Antibody Protein ELISA Kit from MyBioSource header Telephone 1.858.633.0165          
1.855.MyBioSource
Fax 1.858.633.0166    Email sales@mybiosource.com 
tel/fax
menu1 Home Products Ordering Company Help menu7
bottom
   MyBioSource rightarrow Recombinant Protein rightarrow CAPN2  rightarrow LOG IN  rightarrow MY ACCOUNT  rightarrow CART CONTENTS  rightarrow CHECKOUT 
horiz bar
MyBioSource Menu separator
separator
ELISA Kit ELISA Kit
CLIA Kit CLIA Kit
PCR Kit PCR Kit
Monoclonal Antibody Monoclonal Antibody
Polyclonal Antibody Polyclonal Antibody
Secondary Antibody Secondary Antibody
Antigen Antigen
Biochemical Biochemical
cDNA Clone cDNA Clone
siRNA siRNA
Peptide Peptide
Recombinant/Purified Protein Rec./Purified Protein

Custom ELISA Kit Custom ELISA Kit
Custom Protein Custom Protein
Custom Antibody Custom Antibody
Antibody Matched Pairs Antibody Matched Pairs
Antibody & Corresponding Blocking Peptide Pairs Antibody Peptide Pairs
Phospho-Specific Antibodies Phospho Antibodies
Products by Disease Products by Disease
Products by Pathway Products by Pathway
Products by Tissue Products by Tissue

arrow Advanced Search
arrow Submit Technical Q&A
arrow International Distributors
arrow Contact Us
separator
Our Best Sellers moreseparator
separator
 • calcitonin gene related peptide, CGRP ELISA Kit
 • Complement factor H-related protein 1 (CFHR1) ELISA Kit
 • tumor marker DR-70 for lung cancer, DR-70TM ELISA Kit
 • Perforin (PRF1) Antibody
 • LR ELISA Kit
 • ARPC2 Antibody
 • S100A7 Recombinant Protein
 • Angiotensin II (AngII) ELISA Kit
 • Myelin Basic Protein (MBP) ELISA Kit
 • HLA Class 2 Antigen DR11 (HLA-A) Antibody
 • Histone H3.3 (H3F3A) ELISA Kit
 • Alkaline Sphingomyelinase (Alk-Smase) Recombinant Protein
 • Casein Kinase 1, epsilon (CSNK1E) Antibody
 • LTA cDNA Clone
 downarrow more ...
separator
separator
DatasheetFull DatasheetPrinter Friendly DatasheetPrint This DatasheetAdd to Compare ListHave Questions? Ask UsRequest for a Quotation today

CAPN2 recombinant protein :: Calpain-2 catalytic subunit Recombinant Protein

Scan QR to view Datasheet Catalog #    MBS959275
SDS-Page
Unit / Price
0.01 mg (E-Coli)  /  $150 +1 FREE 8GB USB
0.05 mg (E-Coli)  /  $190 +1 FREE 8GB USB
0.1 mg (E-Coli)  /  $285 +1 FREE 8GB USB
0.2 mg (E-Coli)  /  $460 +1 FREE 8GB USB
0.5 mg (E-Coli)  /  $750 +1 FREE 8GB USB
0.05 mg (Yeast)  /  $1,150 +1 FREE 8GB USB
1 mg (E-Coli)  /  $1,180 +1 FREE 8GB USB
0.05 mg (Baculovirus)  /  $1,270 +1 FREE 8GB USB
0.05 mg (Mammalian-Cell)  /  $1,520 +1 FREE 8GB USB
0.2 mg (Yeast)  /  $1,560 +1 FREE 8GB USB
0.1 mg (Baculovirus)  /  $1,610 +2 FREE 8GB USB
0.5 mg (Yeast)  /  $1,765 +2 FREE 8GB USB
0.1 mg (Mammalian-Cell)  /  $2,285 +2 FREE 8GB USB
0.5 mg (Baculovirus)  /  $2,300 +2 FREE 8GB USB
1 mg (Yeast)  /  $2,665 +3 FREE 8GB USB
1 mg (Baculovirus)  /  $3,010 +3 FREE 8GB USB
 
 Go to:   rightarrow  Product Names   rightarrow Product Info   rightarrow Accession #s   rightarrow Product Desc   rightarrow Diseases/Tissues/Pathways   rightarrow Applications   rightarrow References 
 Product Name   

Calpain-2 catalytic subunit (CAPN2), Recombinant Protein

★Popular Item★
 Also Known As   

Recombinant Human Calpain-2 catalytic subunit

 Product Synonym Names    Calcium-activated neutral proteinase 2; CANP 2; Calpain M-type; Calpain large polypeptide L2; Calpain-2 large subunit; Millimolar-calpain; M-calpain
 Product Gene Name   

