Recombinant Human Calpain-2 catalytic subunit (CAPN2)

Code CSB-YP004496HU
MSDS
Size Pls inquire
Source Yeast
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-EP004496HU-B
MSDS
Size Pls inquire
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.
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-BP004496HU
MSDS
Size Pls inquire
Source Baculovirus
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-MP004496HU
MSDS
Size Pls inquire
Source Mammalian cell
Have Questions? Leave a Message or Start an on-line Chat

Product Details

Purity
>85% (SDS-PAGE)
Target Names
CAPN2
Uniprot No.
Alternative Names
Calcium activated neutral proteinase 2; Calcium activated neutral proteinase; Calcium-activated neutral protease 2; catalytic subunit; Calcium-activated neutral proteinase 2; CALP80; Calpain 2 (m/II) large subunit; Calpain 2 catalytic subunit; Calpain 2 large catalytic subunit; Calpain 2 large subunit; Calpain 2; large [catalytic] subunit; Calpain large polypeptide L2; Calpain M type; Calpain M-type; Calpain-2 catalytic subunit; Calpain-2 large subunit; Calpain2; CAN2_HUMAN; CANP 2; CANP L2; CANP2; CANPL 2; CANPL2; CANPml; Capa2; CAPN 2; CAPN2; FLJ39928; M calpain; M calpin; M type; M-calpain; mCANP; Millimolar calpain; Millimolar-calpain
Species
Homo sapiens (Human)
Expression Region
20-700
Target Protein Sequence
S HDRAIKYLNQ DYEALRNECL EAGTLFQDPS FPAIPSALGF KELGPYSSKT RGIEWKRPTE ICADPQFIIG GATRTDICQG ALGDCWLLAA IASLTLNEEI LARVVPLNQS FQENYAGIFH FQFWQYGEWV EVVVDDRLPT KDGELLFVHS AEGSEFWSAL LEKAYAKING CYEALSGGAT TEGFEDFTGG IAEWYELKKP PPNLFKIIQK ALQKGSLLGC SIDITSAADS EAITFQKLVK GHAYSVTGAE EVESNGSLQK LIRIRNPWGE VEWTGRWNDN CPSWNTIDPE ERERLTRRHE DGEFWMSFSD FLRHYSRLEI CNLTPDTLTS DTYKKWKLTK MDGNWRRGST AGGCRNYPNT FWMNPQYLIK LEEEDEDEED GESGCTFLVG LIQKHRRRQR KMGEDMHTIG FGIYEVPEEL SGQTNIHLSK NFFLTNRARE RSDTFINLRE VLNRFKLPPG EYILVPSTFE PNKDGDFCIR VFSEKKADYQ AVDDEIEANL EEFDISEDDI DDGFRRLFAQ LAGEDAEISA FELQTILRRV LAKRQDIKSD GFSIETCKIM VDMLDSDGSG KLGLKEFYIL WTKIQKYQKI YREIDVDRSG TMNSYEMRKA LEEAGFKMPC QLHQVIVARF ADDQLIIDFD NFVRCLVRLE TLFKIFKQLD PENTGTIELD LISWLCFSVL
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

 Customer Reviews

There are currently no reviews for this product.

