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Human CLPX Recombinant Protein (N-His) (HC966012)

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概要
カタログ番号HC966012
説明
Recombinant Human CLPX Protein, N-His (HC966012) expressed in E. coli, spanning Ser287-Ala605. Purity: >90% by SDS-PAGE.
Highlights
  • ●His-Tagged — N-terminal 6×His tag for IMAC purification.
  • ●E. coli Expression — High-yield, cost-effective production.
  • ●High Purity — >90% purity verified by SDS-PAGE.
発現システムE. coli
アクセッション番号O76031
タンパク質長Ser287-Ala605
アプリケーションELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
種Homo sapiens (Human)
性質 Recombinant
エンドトキシンレベル Please contact with the lab for this information.
純度 >90% as determined by SDS-PAGE.
予測分子量 37.19 kDa
形態 Lyophilized
保存バッファー Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.

データシートのハードコピーまたはロット固有のCOAに記載された具体的なバッファー情報を参照してください。

再構成 Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
発送 In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
安定性と保存 Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
別名ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial, ATP-dependent clpX-like chaperone, mitochondrial, CLPX, Caseinolytic mitochondrial matrix peptidase chaperone subunit X, EC:3.6.4.10
背景

ATP-dependent clpX-like chaperone, mitochondrial is a ~69 kDa protein. ATP-dependent chaperone that functions as an unfoldase. As part of the ClpXP protease complex, it recognizes specific protein substrates, unfolds them using energy derived from ATP hydrolysis, and then translocates them to the proteolytic subunit (CLPP) of the ClpXP complex for degradation. Thanks to its chaperone activity, it also functions in the incorporation of the pyridoxal phosphate cofactor into 5-aminolevulinate synthase, thereby activating 5-aminolevulinate (ALA) synthesis, the first step in heme biosynthesis. This chaperone is also involved in the control of mtDNA nucleoid distribution, by regulating mitochondrial transcription factor A (TFAM) activity.

1. Kang, SG. et al. (2002) The Journal of biological chemistry 277, 21095-102. PMID: 11923310
2. Lowth, BR. et al. (2012) Journal of structural biology 179, 193-201. PMID: 22710082
3. Yien, YY. et al. (2017) Proceedings of the National Academy of Sciences of the United States of America 114, E8045-E8052. PMID: 28874591
4. Kasashima, K. et al. (2012) Experimental cell research 318, 2335-43. PMID: 22841477
注意事項 For research use only
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参考文献
Formula
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