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

Name: Human CLPX Recombinant Protein (N-His)
Brand: abinScience
SKU: HC966012
Price: 211 USD
Availability: InStock

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Numéro de catalogue	HC966012
Description	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.
Système d'expression	E. coli
Numéro d'accès	O76031
Longueur de protéine	Ser287-Ala605
Applications	ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
Espèces	Homo sapiens (Human)
Nature	Recombinant
Niveau d'endotoxines	Please contact with the lab for this information.
Pureté	>90% as determined by SDS-PAGE.
Masse moléculaire prédite	37.19 kDa
Forme	Lyophilized
Tampon de stockage	Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Reférez-vous aux informations spécifiques sur le tampon dans la copie papier du datasheet ou dans le COA spécifique au lot.
Reconstitution	Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
Expédition	In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
Stabilité et stockage	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.
Noms alternatifs	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
Contexte	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
Note	For research use only

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Human CLPX Recombinant Protein (N-His).pdf

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