CAPN2 recombinant protein

[Similar Products]
 Product Synonym Gene Name    CANPL2 [Similar Products]
 Research Use Only    For Research Use Only. Not for use in diagnostic procedures.
Table BarTOPTable Bar
 MBS959275 COA    COA PDF
 Sequence Positions    20-700. Mature full length protein.
 Sequence    SHDRAIKYLN QDYEALRNEC LEAGTLFQDP SFPAIPSALG FKELGPYSSK TRGIEWKRPT EICADPQFII GGATRTDICQ GALGDCWLLA AIASLTLNEE ILARVVPLNQ SFQENYAGIF HFQFWQYGEW VEVVVDDRLP TKDGELLFVH SAEGSEFWSA LLEKAYAKIN GCYEALSGGA TTEGFEDFTG GIAEWYELKK PPPNLFKIIQ KALQKGSLLG CSIDITSAAD SEAITFQKLV KGHAYSVTGA EEVESNGSLQ KLIRIRNPWG EVEWTGRWND NCPSWNTIDP EERERLTRRH EDGEFWMSFS DFLRHYSRLE ICNLTPDTLT SDTYKKWKLT KMDGNWRRGS TAGGCRNYPN TFWMNPQYLI KLEEEDEDEE DGESGCTFLV GLIQKHRRRQ RKMGEDMHTI GFGIYEVPEE LSGQTNIHLS KNFFLTNRAR ERSDTFINLR EVLNRFKLPP GEYILVPSTF EPNKDGDFCI RVFSEKKADY QAVDDEIEAN LEEFDISEDD IDDGFRRLFA QLAGEDAEIS AFELQTILRR VLAKRQDIKS DGFSIETCKI MVDMLDSDGS GKLGLKEFYI LWTKIQKYQK IYREIDVDRS GTMNSYEMRK ALEEAGFKMP CQLHQVIVAR FADDQLIIDF DNFVRCLVRL ETLFKIFKQL DPENTGTIEL DLISWLCFSV L
 OMIM    114230
 3D Structure    ModBase 3D Structure for P17655
Section Bar
 Host    E Coli or Yeast or Baculovirus or Mammalian Cell
Section Bar
 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.
Section Bar
 Production Note    Special Offer: The E. coli host-expressed protein is manufactured from a stock plasmid containing the protein gene. E. coli host-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The E. coli host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select E. coli host-expressed protein for the fastest delivery among all hosts. Please contact us or email to support@mybiosource.com for more details.
Section Bar
 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 CAPN2 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.
Table BarTOPTable Bar
 

Related Product Information for CAPN2 recombinant protein

   Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226'.
 Product Categories/Family for CAPN2 recombinant protein    Cancer
Section Bar
 SDS-Page of CAPN2 recombinant protein    CAPN2 recombinant protein SDS-Page image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
Table BarTOPTable Bar
NCBI/Uniprot data below describe general gene information for CAPN2. It may not necessarily be applicable to this product.
 NCBI GeneID    824
 NCBI Accession #    NP_001139540.1 [Other Products]
Section Bar
 UniProt Primary Accession #    P17655 [Other Products]
 UniProt Secondary Accession #    Q16738; Q6PJT3; Q8WU26; Q9HBB1; A6NDG7; B7ZA96; E7ES58 [Other Products]
 UniProt Related Accession #    P17655 [Other Products]
 Molecular Weight    82.2kD
Table BarTOPTable Bar
 NCBI Official Synonym Full Names    calpain 2
 NCBI Official Symbol    CAPN2 [Similar Products]
 NCBI Official Synonym Symbols   
CANP2; mCANP; CANPL2; CANPml
[Similar Products]
 NCBI Protein Information    calpain-2 catalytic subunit
 UniProt Protein Name    Calpain-2 catalytic subunit
 UniProt Synonym Protein Names   
Calcium-activated neutral proteinase 2; CANP 2; Calpain M-type; Calpain large polypeptide L2; Calpain-2 large subunit; Millimolar-calpain; M-calpain
 Protein Family    Calpain
 UniProt Gene Name    CAPN2 [Similar Products]
 UniProt Synonym Gene Names    CANPL2; CANP 2; M-calpain [Similar Products]
 UniProt Entry Name    CAN2_HUMAN
Section Bar
 NCBI Summary for CAPN2    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 2. Multiple heterogeneous transcriptional start sites in the 5' UTR have been reported. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Mar 2009]
Section Bar
 UniProt Comments for CAPN2    Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226' (PubMed:17650508). Proteolytically cleaves CPEB3 following neuronal stimulation which abolishes CPEB3 translational repressor activity, leading to translation of CPEB3 target mRNAs ().
Table BarTOPTable Bar
 

