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Merck

HPA008862

Sigma-Aldrich

Anti-LONP2 antibody produced in rabbit

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

别名:

Anti-peroxisomal LON protease-like antibody produced in rabbit

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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

技術

immunoblotting: 0.04-0.4 μg/mL
immunohistochemistry: 1:50-1:200

免疫原序列

TILGVIPNTPDPASDAQDLPPLHRIGTAALAVQVVGSNWPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVEQLDRLEEFPNTCKMREELGELSEQFYKYAVQLVEMLDMSVPAVAKLRR

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 ... LONP2(83752)

一般說明

LONP2 (lon peptidase 2) is a peroxisomal matrix protein, which contains a serine protease-like domain and a peroxisome-targeting signal 1 (PTS1) region. It belongs to the ATP-dependent Lon protease family. This protein is composed of 852 amino acids and has a molecular weight of 90kDa.

免疫原

peroxisomal LON protease-like 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

LONP2 (lon peptidase 2) controls the β-oxidation of fatty acids in peroxisomes, in coordination with trypsin domain-containing 1 (Tysnd1). It degrades the self-cleaved C- and N-terminal products of Tysnd1 protein. Thus, it controls the turnover and activity of Tysnd1 enzyme, thereby indirectly controlling peroxisomal fatty acid β-oxidation. In mitochondria, this enzyme is responsible for the degradation of folded protein and promotes non-processive substrate cleavage. This enzyme is thought to play a key role in the synthesis of peroxisomes.

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 APREST70788

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

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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

個人防護裝備

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


分析证书(COA)

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Miki Kikuchi et al.
The Journal of biological chemistry, 279(1), 421-428 (2003-10-17)
Subcellular proteomics, which includes isolation of subcellular components prior to a proteomic analysis, is advantageous not only in characterizing large macro-molecular complexes such as organelles but also in elucidating mechanisms of protein transport and organelle biosynthesis. Because of the high
Kanji Okumoto et al.
The Journal of biological chemistry, 286(52), 44367-44379 (2011-10-18)
The molecular mechanisms underlying protein turnover and enzyme regulation in the peroxisomal matrix remain largely unknown. Trypsin domain-containing 1 (Tysnd1) and peroxisomal Lon protease (PsLon) are newly identified peroxisomal matrix proteins that harbor both a serine protease-like domain and a
Gabriela Ondrovicová et al.
The Journal of biological chemistry, 280(26), 25103-25110 (2005-05-05)
Mechanistic studies of ATP-dependent proteolysis demonstrate that substrate unfolding is a prerequisite for processive peptide bond hydrolysis. We show that mitochondrial Lon also degrades folded proteins and initiates substrate cleavage non-processively. Two mitochondrial substrates with known or homology-derived three-dimensional structures

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