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Recombinant Human Clpp Caseinolytic Peptidase, ATP-Dependent, Proteolytic Subunit Homolog (E.coli)

Cat.No. : CLPP-1679H
Product Overview : Recombinant human CLPP protein was expressed in E.coli and purified by using conventional chromatography techniques.
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  • Gene Information
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Cat. No. : CLPP-1679H
Description : CLPP (ATP-dependent Clp protease proteolytic subunit) belongs to the peptidase family S14. CLPP cleaves peptides in various proteins in a process that requires ATP hydrolysis. CLPP, the catalytic core of the Clp proteolytic complex, is widely involved in many cellular processes via the regulation of intracellular protein quality. CLPP may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates.
Concentration : 0.5 mg/ml
Source : Human
Host : E.coli
Form : Supplied as a liquid in 20mM Tris-HCl buffer, pH 7.5, containing 2mM DTT, 20% glycerol and 100mM NaCl.
Purity : > 90% by SDS - PAGE
Sequence : 57-277 amino acids: MPLIPIVVEQ TGRGERAYDI YSRLLRERIV CVMGPIDDSV ASLVIAQLLF LQSESNKKPI HMYINSPGGV VTAGLAIYDT MQYILNPICT WCVGQAASMG SLLLAAGTPG MRHSLPNSRI MIHQPSGGAR GQATDIAIQA EEIMKLKKQL YNIYAKHTKQ SLQVIESAME RDRYMSPMEA QEFGILDKVL VHPPQDGEDE PTLVQKEPVE AA
Molecular Mass : 24.2 kDa
Applications : SDS-PAGE
Storage : Store at 4 deg C for short term storage (1/2 weeks). Aliquot and store at -20 deg C or - 70 deg C for long term storage. Avoid repeated freeze/thaw cycles.
Gene Name : CLPP ClpP caseinolytic peptidase, ATP-dependent, proteolytic subunit homolog (E. coli) [ Homo sapiens ]
Official Symbol : CLPP
Synonyms : CLPP; putative ATP-dependent Clp protease proteolytic; subunit, mitochondrial; endopeptidase Clp; ATP-dependent protease ClpAP, proteolytic subunit, human; ClpP caseinolytic peptidase ATP-dependent, proteolytic subunit; ClpP caseinolytic protease, ATP-dependent, proteolytic subunit homolog
Gene ID : 8192
mRNA Refseq : NM_006012
Protein Refseq : NP_006003
MIM : 601119
UniProt ID : Q16740
Chromosome Location : 19p13.3
Function : ATP binding; nucleotide binding; peptidase activity; protein binding; serine-type endopeptidase activity

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