catalog number :
MBS957983
products type :
Recombinant Protein
products full name :
Recombinant Human Calpain-1 catalytic subunit
products short name :
Calpain-1 catalytic subunit
products name syn :
Calcium-activated neutral proteinase 1; CANP 1; Calpain mu-type; Calpain-1 large subunit; Cell proliferation-inducing gene 30 protein; Micromolar-calpain; muCANP
other names :
calpain-1 catalytic subunit; Calpain-1 catalytic subunit; calpain-1 catalytic subunit; calpain 1; Calcium-activated neutral proteinase 1; CANP 1; Calpain mu-type; Calpain-1 large subunit; Cell proliferation-inducing gene 30 protein; Micromolar-calpain; muCANP
products gene name :
CAPN1
other gene names :
CAPN1; CAPN1; CANP; muCL; CANP1; CANPL1; muCANP; CANPL1; CANP 1; muCANP
uniprot entry name :
CAN1_HUMAN
host :
E Coli or Yeast or Baculovirus or Mammalian Cell
sequence positions :
1-714
sequence :
MSEEIITPVYCTGVSAQVQKQRARELGLGRHENAIKYLG
QDYEQLRVRCLQSGTLFRDEAFPPVPQSLGYKDLGPNSS
KTYGIKWKRPTELLSNPQFIVDGATRTDICQGALGDCWL
LAAIASLTLNDTLLHRVVPHGQSFQNGYAGIFHFQLWQF
GEWVDVVVDDLLPIKDGKLVFVHSAEGNEFWSALLEKAY
AKVNGSYEALSGGSTSEGFEDFTGGVTEWYELRKAPSDL
YQIILKALERGSLLGCSIDIS
purity :
Greater than 90% as determined by SDS-PAGE.
form :
Liquid containing glycerol; lyophilization may be available upon request.
storage stability :
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
products categories :
Cell Biology
products description :
Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.
products 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 acc num :
NP_001185797.1
ncbi gb acc num :
NM_001198868.1
ncbi pathways :
Alzheimer's Disease Pathway (83097); Alzheimer's Disease Pathway (509); Alzheimers Disease Pathway (672448); Apoptosis Pathway (83060); Apoptosis Pathway (470); Degradation Of The Extracellular Matrix Pathway (1270257); Extracellular Matrix Organization Pathway (1270244); Focal Adhesion Pathway (198795); Integrated Pancreatic Cancer Pathway (711360); Integrin-mediated Cell Adhesion Pathway (198816)
ncbi summary :
The calpains, calcium-activated neutral proteases, are nonlysosomal, intracellular cysteine proteases. The mammalian calpains include ubiquitous, stomach-specific, and muscle-specific proteins. The ubiquitous enzymes consist of heterodimers with distinct large, catalytic subunits associated with a common small, regulatory subunit. This gene encodes the large subunit of the ubiquitous enzyme, calpain 1. Several transcript variants encoding two different isoforms have been found for this gene. [provided by RefSeq, Nov 2010]
uniprot summary :
CAPN1: Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Forms a heterodimer with a small (regulatory) subunit (CAPNS1). Ubiquitous. Activated by micromolar concentrations of calcium and inhibited by calpastatin. Belongs to the peptidase C2 family. Protein type: Motility/polarity/chemotaxis; EC 3.4.22.52; Protease. Chromosomal Location of Human Ortholog: 11q13. Cellular Component: cytoplasm; cytosol; focal adhesion; lysosome; membrane; mitochondrion; plasma membrane. Molecular Function: calcium ion binding; calcium-dependent cysteine-type endopeptidase activity; cytoskeletal protein binding; protein binding. Biological Process: extracellular matrix disassembly; extracellular matrix organization and biogenesis; mammary gland involution; positive regulation of cell proliferation; proteolysis; receptor catabolic process
size5 :
0.05 mg (Baculovirus)