Recombinant Mouse Calpain-3 (CAPN3) Protein (His)

Beta LifeScience SKU/CAT #: BLC-00362P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Mouse Calpain-3 (CAPN3) Protein (His)

Beta LifeScience SKU/CAT #: BLC-00362P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

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Product Overview

Description Recombinant Mouse Calpain-3 (CAPN3) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb Q64691
Target Symbol CAPN3
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-6His
Target Protein Sequence IISRNFPIIGVKEKTFEQLRRKCLEKKVLYLDPEFPPDETSLFYSQKFPIQFVWKRPPEICENPRFIIGGANRTDICQGDLGDCWFLAAIACLTLNERLLFRVIPHDQSFTENYAGIFHFQFWRYGDWVDVVIDDCLPTYNNQLVFTKSNHRNEFWSALLEKAYAKLHGSYEALKGGNTTEAMEDFTGGVTEFFEIKDAPSDMYKIMRKAIERGSLMGCSIDDGTNMTYGTSPSGLNMGELIARMVRNMDNSLLRDSDLDPRGSDDRPSRTIVPVQYETRMACGLVKGHAYSVTGLEEALFKGEKVKLVRLRNPWGQVEWNGSWSDGWKDWSFVDKDEKARLQHQVTEDGEFWMSYDDFVYHFTKLEICNLTAD
Expression Range 46-419aa
Protein Length Partial
Mol. Weight 49.1 kDa
Research Area Cell Biology
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. Proteolytically cleaves CTBP1 at 'His-410'. Mediates, with UTP25, the proteasome-independent degradation of p53/TP53.
Subcellular Location Cytoplasm. Nucleus, nucleolus.
Protein Families Peptidase C2 family
Database References

KEGG: mmu:12335

STRING: 10090.ENSMUSP00000028749

UniGene: PMID: 29241457

  • calpain 3 is necessary for ubiquitination and that it acts upstream of the ubiquitination machinery PMID: 15961411
  • Cleavage of C-terminal titin by CAPN3 is associated with limb-girdle muscular dystrophy 2A and tibial muscular dystrophy. PMID: 25877298
  • these studies reveal a novel interaction between CAPN3 and CaM and identify CaM as the first positive regulator of CAPN3 activity. PMID: 25389288
  • our results suggest that a component of FSHD pathogenesis may arise by over-expression of FRG1, reducing Rbfox1 levels and leading to aberrant expression of an altered Calpain 3 protein through dysregulated splicing PMID: 23300487
  • The Ky gene was downregulated in CAPN3 knockout muscles suggesting that Ky protease may play a complementary role in regulating muscle cytoskeleton homeostasis in response to changes in muscle activity PMID: 22820870
  • stretch-induced dynamic redistribution of p94 is dependent on its protease activity and essential to protect muscle from degeneration PMID: 20592470
  • roles for Na(+) dependence of p94 PMID: 20460380
  • In vitro experiments have then revealed that only PDLIM1 is cleaved directly by calpain-3. PMID: 19926129
  • role in muscle maturation PMID: 12084932
  • C/EBP alpha is required for cleavage of cyclin A by calpain 3 in myeloid precursor cells. PMID: 12105198
  • several novel enzymatic properties of calpain 3 were identified PMID: 14594950
  • the Capn3 activation mechanism is similar to the universal activation of caspases and corresponds to an autolysis within the active site of the protease PMID: 14645524
  • Overexpression of CAPN3 exacerbates the muscular dystrophy with myositis , leading to a shorter life span and more severe muscular dystrophy. PMID: 16115818
  • Data suggested that sarcomeric localization of p94 is affected by the combination of contractile status of myofibrils, fiber type compositions, sarcomeric maturation, and the composition of the 'signal complexes' in each region. PMID: 16453164
  • the importance of p94-connectin interaction in the control of p94 functions by regulating autolytic decay of p94 PMID: 16627476
  • These data suggest that the persistence of fusion observed in C3KO cells inhibits subsequent steps of differentiation, such as integrin complex rearrangements and sarcomere assembly. PMID: 16982691
  • These studies are the first to identify possible substrates for CAPN3 in an in vivo system and support a role for CAPN3 in sarcomere remodeling by cleavage of myofibrillar proteins such as MLC1. PMID: 17051641
  • The new compound heterozygous mutations R147X/L212F cause increased autocatalytic activity. Since Arg147 is very close to the active site of the enzyme, R147X may affect the protease activity of calpain 3. L212F may affect the stability of this variant. PMID: 17594342
  • implicate the dynamic nature of connectin molecule as a regulatory scaffold of p94 functions PMID: 18310072
  • CAPN3 to be necessary for recruitment of AldoA to one specific location, namely the triads, which are structural components of muscle responsible for calcium transport and excitation-contraction coupling PMID: 18676612
  • calpain 3 is uniquely activated during lens fiber differentiation. PMID: 19269960
  • Mitochondrial abnormalities in the skeletal muscle of calpain 3 knockout mice correlate with the presence of oxidative stress. PMID: 19483197

    • FAQs

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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.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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