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Mouse Anti-CAPN3 Recombinant Antibody (CBFYC-0797) (CBMAB-C0852-FY)


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Published Data
CBMAB-C0852-FY-1
Mouse Anti-CAPN3 Recombinant Antibody (CBFYC-0797) (CBMAB-C0852-FY) in WB
Analysis of CAPN3 expression in the skeletal muscle by Western blotting. Samples C1-C3, specimens of non-LGMD controls; samples A2-A13, specimens of WES-CAPN3het patients and samples B1-B4, specimens of WES-neg patients. GAPDH and β-actin serve as internal loading control. C1-C3, biceps brachii; A2-A3, A5, A9-A12, and B2-B4, quadriceps; A4, A6-A8, and B1, biceps brachii. ...View More
Macias, A., Fichna, J. P., Topolewska, M., Rȩdowicz, M. J., Kaminska, A. M., & Kostera-Pruszczyk, A. (2021). Targeted next-generation sequencing reveals mutations in non-coding regions and potential regulatory sequences of Calpain-3 gene in polish limb-girdle muscular dystrophy patients. Frontiers in Neuroscience, 15, 692482.
CBMAB-C0852-FY-2
Mouse Anti-CAPN3 Recombinant Antibody (CBFYC-0797) (CBMAB-C0852-FY) in WB
RT-PCR for calpain 3 using primer pairs annealing in exons 14 and 17, and western blots using antibodies against indicated proteins in uninduced (0 day) and 3-, 7-, 14-, and 21-day-induced TA muscles from control and DKO animals. The same TA muscles were used to prepare RNA and protein extracts for RT-PCR and western blots. ...View More
Singh, R. K., Kolonin, A. M., Fiorotto, M. L., & Cooper, T. A. (2018). Rbfox splicing factors maintain skeletal muscle mass by regulating calpain3 and proteostasis. Cell reports, 24(1), 197-208.
CBMAB-C0852-FY-3
Mouse Anti-CAPN3 Recombinant Antibody (CBFYC-0797) (CBMAB-C0852-FY) in WB
Western blot of μ-calpain, m-calpain, calpain-3, calpastatin and GAPDH in C2C12 myotubes. ...View More
Zeng, X., Chen, S., Yang, Y., & Ke, Z. (2017). Acylated and unacylated ghrelin inhibit atrophy in myotubes co-cultured with colon carcinoma cells. Oncotarget, 8(42), 72872.
CBMAB-C0852-FY-4
Mouse Anti-CAPN3 Recombinant Antibody (CBFYC-0797) (CBMAB-C0852-FY) in WB
Representative western blot of native calpain-3 expression. ...View More
Amici, D. R., Pinal-Fernandez, I., Mázala, D. A., Lloyd, T. E., Corse, A. M., Christopher-Stine, L., ... & Chin, E. R. (2017). Calcium dysregulation, functional calpainopathy, and endoplasmic reticulum stress in sporadic inclusion body myositis. Acta neuropathologica communications, 5, 1-11.

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
CBFYC-0797
Antibody Isotype
IgG2a, κ
Application
WB, IP, IF, ELISA, IHC-P

Basic Information

Immunogen
Amino acids 1-80 mapping at the N-terminus of Calpain 3 of human origin.
Host Species
Mouse
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG2a, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
ELISA1:100-1:1,000
IF(ICC)1:50-1:500
IHC-P1:50-1:500

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
< 0.1% sodium azide
Concentration
0.2 mg/ml
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at-20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
AA 210-309

