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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Overview

Catalog No.	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.
Expression system	E. coli
Accession	O76031
Protein length	Ser287-Ala605
Applications	ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
Species	Homo sapiens (Human)
Nature	Recombinant
Endotoxin level	Please contact with the lab for this information.
Purity	>90% as determined by SDS-PAGE.
Predicted molecular weight	37.19 kDa
Form	Lyophilized
Storage buffer	Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.
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.
Shipping	In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
Stability and Storage	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.
Alternate Names	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
Background	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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Datasheet

Human CLPX Recombinant Protein (N-His).pdf

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

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