Recombinant Rat Calpain-1 catalytic subunit (Capn1)

Code CSB-YP004490RA
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Source Yeast
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Code CSB-EP004490RA
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Source E.coli
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Code CSB-EP004490RA-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP004490RA
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Source Baculovirus
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Code CSB-MP004490RA
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Capn1
Uniprot No.
Alternative Names
Capn1; Cls1; Calpain-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
Rattus norvegicus (Rat)
Expression Region
2-713
Target Protein Sequence
AEELITPVY CTGVSAQVQK QRDKELGLGR HENAIKYLGQ DYENLRARCL QNGVLFQDDA FPPVSHSLGF KELGPNSSKT YGIKWKRPTE LLSNPQFIVD GATRTDICQG ALGDCWLLAA IASLTLNETI LHRVVPYGQS FQEGYAGIFH FQLWQFGEWV DVVVDDLLPT KDGKLVFVHS AQGNEFWSAL LEKAYAKVNG SYEALSGGCT SEAFEDFTGG VTEWYDLQKA PSDLYQIILK ALERGSLLGC SINISDIRDL EAITFKNLVR GHAYSVTDAK QVTYQGQRVN LIRMRNPWGE VEWKGPWSDN SYEWNKVDPY EREQLRVKME DGEFWMSFRD FIREFTKLEI CNLTPDALKS RTLRNWNTTF YEGTWRRGST AGGCRNYPAT FWVNPQFKIR LEEVDDADDY DSRESGCSFL LALMQKHRRR ERRFGRDMET IGFAVYQVPR ELAGQPVHLK RDFFLANASR AQSEHFINLR EVSNRIRLPP GEYIVVPSTF EPNKEGDFLL RFFSEKKAGT QELDDQIQAN LPDEKVLSEE EIDDNFKTLF SKLAGDDMEI SVKELQTILN RIISKHKDLR TNGFSLESCR SMVNLMDRDG NGKLGLVEFN ILWNRIRNYL TIFRKFDLDK SGSMSAYEMR MAIEAAGFKL NKKLHELIIT RYSEPDLAVD FDNFVCCLVR LETMFRFFKI LDTDLDGVVT FDLFKWLQLT MFA
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
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 before Lyophilization
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
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