Target

Full Name
CALPAIN 3
Introduction
Calpain, a heterodimer consisting of a large and a small subunit, is a major intracellular protease, although its function has not been well established. This gene encodes a muscle-specific member of the calpain large subunit family that specifically binds to titin. Mutations in this gene are associated with limb-girdle muscular dystrophies type 2A. Alternate promoters and alternative splicing result in multiple transcript variants encoding different isoforms and some variants are ubiquitously expressed.
Entrez Gene ID
825
UniProt ID
P20807
Alternative Names
Calpain 3; New Calpain 1; EC 3.4.22.54; CANPL3; CANP3; NCL-1; Muscle-Specific Calcium-Activated Neutral Protease 3 Large Subunit; Muscle-Specific Calcium-Activated Neutral Protease 3; Calpain P94, Large [Catalytic] Subunit; Calcium-Activated Neutral Proteinase 3; Calpain, Large Polypeptide L3
Function
Calcium-regulated non-lysosomal thiol-protease. Proteolytically cleaves CTBP1 at 'His-409'. Mediates, with UTP25, the proteasome-independent degradation of p53/TP53 (PubMed:23357851, PubMed:27657329).
Biological Process
Apoptotic process Source: UniProtKB
Calcium-dependent self proteolysis Source: UniProtKB
Cellular response to calcium ion Source: UniProtKB
Cellular response to salt stress Source: UniProtKB
G1 to G0 transition involved in cell differentiation Source: Ensembl
Muscle cell cellular homeostasis Source: UniProtKB
Muscle organ development Source: UniProtKB
Muscle structure development Source: UniProtKB
Myofibril assembly Source: UniProtKB
Negative regulation of apoptotic process Source: UniProtKB
Negative regulation of protein sumoylation Source: UniProtKB
Negative regulation of transcription, DNA-templated Source: UniProtKB
Positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
Positive regulation of proteolysis Source: UniProtKB
Positive regulation of release of sequestered calcium ion into cytosol Source: UniProtKB
Positive regulation of satellite cell activation involved in skeletal muscle regeneration Source: UniProtKB
Positive regulation of transcription, DNA-templated Source: UniProtKB
Protein catabolic process Source: UniProtKB
Protein-containing complex assembly Source: UniProtKB
Protein destabilization Source: UniProtKB
Protein localization to membrane Source: UniProtKB
Proteolysis Source: UniProtKB
Regulation of catalytic activity Source: UniProtKB
Regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
Regulation of myoblast differentiation Source: Ensembl
Response to calcium ion Source: UniProtKB
Response to muscle activity Source: UniProtKB
Sarcomere organization Source: UniProtKB
Self proteolysis Source: UniProtKB
Cellular Location
Nucleolus; Cytoplasm
Involvement in disease
Muscular dystrophy, limb-girdle, autosomal recessive 1 (LGMDR1): An autosomal recessive degenerative myopathy characterized by progressive symmetrical atrophy and weakness of the proximal limb muscles and elevated serum creatine kinase. The symptoms usually begin during the first two decades of life, and the disease gradually worsens, often resulting in loss of walking ability 10 or 20 years after onset.
Muscular dystrophy, limb-girdle, autosomal dominant 4 (LGMDD4): A form of autosomal dominant limb-girdle muscular dystrophy, a myopathy characterized by proximal and/or distal muscle weakness and atrophy. The age at onset is variable and can range from the first to the sixth decade, although later onset is less common. LGMDD4 is characterized by onset of proximal muscle weakness in young adulthood, gait difficulties, increased serum creatine kinase, myalgia, and back pain. Some patients may have upper limb involvement. Disease severity and expressivity are highly variable.
More Infomation

Baburuna, Y., Sotnikova, L., & Krestinina, O. (2021). Identification of Phosphorylated Calpain 3 in Rat Brain Mitochondria under mPTP Opening. International Journal of Molecular Sciences, 22(19), 10613.

Chen, L., Tang, F., Gao, H., Zhang, X., Li, X., & Xiao, D. (2021). CAPN3: A muscle‑specific calpain with an important role in the pathogenesis of diseases. International Journal of Molecular Medicine, 48(5), 1-13.

Vissing, J., Dahlqvist, J. R., Roudaut, C., Poupiot, J., Richard, I., Duno, M., & Krag, T. (2020). A single c. 1715G> C calpain 3 gene variant causes dominant calpainopathy with loss of calpain 3 expression and activity. Human Mutation, 41(9), 1507-1513.

Ojima, K., Hata, S., Shinkai-Ouchi, F., Oe, M., Muroya, S., Sorimachi, H., & Ono, Y. (2020). Developing fluorescence sensor probe to capture activated muscle-specific calpain-3 (CAPN3) in living muscle cells. Biology open, 9(9), bio048975.

de Andrade Rosa, I., Correa, S., Costa, M. L., & Mermelstein, C. (2020). The scaffolding protein calpain-3 has multiple distributions in embryonic chick muscle cells and it is essential for the formation of muscle fibers. Tissue and Cell, 67, 101436.

Hata, S., Doi, N., Shinkai-Ouchi, F., & Ono, Y. (2020). A muscle-specific calpain, CAPN3, forms a homotrimer. Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics, 1868(7), 140411.

El-Khoury, R., Traboulsi, S., Hamad, T., Lamaa, M., Sawaya, R., & Ahdab-Barmada, M. (2019). Divergent Features of Mitochondrial Deficiencies in LGMD2A Associated With Novel Calpain-3 Mutations. Journal of Neuropathology & Experimental Neurology, 78(1), 88-98.

Kramerova, I., Torres, J. A., Eskin, A., Nelson, S. F., & Spencer, M. J. (2018). Calpain 3 and CaMKII β signaling are required to induce HSP70 necessary for adaptive muscle growth after atrophy. Human molecular genetics, 27(9), 1642-1653.

Wu, R., Wang, J., Yao, J., Dong, Z., Liu, Y., & Liu, M. (2018). MEF2A regulates Calpain 3 expression in L6 myoblasts. Gene, 668, 204-210.

Yalvac, M. E., Amornvit, J., Braganza, C., Chen, L., Hussain, S. R. A., Shontz, K. M., ... & Sahenk, Z. (2017). Impaired regeneration in calpain-3 null muscle is associated with perturbations in mTORC1 signaling and defective mitochondrial biogenesis. Skeletal muscle, 7(1), 1-18.

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For research use only. Not intended for any clinical use.

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