product summary
Loading...
company name :
MyBioSource
product type :
protein
product name :
Recombinant Human Calpain-1 catalytic subunit
catalog :
MBS957983
quantity :
0.05 mg (E-Coli)
price :
190 USD
more info or order :
product information
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 length :
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 gi num :
311893363
ncbi acc num :
NP_001185797.1
ncbi gb acc num :
NM_001198868.1
uniprot acc num :
P07384
ncbi mol weight :
85.9kD
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
size1 :
0.05 mg (E-Coli)
price1 :
190 USD
size2 :
0.2 mg (E-Coli)
price2 :
460
size3 :
0.5 mg (E-Coli)
price3 :
750
size4 :
1 mg (E-Coli)
price4 :
1180
size5 :
0.05 mg (Baculovirus)
price5 :
1520
more info or order :
company information
MyBioSource
P.O. Box 153308
San Diego, CA 92195-3308
sales@mybiosource.com
https://www.mybiosource.com
1-888-627-0165
headquarters: USA
MyBioSource, LLC was orginally founded in Vancouver by three enthusiastic scientists who are passionate about providing the world with the best reagents available. Together, they form a company with a big vision known as MyBioSource. MyBioSource is now located in San Diego, California, USA.

"MyBioSource's number 1 vision is to be the world's number 1 quality reagents provider."

Our goal is to provide researchers, scientists and customers alike with a one-stop-shop for all of their reagents needs, whether it is monoclonal antibody, polyclonal antibody, recombinant protein, peptide, etc...

"MyBioSource offers the best products at unbeatable prices."

Please spend a few minutes to browse our online catalogs and see the wide range of products available. We ship our products through our shipping/distribution facility in San Diego, California, USA.

Would you like to receive email and e-newsletter from MyBioSource about new products, special offers and events? Please click here to join our Mailing List!