Calpain-1 catalytic subunit (CAPN1) Recombinant Protein | CAPN1 recombinant protein
Recombinant Human Calpain-1 catalytic subunit (CAPN1)
Gene Names
CAPN1; CANP; muCL; CANP1; CANPL1; muCANP
Purity
Greater or equal to 85% purity as determined by SDS-PAGE.
Synonyms
Calpain-1 catalytic subunit (CAPN1); N/A; Recombinant Human Calpain-1 catalytic subunit (CAPN1); Calcium-activated neutral proteinase 1; CANP 1; Calpain mu-type; Calpain-1 large subunit; Cell proliferation-inducing gene 30 protein; Micromolar-calpain; muCANP; CAPN1 recombinant protein
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Purity/Purification
Greater or equal to 85% purity as determined by SDS-PAGE.
Form/Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Sequence Positions
1-714aa; Full Length Protein
Sequence
MSEEIITPVYCTGVSAQVQKQRARELGLGRHENAIKYLGQDYEQLRVRCLQSGTLFRDEAFPPVPQSLGYKDLGPNSSKTYGIKWKRPTELLSNPQFIVDGATRTDICQGALGDCWLLAAIASLTLNDTLLHRVVPHGQSFQNGYAGIFHFQLWQFGEWVDVVVDDLLPIKDGKLVFVHSAEGNEFWSALLEKAYAKVNGSYEALSGGSTSEGFEDFTGGVTEWYELRKAPSDLYQIILKALERGSLLGCSIDISSVLDMEAITFKKLVKGHAYSVTGAKQVNYRGQVVSLIRMRNPWGEVEWTGAWSDSSSEWNNVDPYERDQLRVKMEDGEFWMSFRDFMREFTRLEICNLTPDALKSRTIRKWNTTLYEGTWRRGSTAGGCRNYPATFWVNPQFKIRLDETDDPDDYGDRESGCSFVLALMQKHRRRERRFGRDMETIGFAVYEVPPELVGQPAVHLKRDFFLANASRARSEQFINLREVSTRFRLPPGEYVVVPSTFEPNKEGDFVLRFFSEKSAGTVELDDQIQANLPDEQVLSEEEIDENFKALFRQLAGEDMEISVKELRTILNRIISKHKDLRTKGFSLESCRSMVNLMDRDGNGKLGLVEFNILWNRIRNYLSIFRKFDLDKSGSMSAYEMRMAIESAGFKLNKKLYELIITRYSEPDLAVDFDNFVCCLVRLETMFRFFKTLDTDLDGVVTFDLFKWLQLTMFA
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
Related Product Information for CAPN1 recombinant protein
Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.
Product Categories/Family for CAPN1 recombinant protein
References
Complete amino acid sequence of the large subunit of the low-Ca2+-requiring form of human Ca2+-activated neutral protease (muCANP)
deduced from its cDNA sequence.Aoki K., Imajoh S., Ohno S., Emori Y., Koike M., Kosaki G., Suzuki K.FEBS Lett. 205:313-317(1986)
A novel member of the calcium-dependent cysteine protease family.Sorimachi H., Ohmi S., Emori Y., Kawasaki H., Saido T.C., Ohno S., Minami Y., Suzuki K.Biol. Chem. Hoppe-Seyler 371:171-176(1990)
Identification of a human cell proliferation inducing gene.Kim J.W.NIEHS SNPs program
Modulation of the calpain autoproteolysis by calpastatin and phospholipids.Melloni E., Michetti M., Salamino F., Minafra R., Pontremoli S.Biochem. Biophys. Res. Commun. 229:193-197(1996)
Autolysis of human erythrocyte calpain produces two active enzyme forms with different cell localization.Michetti M., Salamino F., Tedesco I., Averna M., Minafra R., Melloni E., Pontremoli S.FEBS Lett. 392:11-15(1996)
Calcium-binding properties of human erythrocyte calpain.Michetti M., Salamino F., Minafra R., Melloni E., Pontremoli S.Biochem. J. 325:721-726(1997)
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.Anal. Chem. 81:4493-4501(2009)
Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011)
Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012)
N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012)
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014)
Molecular mode of action of a covalently inhibiting peptidomimetic on the human calpain protease core.Li Q., Hanzlik R.P., Weaver R.F., Schonbrunn E.Biochemistry 45:701-708(2006)
NCBI and Uniprot Product Information
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
Molecular Weight
85.9 kDa
NCBI Official Full Name
calpain-1 catalytic subunit
NCBI Official Synonym Full Names
calpain 1
NCBI Official Symbol
CAPN1
NCBI Official Synonym Symbols
CANP; muCL; CANP1; CANPL1; muCANP
NCBI Protein Information
calpain-1 catalytic subunit
UniProt Protein Name
Calpain-1 catalytic subunit
UniProt Gene Name
CAPN1
UniProt Synonym Gene Names
CANPL1; CANP 1; muCANP
UniProt Entry Name
CAN1_HUMAN