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CAPN1 recombinant protein :: Calpain-1 catalytic subunit Recombinant Protein

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Catalog # MBS957983
Unit / Price
  0.01 mg (E-Coli)  /  $160 +1 FREE 8GB USB
  0.05 mg (E-Coli)  /  $200 +1 FREE 8GB USB
  0.1 mg (E-Coli)  /  $295 +1 FREE 8GB USB
  0.2 mg (E-Coli)  /  $480 +1 FREE 8GB USB
  0.5 mg (E-Coli)  /  $790 +1 FREE 8GB USB
  1 mg (E-Coli)  /  $1,215 +1 FREE 8GB USB
SDS-PAGE
Product Name

Calpain-1 catalytic subunit (CAPN1), Recombinant Protein

Popular Item
Full Product Name

Recombinant Human Calpain-1 catalytic subunit

Product Synonym Names
Calcium-activated neutral proteinase 1; CANP 1; Calpain mu-type; Calpain-1 large subunit; Cell proliferation-inducing gene 30 protein; Micromolar-calpain; muCANP
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Sequence Positions
1-714. Full length.
Sequence
MSEEIITPVY CTGVSAQVQK QRARELGLGR HENAIKYLGQ DYEQLRVRCL QSGTLFRDEA FPPVPQSLGY KDLGPNSSKT YGIKWKRPTE LLSNPQFIVD GATRTDICQG ALGDCWLLAA IASLTLNDTL LHRVVPHGQS FQNGYAGIFH FQLWQFGEWV DVVVDDLLPI KDGKLVFVHS AEGNEFWSAL LEKAYAKVNG SYEALSGGST SEGFEDFTGG VTEWYELRKA PSDLYQIILK ALERGSLLGC SIDISSVLDM EAITFKKLVK GHAYSVTGAK QVNYRGQVVS LIRMRNPWGE VEWTGAWSDS SSEWNNVDPY ERDQLRVKME DGEFWMSFRD FMREFTRLEI CNLTPDALKS RTIRKWNTTL YEGTWRRGST AGGCRNYPAT FWVNPQFKIR LDETDDPDDY GDRESGCSF VLALMQKHR RRERRFGRDM ETIGFAVYEV PPELVGQPAV HLKRDFFLAN ASRARSEQFI NLREVSTRFR LPPGEYVVVP STFEPNKEGD FVLRFFSEKS AGTVELDDQI QANLPDEQVL SEEEIDENFK ALFRQLAGED MEISVKELRT ILNRIISKHK DLRTKGFSLE SCRSMVNLMD RDGNGKLGLV EFNILWNRIR NYLSIFRKFD LDKSGSMSAY EMRMAIESAG FKLNKKLYEL IITRYSEPDL AVDFDNFVCC LVRLETMFRF FKTLDTDLDG VVTFDLFKWL QLTMFA
OMIM
114220
3D Structure
ModBase 3D Structure for P07384
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Purity/Purification
Greater than 90% as determined by SDS-PAGE. (lot specific)
Form/Format
Liquid containing glycerol
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
ISO Certification
Manufactured in an ISO 9001:2008 Certified Laboratory.
Other Notes
Small volumes of CAPN1 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
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

CAPN1 recombinant protein SDS-PAGE image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
NCBI/Uniprot data below describe general gene information for CAPN1. It may not necessarily be applicable to this product.
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
85.9kD
NCBI Official Full Name
calpain-1 catalytic subunit
NCBI Official Synonym Full Names
calpain 1
NCBI Official Symbol
CAPN1  [Similar Products]
NCBI Official Synonym Symbols
CANP; muCL; CANP1; CANPL1; muCANP
  [Similar Products]
NCBI Protein Information
calpain-1 catalytic subunit
UniProt Protein Name
Calpain-1 catalytic subunit
UniProt Synonym Protein Names
Calcium-activated neutral proteinase 1; CANP 1; Calpain mu-type; Calpain-1 large subunit; Cell proliferation-inducing gene 30 protein; Micromolar-calpain; muCANP
Protein Family
UniProt Gene Name
CAPN1  [Similar Products]
UniProt Synonym Gene Names
CANPL1; CANP 1; muCANP  [Similar Products]
UniProt Entry Name
CAN1_HUMAN
NCBI Summary for CAPN1
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 Comments for CAPN1
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
Product References and Citations for CAPN1 recombinant protein
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)

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