Anti-Human CLPX DyLight® 488 conjugated Antibody, Carrier-free

Boster Bio Anti-Human CLPX DyLight® 488 conjugated Antibody catalog # A00978-Dyl488. Tested in Flow Cytometry applications. This antibody reacts with Human.

Product Specifications

Background

ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial is an enzyme that in humans is encoded by the CLPX gene. This protein is a member of the family of AAA Proteins (AAA+ ATPase) and is to form the protein complex of Clp protease. The protein encoded by this gene is part of a protease found in mitochondria. This protease is ATP-dependent and targets specific proteins for degradation. The protease consists of two heptameric rings of the CLPP catalytic subunit sandwiched between two hexameric rings of the chaperone subunit encoded by this gene. Targeted proteins are unwound by this protein and then passed on to the CLPP subunit for degradation. Two transcript variants, one protein-coding and the other non-protein coding, have been found for this gene.

Synonyms

ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial; CLPX

Gene Name

caseinolytic mitochondrial matrix peptidase chaperone subunit

Gene ID

10845

UniProt

O76031

Host

Rabbit

Reactivity

Human

Cross Reactivity

No cross-reactivity with other proteins.

Immunogen

E. coli-derived human CLPX recombinant protein (Position: A337-E574).

Clonality

Polyclonal

Label

DyLight®488

Tissue Specificity

Higher expression in skeletal muscle and heart and to a lesser extent in liver, brain, placenta, lung, kidney and pancreas.

Applications

Flow Cytometry

Concentration

0.5-1mg/ml, actual concentration vary by lot. Use suggested dilution ratio to decide dilution procedure.

Form

Liquid

Function

ATP-dependent specificity component of the Clp protease complex. Hydrolyzes ATP. Targets specific substrates for degradation by the Clp complex (PubMed:11923310, PubMed:22710082). Can perform chaperone functions in the absence of CLPP. Enhances the DNA-binding activity of TFAM and is required for maintaining a normal mitochondrial nucleoid structure (PubMed:22841477). ATP- dependent unfoldase that stimulates the incorporation of the pyridoxal phosphate cofactor into 5-aminolevulinate synthase, thereby activating 5-aminolevulinate (ALA) synthesis, the first step in heme biosynthesis. Important for efficient erythropoiesis through upregulation of heme biosynthesis (PubMed:25957689).

Components

Each vial contains 50% glycerol, 0.9% NaCl, 0.2% Na2HPO4, 0.02% NaN3.

References & Citations

1. Corydon, T. J., Wilsbech, M., Jespersgaard, C., Andresen, B. S., Borglum, A. D., Pedersen, S., Bolund, L., Gregersen, N., Bross, P. Human and mouse mitochondrial orthologs of bacterialClpX. Mammalian Genome 11: 899-905, 2000. 2. Kang, S. G., Dimitrova, M. N., Ortega, J., Ginsburg, A., Maurizi, M. R. Human mitochondrial ClpP is a stable heptamer that assembles into a tetradecamer in the presence of ClpX. J. Biol. Chem. 280: 35424-35432, 2005.