Submit a Review here

Target Background

Function
Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226'. Proteolytically cleaves CPEB3 following neuronal stimulation which abolishes CPEB3 translational repressor activity, leading to translation of CPEB3 target mRNAs.
Gene References into Functions
  1. High CCNA2 expression is associated with gefitinib resistance in lung cancer. PMID: 30106446
  2. in the field of neural injury, calpain-2 and caspase-3 proteases generate breakdown-products (BDPs) fragments that are indicative of different neural cell death mechanisms in different injury scenarios. Advanced proteomic techniques have shown a remarkable progress in identifying these BDPs experimentally PMID: 28112201
  3. The results of the present study suggested that miR93 regulated MMP1 and collagen I expression in fibroblasts via calpain2. miR93 mediated collagen expression in stress urinary incontinence via calpain2. PMID: 29115452
  4. Hyperactivated m-calpain induced cytoplasmic accumulation of truncated topoisomerase IIalpha in doxorubicin resistant T47D cells. PMID: 29425806
  5. Results find that overexpression of hTau increases intracellular calcium, which in turn activates calpain-2 and induces degradation of alpha4 nAChR. PMID: 27277673
  6. m-calpain translocated as the result of calcium influx was involved in DNA double-strand breaks repair, especially in the non-homologous end-joining pathway through proteolysis of nuclear Ku80. Cleaved Ku80 was still able to form a heterodimer with Ku70 and enhance DNA repair activity. PMID: 27121057
  7. 3 novel loci associated with serum alpha-carotene concentrations among a population that consumed a controlled diet. While replication is necessary, the CAPN2/CAPN8 locus provides compelling evidence for an association with serum alpha-carotene concentrations and may suggest a relationship with the development and progression of cancers. PMID: 28002826
  8. The inhibitory effects of BMP4 on PDGF-induced cell proliferation, collagen synthesis, and calpain-2 activation are impaired in pulmonary artery smooth muscle cells from pulmonary arterial hypertension patient. PMID: 28235949
  9. Calpain-2 upregulates PDGF-induced Akt phosphorylation in pulmonary vascular remodeling via an intracrine TGF-beta1/mTORC2 mechanism. PMID: 27099352
  10. the expression of CAPN2 was elevated in prostate cancer tissues than that in normal control tissues. PMID: 28280729
  11. Calpain 2-mediated cleavage of Atg3 and Atg7 accounts for the impaired autophagy. PMID: 27077802
  12. Calcineurin together with its upstream molecule, calpain 2, and its downstream effector, NFAT-c3, might contribute to the development of atrial fibrillation in patients with heart valve disease and diabetes. PMID: 27123462
  13. Calpain-2 modulates pulmonary vascular remodeling in pulmonary arterial hypertension. PMID: 26248159
  14. Taken together, our results demonstrated the deregulation of GAS2 in both AML and ALL and the requirement of GAS2-Calpain2 axis for the growth of leukemic cells. PMID: 26358320
  15. The combination of Ca2+ and ionomycin was required to activate calpain 2, resulting in the further degradation of Dicer and the appearance of a degradation product similar to that detected in platelets from some diabetic individuals. PMID: 25944670
  16. In a transgenic mouse model, hypoxia-triggered m-calpain activation is involved in endoplasmic reticulum stress-mediated Alzheimer's disease pathogenesis. PMID: 23889979
  17. Small interfering RNA (siRNA)-mediated silencing of m-calpain expression significantly suppressed the adhesive, migrative and invasive potentials of human hepatoma cells. PMID: 23733271
  18. The data reveal that hGAAP is a novel regulator of focal adhesion dynamics, cell adhesion, and migration by controlling localized Ca(2+)-dependent activation of calpain 2. PMID: 23940116
  19. The carboxyl tail of alpha-actinin-4 regulates its susceptibility to m-calpain and thus functions in cell migration and spreading. PMID: 23466492
  20. data demonstrate that GSK-3beta plays an important role in regulating tRXRalpha production by calpain II in cancer cells PMID: 23389291
  21. alpha-II spectrin was drastically accumulated in infected T cells derived from adult T-cell leukemia patients, whereas its digestive protease calpain-2 (CAN2) was significantly downregulated. PMID: 23538341
  22. The results suggest that calpain-2 and calpastatin expression is important in pancreatic cancers, influencing disease progression PMID: 23140395
  23. High expression of calpain-2 is significantly associated with resistance to platinum-based adjuvant chemotherapy. PMID: 22435971
  24. Expression of the large catalytic subunit of calpain-2 is significantly associated with clinical outcome of patients with triple-negative and basal-like disease. PMID: 22745213
