Mouse Capn3 ELISA Kit (V2LY-0626-LY1381)

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Tested Data
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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Sensitivity
0.55 ng/mL
Detection Range
1-400 ng/mL
Sample Type
Serum, Plasma, cell culture supernates
Specificity
Mouse
Assay Type
Sandwich
Reactivity
Mouse
Assay Time
1.5 h
Molecule Mass
94.2 kDa
Components
  • Pre-coated ELISA plate: 12 wells * 8 detachable strips
  • Standard solution: 0.5ml x1
  • Standard diluent: 3ml x1
  • Streptavidin-HRP: 6ml x1
  • Stop solution: 6ml x1
  • Substrate solution A: 6ml x1
  • Substrate solution B: 6ml x1
  • Wash buffer concentrate (25x): 20ml x1
  • Biotinylated antibody: 1ml x1

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

Storage
Store at 2-8°C
More Infomation

Target

Full Name
CALPAIN 3
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.

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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