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Key Documents

HPA020342

Sigma-Aldrich

Anti-CPA2 antibody produced in rabbit

enhanced validation

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

同義詞:

Anti-Carboxypeptidase A2

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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

品質等級

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
independent
Learn more about Antibody Enhanced Validation

技術

immunohistochemistry: 1:500- 1:1000

免疫原序列

MIEDVQVLLDKENEEMLFNRRRERSGNFNFGAYHTLEEISQEMDNLVAEHPGLVSKVNIGSSFENRPMNV

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 ... CPA2(1358)

相關類別

一般說明

Carboxypeptidase A2 (CPA2) is formed by the release of the 81-residue activation domain of its proenzyme-procarboxypeptidase A2.

免疫原

Carboxypeptidase A2 Precursor recombinant protein epitope signature tag (PrEST)

應用

All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project and as a result, are supported by the most extensive characterization in the industry.

The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. We also provide Prestige Antibodies® protocols and other useful information.

生化/生理作用

Carboxypeptidase A2 (CPA2) cleaves aromatic C-terminal residues in proteins. Its proenzyme form has been used in different methods to enhance the stability of proteins. Studies have indicated that in some conditions CPA2 forms amyloid fibrils in vitro.

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 APREST75040

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


分析證明 (COA)

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M Angeles Jiménez et al.
Protein science : a publication of the Protein Society, 12(2), 296-305 (2003-01-23)
The activation domain of human procarboxypeptidase A2, ADA2h, is an 81-residue globular domain released during the proteolytic activation of the proenzyme. The role of this and other similar domains as assistants of the correct folding of the enzyme is not
I García-Sáez et al.
The EMBO journal, 16(23), 6906-6913 (1998-01-31)
The three-dimensional structure of human procarboxypeptidase A2 has been determined using X-ray crystallography at 1.8 A resolution. This is the first detailed structural report of a human pancreatic carboxypeptidase and of its zymogen. Human procarboxypeptidase A2 is formed by a

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