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Mouse Anti-CAPN1 Recombinant Antibody (CBFYM-0893) (CBMAB-M1041-FY)

This product is mouse antibody that recognizes CAPN1. The antibody CBFYM-0893 can be used for immunoassay techniques such as: FC, ICC, IF, IHC-Fr, IHC, WB.
See all CAPN1 antibodies

Summary

Host Animal
Mouse
Specificity
Cattle, Hamster, Human, Mouse, Pig, Rabbit, Rat
Clone
CBFYM-0893
Antibody Isotype
IgG1
Application
FC, ICC, IF, IHC-Fr, IHC, WB

Basic Information

Immunogen
Purified bovine skeletal muscle 80 kDa mu-calpain subunit
Specificity
Cattle, Hamster, Human, Mouse, Pig, Rabbit, Rat
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

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

Format
Liquid
Buffer
PBS, 0.1% BSA
Preservative
0.05% Sodium azide
Concentration
1 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.

Target

Full Name
Calpain 1
Introduction
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.
Entrez Gene ID
Human823
Mouse12333
Rat29153
Cattle281661
Pig397027
Hamster101834701
Rabbit100009089
UniProt ID
HumanP07384
MouseO35350
RatP97571
CattleQ27970
PigP35750
HamsterA0A1U8D291
RabbitP06815
Alternative Names
Calpain 1; Cell Proliferation-Inducing Gene 30 Protein; Calcium-Activated Neutral Proteinase 1; Calpain 1, (Mu/I) Large Subunit; Calpain-1 Large Subunit; Micromolar-Calpain; Calpain Mu-Type; EC 3.4.22.52; CANP 1; CANPL1
Function
Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction (PubMed:21531719, PubMed:2400579).
Proteolytically cleaves CTBP1 at 'Asn-375', 'Gly-387' and 'His-409' (PubMed:23707407).
Biological Process
Cornification Source: Reactome
Extracellular matrix disassembly Source: Reactome
Mammary gland involution Source: Ensembl
Neutrophil degranulation Source: Reactome
Positive regulation of cell population proliferation Source: ProtInc
Proteolysis Source: UniProtKB
Receptor catabolic process Source: Ensembl
Regulation of catalytic activity Source: UniProtKB
Regulation of macroautophagy Source: ParkinsonsUK-UCL
Regulation of NMDA receptor activity Source: ARUK-UCL
Self proteolysis Source: UniProtKB
Cellular Location
Cell membrane; Cytoplasm. Translocates to the plasma membrane upon Ca2+ binding. In granular keratinocytes and in lower corneocytes, colocalizes with FLG and FLG2 (PubMed:21531719).
Involvement in disease
Spastic paraplegia 76, autosomal recessive (SPG76): A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body.
PTM
Undergoes calcium-induced successive autoproteolytic cleavages that generate a membrane-bound 78 kDa active form and an intracellular 75 kDa active form. Calpastatin reduces with high efficiency the transition from 78 kDa to 75 kDa calpain forms.

Wang, J., Ciampa, G., Zheng, D., Shi, Q., Chen, B., Abel, E. D., ... & Song, L. S. (2021). Calpain-2 Specifically Cleaves Junctophilin-2 at the Same Site as Calpain-1 but with Less Efficacy. Biochemical Journal.

Su, W., Bi, X., Wang, Y., & Baudry, M. (2021). Changes in neurodegeneration-related miRNAs in brains from CAPN1−/− mice. BBA Advances, 1, 100004.

Su, W., Zhou, Q., Wang, Y., Chishti, A., Li, Q. Q., Dayal, S., ... & Baudry, M. (2020). Deletion of the Capn1 gene results in alterations in signaling pathways related to Alzheimer’s disease, protein quality control and synaptic plasticity in mouse brain. Frontiers in genetics, 11, 334.

Lai, L. L., Chen, Y. J., Li, Y. L., Lin, X. H., Wang, M. W., Dong, E. L., ... & Lin, X. (2020). Novel CAPN1 mutations extend the phenotypic heterogeneity in combined spastic paraplegia and ataxia. Annals of clinical and translational neurology, 7(10), 1862-1869.

Matos, A. M., Pinto, F. R., Barros, P., Amaral, M. D., Pepperkok, R., & Matos, P. (2019). Inhibition of calpain 1 restores plasma membrane stability to pharmacologically rescued Phe508del-CFTR variant. Journal of Biological Chemistry, 294(36), 13396-13410.

Cotti Piccinelli, S., Bassi, M. T., Citterio, A., Manganelli, F., Tozza, S., Santorelli, F. M., ... & Filosto, M. (2019). A Novel CAPN1 mutation causes a pure hereditary spastic paraplegia in an Italian family. Frontiers in neurology, 10, 580.

Peng, F., Sun, Y. M., Quan, C., Wang, J., & Wu, J. J. (2019). Two novel homozygous mutations of CAPN1 in Chinese patients with hereditary spastic paraplegia and literatures review. Orphanet journal of rare diseases, 14(1), 1-9.

Kocoglu, C., Gundogdu, A., Kocaman, G., Kahraman-Koytak, P., Uluc, K., Kiziltan, G., ... & Basak, A. N. (2018). Homozygous CAPN1 mutations causing a spastic-ataxia phenotype in 2 families. Neurology Genetics, 4(1).

Liu, B., Zhou, Y., Lu, D., Liu, Y., Zhang, S. Q., Xu, Y., ... & Gu, X. (2017). Comparison of the protein expression of calpain‑1, calpain‑2, calpastatin and calmodulin between gastric cancer and normal gastric mucosa. Oncology letters, 14(3), 3705-3710.

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

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