Recombinant Mouse Calpain-1 Catalytic Subunit (CAPN1) Protein (His)

Beta LifeScience SKU/CAT #: BLC-04251P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Mouse Calpain-1 Catalytic Subunit (CAPN1) Protein (His)

Beta LifeScience SKU/CAT #: BLC-04251P
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Product Overview

Description Recombinant Mouse Calpain-1 Catalytic Subunit (CAPN1) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb O35350
Target Symbol CAPN1
Synonyms Capn1; Canp1; Capa1Calpain-1 catalytic subunit; EC 3.4.22.52; Calcium-activated neutral proteinase 1; CANP 1; Calpain mu-type; Calpain-1 large subunit; Micromolar-calpain; muCANP
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-6His
Target Protein Sequence MTEELITPVYCTGVSAQVQKKRDKELGLGRHENAIKYLGQDYETLRARCLQSGVLFQDEAFPPVSHSLGFKELGPHSSKTYGIKWKRPTELMSNPQFIVDGATRTDICQGALGDCWLLAAIASLTLNETILHRVVPYGQSFQDGYAGIFHFQLWQFGEWVDVVIDDLLPTKDGKLVFVHSAQGNEFWSALLEKAYAKVNGSYEALSGGCTSEAFEDFTGGVTEWYDLQKAPSDLYQIILKALERGSLLGCSINISDIRDLEAITFKNLVRGHAYSVTGAKQVTYQGQRVNLIRMRNPWGEVEWKGPWSDSSYEWNKVDPYEREQLRVKMEDGEFWMSFRDFIREFTKLEICNLTPDALKSRTLRNWNTTFYEGTWRRGSTAGGCRNYPATFWVNPQFKIRLEEVDDADDYDNRESGCSFLLALMQKHRRRERRFGRDMETIGFAVYQVPRELAGQPVHLKRDFFLANASRAQSEHFINLREVSNRIRLPPGEYIVVPSTFEPNKEGDFLLRFFSEKKAGTQELDDQIQANLPDEKVLSEEEIDDNFKTLFSKLAGDDMEISVKELQTILNRIISKHKDLRTNGFSLESCRSMVNLMDRDGNGKLGLVEFNILWNRIRNYLTIFRKFDLDKSGSMSAYEMRMAIEAAGFKLNKKLHELIITRYSEPDLAVDFDNFVCCLVRLETMFRFFKLLDTDLDGVVTFDLFKWLQLTMFA
Expression Range 1-713aa
Protein Length Full Length
Mol. Weight 86.1kDa
Research Area Others
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves CTBP1 at 'Asn-375', 'Gly-388' and 'His-410'.
Subcellular Location Cytoplasm. Cell membrane.
Protein Families Peptidase C2 family
Database References

