線

Prestige Antibodies® Powered by Atlas Antibodies

形狀

buffered aqueous glycerol solution

物種活性

human

加強驗證

orthogonal RNAseq
Learn more about Antibody Enhanced Validation

技術

immunoblotting: 0.04-0.4 μg/mL
immunohistochemistry: 1:200-1:500

免疫原序列

AVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVPFKAALTERLALIQPSREQVQRLIAEQPPHLTPGIRELVSRLQERNVQVFLISG

UniProt登錄號

運輸包裝

wet ice

儲存溫度

−20°C

目標翻譯後修改

unmodified

基因資訊

human ... PSPH(5723)

一般說明

Phosphoserine phosphatase (PSPH) is an Mg2+-dependent enzyme having a molecular mass of 25kDa. It belongs to the haloacid dehalogenase (HAD) superfamily and possesses 225 amino acids. PSPH is present in endosomes and has an amino terminal motif required for its activity. The gene encoding the enzyme is localized on human chromosome 7.

免疫原

Phosphoserine phosphatase recombinant protein epitope signature tag (PrEST)

應用

Anti-PSPH antibody produced in rabbit, a Prestige Antibody, is developed and validated by the Human Protein Atlas (HPA) project . Each antibody is tested by immunohistochemistry against hundreds of normal and disease tissues. These images can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. The antibodies are also tested using immunofluorescence and western blotting. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)

生化/生理作用

Phosphoserine phosphatase (PSPH) takes part in the hydrolysis of L-phosphoserine and the formation of L-serine. Deficiency of the enzyme has been associated with Williams syndrome.

特點和優勢

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.

聯結

Corresponding Antigen APREST75004

外觀

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

法律資訊

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

免責聲明

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.

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儲存類別代碼

10 - Combustible liquids

水污染物質分類(WGK)

WGK 1

閃點(°F)

Not applicable

閃點(°C)

Not applicable


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Kuniaki Sato et al.
Anticancer research, 37(5), 2365-2371 (2017-05-10)
Amplification of chromosome 7p (Ch.7p) is common in colorectal cancer (CRC). The aim of this study was to identify potential driver genes on Ch.7p that are overexpressed due to DNA copy number amplification and determine their clinical significance in CRC.
Satoshi Kitazawa et al.
Oncotarget, 8(17), 28922-28938 (2017-04-21)
Mutations in succinate dehydrogenase B (SDHB) gene are frequently observed in several tumors and associated with poor prognosis in these tumors. Therefore, drugs effective for SDHB-deficient tumors could fulfill an unmet medical need. In addition, such drugs would have an
Yves Peeraer et al.
European journal of biochemistry, 271(16), 3421-3427 (2004-08-05)
The structure of the Mg(2+)-dependent enzyme human phosphoserine phosphatase (HPSP) was exploited to examine the structural and functional role of the divalent cation in the active site of phosphatases. Most interesting is the biochemical observation that a Ca(2+) ion inhibits
Maria Veiga-da-Cunha et al.
European journal of human genetics : EJHG, 12(2), 163-166 (2003-12-16)
We report the identification of the mutations in the only known case of L-3-phosphoserine phosphatase deficiency, a recessively inherited condition. The two mutations correspond to the replacement of the semiconserved Asp32 residue by an asparagine and of the extremely conserved
Yves Peeraer et al.
Acta crystallographica. Section D, Biological crystallography, 59(Pt 6), 971-977 (2003-06-05)
The crystal structure of human phosphoserine phosphatase (HPSP) in the open conformation has been determined at a resolution of 1.53 A. The crystals are orthorhombic, belonging to space group C222(1), with unit-cell parameters a = 49.03, b = 130.25, c

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