Product References and Citations for CAPN2 recombinant protein

   Molecular cloning of the cDNA for the large subunit of the high-Ca2+-requiring form of human Ca2+-activated neutral protease.Imajoh S., Aoki K., Ohno S., Emori Y., Kawasaki H., Sugihara H., Suzuki K.Biochemistry 27:8122-8128(1988) cDNA cloning by amplification of circularized first strand cDNAs reveals non-IRE-regulated iron-responsive mRNAs.Ye Z., Connor J.R.Biochem. Biophys. Res. Commun. 275:223-227(2000) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) NIEHS SNPs programThe DNA sequence and biological annotation of human chromosome 1.Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.Nature 441:315-321(2006) Tandemly reiterated negative enhancer-like elements regulate transcription of a human gene for the large subunit of calcium-dependent protease.Hata A., Ohno S., Akita Y., Suzuki K.J. Biol. Chem. 264:6404-6411(1989) Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.Nat. Biotechnol. 21:566-569(2003) Characterization of the intracellular proteolytic cleavage of myocilin and identification of calpain II as a myocilin-processing protease.Sanchez-Sanchez F., Martinez-Redondo F., Aroca-Aguilar J.D., Coca-Prados M., Escribano J.J. Biol. Chem. 282:27810-27824(2007) 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) The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium.Strobl S., Fernandez-Catalan C., Braun M., Huber R., Masumoto H., Nakagawa K., Irie A., Sorimachi H., Bourenkow G., Bartunik H., Suzuki K., Bode W.Proc. Natl. Acad. Sci. U.S.A. 97:588-592(2000) 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)
Section Bar
 Research Articles on CAPN2    1. The combination of Ca2+ and ionomycin was required to activate calpain 2, resulting in the further degradation of Dicer and the appearance of a degradation product similar to that detected in platelets from some diabetic individuals.
Table BarTOPTable Bar
 Precautions    All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.
 Disclaimer    While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.
Table BarTOPTable Bar
Products associated with CAPN2 recombinant proteinPathways associated with CAPN2 recombinant protein
 Reference Product  PubMed Publications
 CAPNS1 recombinant protein  >16 publications with CAPN2 and CAPNS1
 CAST recombinant protein  >4 publications with CAPN2 and CAST
 SRC recombinant protein  >2 publications with CAPN2 and SRC
 TLN1 recombinant protein  >2 publications with CAPN2 and TLN1
 CDK5R1 recombinant protein  >1 publications with CAPN2 and CDK5R1
 MAPK3 recombinant protein  >1 publications with CAPN2 and MAPK3
 TLN2 recombinant protein  >1 publications with CAPN2 and TLN2
 Products by Pathway  Pathway Diagram
 Alzheimer's Disease Pathway antibodies  Alzheimer's Disease Pathway Diagram
 Alzheimer's Disease Pathway antibodies  Alzheimer's Disease Pathway Diagram
 Alzheimers Disease Pathway antibodies  Alzheimers Disease Pathway Diagram
 Apoptosis Pathway antibodies  Apoptosis Pathway Diagram
 Apoptosis Pathway antibodies  Apoptosis Pathway Diagram
 ErbB1 Downstream Signaling Pathway antibodies  ErbB1 Downstream Signaling Pathway Diagram
 Focal Adhesion Pathway antibodies  Focal Adhesion Pathway Diagram
 Focal Adhesion Pathway antibodies  Focal Adhesion Pathway Diagram
 Integrin-mediated Cell Adhesion Pathway antibodies  Integrin-mediated Cell Adhesion Pathway Diagram
 Protein Processing In Endoplasmic Reticulum Pathway antibodies  Protein Processing In Endoplasmic Reticulum Pathway Diagram
Diseases associated with CAPN2 recombinant proteinOrgans/Tissues associated with CAPN2 recombinant protein
 Disease Name  Pubmed Publications
 Nervous System Diseases Antibodies  >7 publications with CAPN2 and Nervous System Diseases
 Inflammation Antibodies  >6 publications with CAPN2 and Inflammation
 Breast Neoplasms Antibodies  >6 publications with CAPN2 and Breast Neoplasms
 Cardiovascular Diseases Antibodies  >4 publications with CAPN2 and Cardiovascular Diseases
 Heart Diseases Antibodies  >3 publications with CAPN2 and Heart Diseases
 Carcinoma, Hepatocellular Antibodies  >2 publications with CAPN2 and Carcinoma, Hepatocellular
 Liver Neoplasms Antibodies  >2 publications with CAPN2 and Liver Neoplasms
 Hypertrophy Antibodies  >2 publications with CAPN2 and Hypertrophy
 Liver Diseases Antibodies  >2 publications with CAPN2 and Liver Diseases
 Necrosis Antibodies  >2 publications with CAPN2 and Necrosis
 Organ/Tissue Name  Pubmed Publications
 Muscle Antibodies  >17 publications with CAPN2 and Muscle
 Brain Antibodies  >8 publications with CAPN2 and Brain
 Embryonic Tissue Antibodies  >7 publications with CAPN2 and Embryonic Tissue
 Nerve Antibodies  >5 publications with CAPN2 and Nerve
 Blood Antibodies  >5 publications with CAPN2 and Blood
 Lung Antibodies  >4 publications with CAPN2 and Lung
 Liver Antibodies  >3 publications with CAPN2 and Liver
 Bone Antibodies  >3 publications with CAPN2 and Bone
 Heart Antibodies  >3 publications with CAPN2 and Heart
 Prostate Antibodies  >2 publications with CAPN2 and Prostate
Table BarTOPTable Bar
horiz bar
 SSL   Follow us on Facebook Follow us onTwitter Follow us on Google Plus Connect us on LinkedIn Subscribe to our RSS Feed for latest products and special promotions