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Official Full Name ClpP caseinolytic peptidase, ATP-dependent, proteolytic subunit homolog
Background The protein encoded by this gene belongs to the peptidase family S14 and hydrolyzes proteins into small peptides in the presence of ATP and magnesium. The protein is transported into mitochondrial matrix and is associated with the inner mitochondrial membrane.
Synonyms CLPP; ClpP caseinolytic peptidase, ATP-dependent, proteolytic subunit homolog (E. coli); ClpP (caseinolytic protease, ATP dependent, proteolytic subunit, E. coli) homolog , ClpP caseinolytic protease, ATP dependent, proteolytic subunit homolog (E. coli)
    • Species :
    • Bacillus subtilis
    • Clostridium Botulinum
    • E.coli
    • Human
    • Mouse
    • Staphylococcus
    • Streptomyces coelicolor A3(2)
    • Zebrafish
    • Source :
    • E. coli or Yeast
    • E.coli
    • HEK293
    • HEK293T
    • Human
    • Mammalian Cell
    • Wheat Germ
    • Tag :
    • GST
    • His
    • His/Myc
    • SUMO
    • Myc/DDK
    • N/A
    Species Cat.# Product name Source (Host) Tag Protein Length Price
    Human CLPP-11343H Recombinant Human CLPP, GST-tagged E.coli GST
    Human CLPP-1512H Recombinant Human CLPP Protein, GST-tagged Wheat Germ GST
    Human CLPP-1679H Recombinant Human Clpp Caseinolytic Peptidase, ATP-Dependent, Proteolytic Subunit Homolog (E.coli) Human N/A
    Human CLPP-3538H Recombinant Human CLPP, His-tagged Human His
    Human CLPP-694H Recombinant Human caseinolytic mitochondrial matrix peptidase proteolytic subunit, His-tagged E.coli His
    Human CLPP-7434HCL Recombinant Human CLPP 293 Cell Lysate HEK293 N/A
    Mouse Clpp-2197M Recombinant Mouse Clpp Protein, Myc/DDK-tagged HEK293T Myc/DDK
    Mouse CLPP-3599M Recombinant Mouse CLPP Protein Mammalian Cell His
    Zebrafish CLPP-2847Z Recombinant Zebrafish CLPP Mammalian Cell His
    E.coli CLPP-1032E Recombinant Escherichia coli (strain UTI89/UPEC) clpP protein (ATP-dependent Clp protease proteolytic subunit), His/Myc-tagged E.coli His/Myc
    Staphylococcus CLPP-0016S Recombinant Staphylococcus aureus subsp. aureus NCTC 8325 CLPP protein, His-tagged E. coli or Yeast His
    Bacillus subtilis CLPP-0097B Recombinant Bacillus subtilis CLPP protein, His-tagged E. coli or Yeast His
    Clostridium Botulinum CLPP-1971C Recombinant Clostridium Botulinum CLPP Protein (1-194 aa), His-SUMO-tagged E.coli His/SUMO
    Staphylococcus CLPP-3272S Recombinant Staphylococcus epidermidis ATCC 12228 CLPP protein, His-tagged E. coli or Yeast His
    Streptomyces coelicolor A3(2) CLPP-937S Recombinant Streptomyces coelicolor A3(2) CLPP protein, His-tagged E. coli or Yeast His

    clpp involved in several pathways and played different roles in them. We selected most pathways clpp participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with clpp were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein

    clpp has several biochemical functions, for example, identical protein binding, peptidase activity, protein binding. Some of the functions are cooperated with other proteins, some of the functions could acted by clpp itself. We selected most functions clpp had, and list some proteins which have the same functions with clpp. You can find most of the proteins on our site.

    Function Related Protein
    identical protein binding Serpina1c; GYPA; NDE1; SETX; LCK; SOD2; SERPINA1; IAPP; GLUL; ETNPPL
    peptidase activity ELA2L; KLK1B8; KLK1B1; CAPN2B; APH1C; PRSS59.2; PAPPAB; Casp3; MCPT1; Gzmg
    protein binding LANCL2; ATP6V1D; MDFIC; ERGIC1; AHR; MIPOL1; MYH10; ASPH; CASP9; FAM72A
    serine-type endopeptidase activity PRSS48; CTRL; KLK6; GZMK; TMPRSS4; KLK2; LPA; F12; HGF; ST14A

    clpp has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with clpp here. Most of them are supplied by our site. Hope this information will be useful for your research of clpp.


    Zhou, MX; Zhu, F; et al. Gap1 functions as a molecular chaperone to stabilize its interactive partner Gap3 during biogenesis of serine-rich repeat bacterial adhesin. MOLECULAR MICROBIOLOGY 83:866-878(2012).
    Ito, J; Nagayasu, Y; et al. ApoA-I enhances generation of HDL-like lipoproteins through interaction between ABCA1 and phospholipase C gamma in rat astrocytes. BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS 1811:1062-1069(2011).

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