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SDS-PAGE

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
Ordering
For Research Use Only!
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

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
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
823
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
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

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Product Notes

The CAPN1 capn1 (Catalog #AAA18465) is a Recombinant Protein produced from E Coli or Yeast or Baculovirus or Mammalian Cell and is intended for research purposes only. The product is available for immediate purchase. The immunogen sequence is 1-714aa; Full Length Protein. The amino acid sequence is listed below: 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 GDRESGCSFV LALMQKHRRR ERRFGRDMET IGFAVYEVPP ELVGQPAVHL KRDFFLANAS RARSEQFINL REVSTRFRLP PGEYVVVPST FEPNKEGDFV LRFFSEKSAG TVELDDQIQA NLPDEQVLSE EEIDENFKAL FRQLAGEDME ISVKELRTIL NRIISKHKDL RTKGFSLESC RSMVNLMDRD GNGKLGLVEF NILWNRIRNY LSIFRKFDLD KSGSMSAYEM RMAIESAGFK LNKKLYELII TRYSEPDLAV DFDNFVCCLV RLETMFRFFK TLDTDLDGVV TFDLFKWLQL TMFA . It is sometimes possible for the material contained within the vial of "Calpain-1 catalytic subunit (CAPN1), Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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