Calpain-1 catalytic subunit (CAPN1) Recombinant Protein | CAPN1 recombinant protein

Recombinant Human Calpain-1 catalytic subunit (CAPN1)

Cat. Num. AAA18465

• 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.

SDS-PAGE

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

Cell Biology

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 #: 311893363
• NCBI GeneID: 823
• NCBI Accession #: NP_001185797.1
• NCBI GenBank Nucleotide #: NM_001198868.1
• UniProt Accession #: P07384; Q2TTR0; Q6DHV4
• 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