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-364', 'Gly-377' and 'His-399'.
Gene References into Functions
  1. The protective effect of oxytocin in ischemic stroke may be associated with calpain-1-dependent mechanisms. PMID: 29249590
  2. inhibition of pathological micro-calpain activation may present an interesting novel drug target in the treatment of postherpetic neuralgia. PMID: 28714350
  3. 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
  4. Our findings indicate that calpain-GRIP signaling is essential for the restabilization process that is associated with drug cue memory and the inhibition of calpain activity may be a novel strategy for the prevention of drug relapse. PMID: 28821652
  5. Our results are supportive of the hypothesis that suppression of calpain expression leading to slowing of cell migration is a potential mechanism through which NSAIDs cause GI toxicity. PMID: 28342779
  6. This study demonstrates that Nav channel expression in lumbar motoneurons is altered after SCI, and it shows a tight relationship between the calpain-dependent proteolysis of Nav1.6 channels, the upregulation of I(NaP) and spastici PMID: 26974309
  7. Our results indicate that low calpain activity, due to absence of calpain 1 and degradation of calpain 2, results in a preference for ACD over apoptosis in insulin-deprived HCN cells PMID: 26086870
  8. Calpain-1 activation plays critical role in vascular calcification caused by oxidized low density lipoprotein, which might be mediated by pyrophosphate metabolism disorder. PMID: 26047104
  9. Manganese induces the cleavage of alpha-synuclein protein via overactivation of calpain and subsequent alpha-synuclein oligomerization. PMID: 25756858
  10. study indicates that blocking of calpain during unloading decreases skeletal muscle atrophy by inhibiting UPP activation and preserving anabolic signaling PMID: 26297661
  11. Neuroprotective properties of exogenous calpain regulators differing in the mechanisms of action (sex steroids, calcium regulators) were tested on studied neurodegeneration models. PMID: 25895366
  12. Calpain-mediated MFN2 degradation is a novel mechanism regulating mitochondrial fusion during glutamate excitotoxicity. PMID: 25416777
  13. CAPN1 anchors to two NCX1 regions and cleaves at methionine-369, leading to NCX1 inactivation in heart failure. PMID: 25336645
  14. Ayloid beta mediates calpain cleavage of NCX3 in Alzheimer's disease brain. PMID: 23919677
  15. Reactive oxygen species stimulate calpain activation during glucose deprivation and that this mechanism is involved in neuronal death. PMID: 23994487
  16. Calpain 1 activation contributes to tissue damage and impaired locomotor function following spinal cord injury. PMID: 23102374
  17. a truncated fragment of Src protein kinase generated by calpain-mediated cleavage is a mediator of neuronal death in excitotoxicity PMID: 23400779
  18. Extracellular signal-regulated kinase and glycogen synthase kinase 3beta regulate gephyrin postsynaptic aggregation and GABAergic synaptic function in a calpain-dependent mechanism PMID: 23408424
  19. Calpain-2 expression was slightly decreased, whereas calpain-1 expression was unaltered in tail-suspended rats. PMID: 20945043
  20. Data indicate that calpain-1 plays a pivotal role in matrix metalloproteinase 2 (MMP2) activation and extracellular matrix remodeling, including fibrosis and vascular calcification. PMID: 23006733
  21. passive stretch on soleus muscles may prevent in part unloading-induced atrophy through a calpain signal pathway PMID: 22547201
  22. These findings also identify a mechanism by which site-specific phosphorylation and calpain-mediated cleavage operate in concert to regulate GSK-3beta activity. PMID: 22496446
  23. Calpain-mediated cleavage of fGAD65 is pathological, presumably due to decrease in the activity of synaptic vesicle - associated fGAD65 resulting in a decrease in the GABA synthesis - packaging coupling process leading to reduced GABA neurotransmission. PMID: 22427928
  24. All calpain-3 is bound tightly within a fibre, whereas most mu-calpain ( approximately 0.2 microm) is initially freely diffusible in the cytoplasm at resting [Ca(2+)] but binds within seconds at high [Ca(2+)]. PMID: 16857710
  25. calpain inhibition downregulates expression of proapoptotic proteins and the proinflammatory molecule nuclear factor-kappa B (NF-kappaB) in the retina of Lewis rats with acute EAE. PMID: 21613375
  26. Beclin-1 undergoes proteolytic cleavage by calpain following retinal ischemia-reperfusion. PMID: 21490676
  27. calcium-activated neutral protease was demonstrated in the axon of peripheral nerve , but not in the myelin sheath or endoneurium PMID: 16758583
  28. Calpain inhibitor Calpeptin has a role in preventing focal cerebral ischemia-reperfusion injury in rats PMID: 20473717
  29. Data identified ATP synthase subunit alpha and alpha actinin 3 as key partners of calpains during muscle aging. PMID: 20850499
  30. The expressions of micro-calpain mRNA and protein increase with hypoxic-ischemic brain damage. PMID: 17953355
  31. Activation of the protease core of mu calpain requires cooperative binding of two Ca(2+) atoms at two conserved non-EF-hand sites. The protease region is not affected by calpastatin, and may contribute to calpain-mediated pathologies. PMID: 11893336
  32. difference in Ca2+ requirement for activation of mu- and m-calpain PMID: 12014988
  33. Cell infiltration and increased calpain activity do not begin in the CNS until the onset of clinical signs in experimental autoimmune encephalitis. PMID: 12161014
  34. there is a differential expression of calpain I and II under pathological conditions induced either by endotoxin stimuli or Leydig cell depletion, which may produce a differential effect on IL-1alpha processing. PMID: 12534936
  35. Ca2+-free micro-calpain may represent a partially activated structure, requiring lower Ca2+ concentration to trigger its activation PMID: 14656436
  36. calpain may play a role in the mechanism of oxidative cataract of rat PMID: 15101113
  37. Endosomal uptake of the Tat-calpastatin prevents its interaction with calpain in other cellular compartments. PMID: 15191812
  38. During hypoxia in rat retinas, calpains may be major proteases causing breakdown of neuronal proteins involved in apoptotic cell death PMID: 15979593
  39. the time- and concentration-dependent changes in [Ca2+]i that occurred during concentric exercise fall near but below the level necessary to cause autolysis of calpains in vivo PMID: 16107503
  40. Subsequently, memantine was found to have neuroprotective effects and save striatal cells with decreasing calpain levels in the 3NP model of Huntington's disease PMID: 16959224
  41. The mu-calpain-mediated proteolytic modification of TnT by removing the NH2-terminal variable region of TnT may act as an acute mechanism to adjust muscle contractility under stress conditions. PMID: 16981728
  42. phosphorylation of Thr(138) predominantly defines the susceptibility of p35 to calpain-dependent cleavage and dephosphorylation of this site is a critical determinant of Cdk5-p25-induced cell death associated with neurodegeneration PMID: 17121855
  43. Calpain 1 is involved in atrophy development in slow type skeletal muscle fibers. PMID: 17182728
  44. neuronal loss in primary cortical cultures involves neurodegeneration-like cell death through the activation of calpains and the subsequent processing of p35 to p25 PMID: 17334225
  45. H(2)O(2)-induced activation of p38 MAPK and subsequent HSP25/27 translocation attenuates desmin degradation brought about by calpain-1 activation in ischemia-reperfused hearts. PMID: 17513494
  46. Calpain activation contributes to the inhibition of neurite growth by depolarization. PMID: 18055215
  47. calpain 1 N-terminus is a mitochondrial targeting sequence PMID: 18070881
  48. Taken together, our data suggest that early calpain activation, but not caspase activation, is involved in neurotoxicity in the hippocampus after status epilepticus. PMID: 18088374
  49. Calpain 1 was able to cleave alpha-actinin in the absence of phosphoinositide binding; however, PtdIns(3,4,5)P(3) binding increased the rate of proteolysis, and PtdIns(4,5)P(2) binding significantly inhibited cleavage PMID: 18258589
  50. The present study suggests that Ca(2+), calpain, and p25 in CDK5 pathway may play important roles in Abeta(25-35)-induced tau hyperphosphorylation. PMID: 18289510

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Subcellular Location
Cytoplasm. Cell membrane.
Protein Families
Peptidase C2 family
Database Links
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