KEGG: mmu:12333

STRING: 10090.ENSMUSP00000025891

UniGene: PMID: 28202907

  • calpain contributes to the regulation of new gene expression that is necessary for these memory processes as a regulator of Ca(2+)-signal transduction pathway. PMID: 29258546
  • the present study suggested that ephrinB/EphB signaling contributes to spinal nociceptive processing via the actions of calpain1 and caspase3. PMID: 29749521
  • Authors provide the first evidence that calpain-1 regulates platelet hyperactivity in sickle mice. PMID: 29101791
  • A total of 55 genes were differentially expressed in micro-calpain knockout mice. PMID: 29775750
  • calpains inhibition plays crucial roles in vascular restenosis by preventing neointimal hyperplasia at the early stage via suppression of the MMP2/TGF-beta1 pathway. PMID: 27453531
  • indicate that calpain-1 and calpain-2 play opposite roles in high increased intraocular pressure-induced ischemic injury PMID: 27185592
  • Results strengthen the roles of both calpain-1 and PHLPP1 in synaptic plasticity and learning and memory, and illustrate the complexities of the interactions between multiple pathways participating in synaptic plasticity. PMID: 27421891
  • Genetic ablation of calpain-1 ameliorates chronic pain behavior in sickle cell mice. PMID: 27418647
  • Our results indicate that calpain mediates cytokine-induced collagen-I synthesis and proliferation of ASMCs via the mTORC2/Akt signalling pathway, thereby regulating airway smooth muscle remodelling in asthma. PMID: 27649066
  • mutations in CAPN1 are an additional cause of ataxia in mammals, including humans. PMID: 27320912
  • Results indicate that calpain-1 and calpain-2 are differentially activated in hippocampus following seizure activity, with calpain-1 activation being limited to a small population of interneurons, and possibly triggering neuroprotective events, while calpain-2 is widely activated in pyramidal neurons of CA1 and CA3, and triggers neurodegenerative cascades. PMID: 27622212
  • Here we show the combined loss of glial glutamate transporters GLT1 and GLAST in spinal cord caused motor neuronal death and hindlimb paralysis. PMID: 28821644
  • These results suggested that Streptococcus pneuomoniae PLY induces the influx of calcium in Streptococcus pneumoniae-infected macrophages, followed by calpain activation and subsequent IL-1alpha maturation and secretion. PMID: 28630064
  • High calpain expression is associated with brain injury. PMID: 27875293
  • the expression of the full-length 60-kDa calcineurin protein is down-regulated due to over-activated calpain that cleaves calcineurin to form a 45-kDa fragment. PMID: 27171192
  • calpains and calpastatin in patients with idiopathic pulmonary arterial hypertension (PAH) and mice with hypoxic or spontaneous (SM22-5HTT(+) strain) PH, were investigated. PMID: 26974350
  • Attenuation of atherosclerotic lesions/inflammation in ApoE KO mice by simvastatin might be associated with the downregulation of CD36 and calpain-1. PMID: 28448973
  • Leukocyte calpain-1/calpain-2 deficiency reduces angiotensin II-induced inflammation and atherosclerosis but not abdominal Aortic aneurysms in mice. PMID: 26966280
  • Taken together, our findings suggested that DHRS7C maintains intracellular Ca(2+) homeostasis involving the ER/SR and that functional loss of DHRS7C leads to Ca(2+) overload in the cytosol and ER/SR, resulting in enlarged cellular morphology via calpain activation PMID: 27806939
  • In conclusion, calpain was involved in oxygen glucose deprivation-induced RGC-5 necroptosis with the increased expression of its downstream molecule tAIF. PMID: 27752886
  • CRYbetaA3/A1-crystallin has a role in preventing nuclear cataract impaired lysosomal cargo clearance and calpain activation PMID: 26863613
  • Capn1 protein and activity in mitochondria were elevated in diabetic mouse hearts. Increased mitochondrial Capn1 was associated with increased mitochondrial ROS generation and oxidative damage and reduced ATP5A1 protein and ATP synthase activity. PMID: 26470784
  • LOX-1 is, at least in part, responsible for the inhibitory effect of ox-LDL on macrophage migration and this process involves calpain-1 and -2. PMID: 26393906
  • Over-expression of Cast inhibits calpain activation and attenuates post-infarction myocardial remodeling. PMID: 25786109
  • Junctophilin-2 is cleaved by calpain at multiple sites, resulting in dysfunctional junctophilin-2 truncations. PMID: 26063807
  • Data indicate that calpain-1 up-regulation induces endoplasmic reticulum (ER) stress. PMID: 25660447
  • Calcitriol stimulates expression of mu-calpain in co-cultured mouse cells. PMID: 24687633
  • Data suggest that vitamin D3 up-regulates skeletal muscle fat deposition, up-regulates muscle u-calpain/Capn1 and m-calpain/Capn2 expression, and down-regulates muscle calpastatin expression. PMID: 25520983
  • Calpain-mediated MFN2 degradation is a novel mechanism regulating mitochondrial fusion during glutamate excitotoxicity. PMID: 25416777
  • in spinal cord of 30 day old mice, activation of calpain-1 produces high amounts of nNOS active species, while in 120 day old mice enhanced-prolonged activation of calpain-1 inactivates nNOS and down-regulates NR2B PMID: 25151305
  • Overexpression of the calpain-specific inhibitor calpastatin reduces human alpha-synuclein processing, aggregation and synaptic impairment in transgenic mice. PMID: 24619358
  • Calpain-2 compensation promotes angiotensin II-induced ascending and abdominal aortic aneurysms in calpain-1 deficient mice. PMID: 23977256
  • Our findings support the therapeutic promise of highly specific calpain inhibition in the treatment of tauopathies and other neurodegenerative states. PMID: 25009256
  • The suppressive effects of PDGF-BB on Ca(2+) overload in neurons were more potent than those of PDGF-AA. PMID: 24454980
  • calpain-1 is identified as a novel regulator in IgE-mediated mast cell activation and could serve as a potential therapeutic target for the management of allergic inflammation. PMID: 24760147
  • The results of the present study highlight a dual role for calpain-1 in the weaned gland after the pregnancy/lactation cycle, controlling programmed cell death and participating in the epigenetic programme during adipocyte differentiation. PMID: 24467364
  • Calpain induced myocardial NF-kappaB activation, TNF-alpha expression, and myocardial dysfunction in septic mice through IkappaBalpha protein cleavage. PMID: 24441549
  • These data contribute to the existing evidence of the importance of the calpain system's involvement in muscle growth, development, and atrophy. PMID: 23798514
  • synaptic NMDAR-coupled mu-calpain activation is neuroprotective PMID: 24285894
  • The calpain/calpastatin system has opposing roles in growth and metastatic dissemination of melanoma. PMID: 23565252
  • data suggest that skNAC controls myoblast migration and sarcomere architecture in a calpain-dependent manner PMID: 23662692
  • Activated skeletal muscle calpain regulates acetylcholine release in motor nerve terminals via nitric oxide and neural microRNAs, a novel mechanism for the modulation of synaptic activity in normal or pathological conditions. PMID: 23616539
  • Both CAPN-1 and -2 were induced after weaning and its activity increased in isolated mitochondria and lysosomes. PMID: 22555453
  • This study demonistrated that conditional model of calpain deficiency in the CNS has provided a clearer understanding of calpain biology in the brain regarding CNS development, synaptic plasticity, and specific neuronal death paradigms. PMID: 23536090
  • Calpain-1 gene deletion improved RBC deformability without any effect on RBC lifespan. Ankyrin, band 3, protein 4.1R, adducin & dematin were not degraded. K+-Cl- co-transporter & the Gardos channel were reduced. PMID: 22870887
  • Potentiation of the platelet spreading phenotype in calpain-1(-/-) mice suggests a novel role of calpain-1 in hemostasis. PMID: 22458296
  • Increased STEP and calpain activation contribute to altered NMDAR localization in an Huntington's disease mouse model. PMID: 22523092
  • Increased lipid peroxidation and low-density lipoprotein oxidation in the brain of hyperlipidemic mice are associated with increased activation of calpain-1/2. PMID: 21836084
  • Calpain cleaves and activates the TRPC5 channel to participate in semaphorin 3A-induced neuronal growth cone collapse. PMID: 22547824

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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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