Recombinant Mouse Calpain-3 (Capn3), partial

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Code CSB-EP720693MO
MSDS
Size $306
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Purity
Greater than 85% as determined by SDS-PAGE.
Target Names
Capn3
Uniprot No.
Research Area
Cell Biology
Species
Mus musculus (Mouse)
Source
E.coli
Expression Region
46-419aa
Target Protein Sequence
IISRNFPIIGVKEKTFEQLRRKCLEKKVLYLDPEFPPDETSLFYSQKFPIQFVWKRPPEICENPRFIIGGANRTDICQGDLGDCWFLAAIACLTLNERLLFRVIPHDQSFTENYAGIFHFQFWRYGDWVDVVIDDCLPTYNNQLVFTKSNHRNEFWSALLEKAYAKLHGSYEALKGGNTTEAMEDFTGGVTEFFEIKDAPSDMYKIMRKAIERGSLMGCSIDDGTNMTYGTSPSGLNMGELIARMVRNMDNSLLRDSDLDPRGSDDRPSRTIVPVQYETRMACGLVKGHAYSVTGLEEALFKGEKVKLVRLRNPWGQVEWNGSWSDGWKDWSFVDKDEKARLQHQVTEDGEFWMSYDDFVYHFTKLEICNLTAD
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
49.1 kDa
Protein Length
Partial
Tag Info
N-terminal 6xHis-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description

The creation of the recombinant Mouse Capn3 protein is achieved through genetic engineering techniques. A specific DNA sequence coding for the Mouse Capn3 protein (46-419aa) is integrated into an expression vector, which serves as a carrier for gene expression. This vector is then introduced into e.coli cells, which are cultured to facilitate the expression of the desired protein. The protein is fused with a N-terminal 6xHis tag. The recombinant Mouse Capn3 protein is subsequently purified using affinity purification, resulting in a purity level exceeding 85%, as verified by SDS-PAGE analysis.

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Target Background

Function
Calcium-regulated non-lysosomal thiol-protease. Proteolytically cleaves CTBP1 at 'His-410'. Mediates, with UTP25, the proteasome-independent degradation of p53/TP53.
Gene References into Functions
  1. Study shows that impaired skeletal muscle regeneration in calpain-3 null muscle is associated with perturbations in mTORC1 signaling and defective mitochondrial biogenesis. PMID: 29241457
  2. calpain 3 is necessary for ubiquitination and that it acts upstream of the ubiquitination machinery PMID: 15961411
  3. Cleavage of C-terminal titin by CAPN3 is associated with limb-girdle muscular dystrophy 2A and tibial muscular dystrophy. PMID: 25877298
  4. these studies reveal a novel interaction between CAPN3 and CaM and identify CaM as the first positive regulator of CAPN3 activity. PMID: 25389288
  5. 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
  6. 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
  7. stretch-induced dynamic redistribution of p94 is dependent on its protease activity and essential to protect muscle from degeneration PMID: 20592470
  8. roles for Na(+) dependence of p94 PMID: 20460380
  9. In vitro experiments have then revealed that only PDLIM1 is cleaved directly by calpain-3. PMID: 19926129
  10. role in muscle maturation PMID: 12084932
  11. C/EBP alpha is required for cleavage of cyclin A by calpain 3 in myeloid precursor cells. PMID: 12105198
  12. several novel enzymatic properties of calpain 3 were identified PMID: 14594950
  13. 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
  14. Overexpression of CAPN3 exacerbates the muscular dystrophy with myositis , leading to a shorter life span and more severe muscular dystrophy. PMID: 16115818
  15. 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
  16. the importance of p94-connectin interaction in the control of p94 functions by regulating autolytic decay of p94 PMID: 16627476
  17. 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
  18. 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
  19. 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
  20. implicate the dynamic nature of connectin molecule as a regulatory scaffold of p94 functions PMID: 18310072
  21. 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
  22. calpain 3 is uniquely activated during lens fiber differentiation. PMID: 19269960
  23. Mitochondrial abnormalities in the skeletal muscle of calpain 3 knockout mice correlate with the presence of oxidative stress. PMID: 19483197

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Subcellular Location
Cytoplasm. Nucleus, nucleolus.
Protein Families
Peptidase C2 family
Database Links
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