  25. betaig-h3 co-localized with integrin alpha5beta1 to enhance the invasion of U87 cells, and that calpain-2, is involved in this process, acting as a downstream molecule. PMID: 22629380
  26. Two human hepatocellular carcinoma cell lines were researched using proteomics. A proteolysis network was built up, of which the CAPN2 centered subnetwork, including SPTBN1, ATP5B, and VIM, was more active in the highly metastatic HCC cell line. PMID: 22623320
  27. cleavage of CPEB3 by NMDA-activated calpain 2 accounts for the activity-related translation of CPEB3-targeted RNAs PMID: 22711986
  28. Staining intensity of calpain 2 in ovarian carcinoma decreased with increasing lymph node status. PMID: 22335024
  29. Subtype-selective induction of m-calpain in aorta during atherosclerotic progression is associated with proteolytic disorganization of VE-cadherin and proatherogenic hyperpermeability in cells. PMID: 22064597
  30. The expression of m-calpain-induced degradation products of extracellular matrix was correlated with the degree of disc degeneration in human intervertebral disc tissue PMID: 21839844
  31. Data show that transfection of cells with GRP78 or calpain I and calpain II siRNA reduced MPTB-mediated cell apoptosis in chondrosarcoma JJ012 cells. PMID: 21374734
  32. Calpain 2-mediated hTOP1 proteolysis not only impacts its biochemical activities but also alters some cellular functions of hTOP1. PMID: 21086148
  33. Confocal immunostaining demonstrated colocalization of m-calpain and the aggrecan product within the lower hypertrophic chondrocytes and in limited region of the pericellular matrix. PMID: 21117903
  34. NHE1 might participate in HIF-1-induced angiogenesis due, at least in part, to the alteration of calpain activity. PMID: 21185840
  35. Findings support the idea that calpain is involved in the turnover of LFA-1 adhesions at the rear of the cell. PMID: 21152086
  36. In brain, calpain-2 plays critical roles in developmental and adult synaptic plasticity. PMID: 20924799
  37. Knockdown of calpain 2 expression using shRNA or chemical inhibition of calpain activity reduced glioblastoma cell invasion by 90%. PMID: 20730561
  38. m-Calpain activation is regulated by its membrane localization and by its binding to phosphatidylinositol 4,5-bisphosphate. PMID: 20729206
  39. Data indicate that calpains are involved in the C-terminal truncation of aggrecan and might have a minor role in arthritic diseases. PMID: 20618160
  40. High m-calpain expression is associated with rhabdomyosarcoma aggressiveness. PMID: 20193680
  41. Overexpression of calpain-2 and low expression of calpastatin may involve in the pathological development of stress urinary incontinence. PMID: 19756344
  42. analysis of a novel role for calpain proteolysis of FAK in regulating adhesion dynamics in motile cells PMID: 20150423
  43. excessive TRPM7 channel activity causes oxidative and nitrosative stresses, producing cell rounding mediated by p38 MAPK/JNK-dependent activation of m-calpain PMID: 20070945
  44. m-Calpain antagonizes RhoA overactivation and endothelial barrier dysfunction under disturbed shear conditions. PMID: 19752040
  45. a higher calpain/calpastatin ratio collaborates with activated ERK to promote the generation of the low molecular weight-AR PMID: 19946123
  46. Overactivation of Ca(2+)-calpain pathways contributes to beta cell dysfunction and apoptosis in type 2 diabetes. PMID: 19861418
  47. Calpain activation in neurodegenerative diseases PMID: 12070670
  48. colocalization with detergent-insoluble rafts on T-cells PMID: 12150984
  49. localization of m-calpain within caveolae may contribute to maintenance of the enzyme in an inactive state and that m-calpain may also contribute to the regulation of calcium-sensing receptor levels. PMID: 12783889
  50. activation of m-calpain during mitosis is required for cells to establish the chromosome alignment by regulating some molecules that generate polar ejection force PMID: 14688278

Show More

Hide All

Subcellular Location
Cytoplasm. Cell membrane. Note=Translocates to the plasma membrane upon Ca(2+) binding.
Protein Families
Peptidase C2 family
Tissue Specificity
Ubiquitous.
Database Links

HGNC: 1479

OMIM: 114230

KEGG: hsa:824

STRING: 9606.ENSP00000295006

UniGene: Hs.350899

icon of phone
Call us
301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
icon of address
Address
7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
icon of social media
Join us with

Subscribe newsletter

Leave a message

* To protect against spam, please pass the CAPTCHA test below.
CAPTCHA verification
© 2007-2024 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1