Name: Recombinant Human Calpain-2 catalytic subunit (CAPN2)
Brand: CUSABIO
SKU: CSB-EP004496HU

Product Details

Purity

Greater than 90% as determined by SDS-PAGE.

Target Names

CAPN2

Uniprot No.

P17655

Research Area

Cancer

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)

Source

E.coli

Expression Region

20-700aa

Target Protein Sequence

SHDRAIKYLNQDYEALRNECLEAGTLFQDPSFPAIPSALGFKELGPYSSKTRGIEWKRPTEICADPQFIIGGATRTDICQGALGDCWLLAAIASLTLNEEILARVVPLNQSFQENYAGIFHFQFWQYGEWVEVVVDDRLPTKDGELLFVHSAEGSEFWSALLEKAYAKINGCYEALSGGATTEGFEDFTGGIAEWYELKKPPPNLFKIIQKALQKGSLLGCSIDITSAADSEAITFQKLVKGHAYSVTGAEEVESNGSLQKLIRIRNPWGEVEWTGRWNDNCPSWNTIDPEERERLTRRHEDGEFWMSFSDFLRHYSRLEICNLTPDTLTSDTYKKWKLTKMDGNWRRGSTAGGCRNYPNTFWMNPQYLIKLEEEDEDEEDGESGCTFLVGLIQKHRRRQRKMGEDMHTIGFGIYEVPEELSGQTNIHLSKNFFLTNRARERSDTFINLREVLNRFKLPPGEYILVPSTFEPNKDGDFCIRVFSEKKADYQAVDDEIEANLEEFDISEDDIDDGFRRLFAQLAGEDAEISAFELQTILRRVLAKRQDIKSDGFSIETCKIMVDMLDSDGSGKLGLKEFYILWTKIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFKMPCQLHQVIVARFADDQLIIDFDNFVRCLVRLETLFKIFKQLDPENTGTIELDLISWLCFSVL
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.

Mol. Weight

82.1kDa

Protein Length

Full Length of Mature Protein

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.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
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°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein 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

Calpain-2 catalytic subunit (CAPN2) CSB-EP004496HU is a recombinant full Length of mature protein carrying a 6xHis-tag at the N-terminus. This protein containing amino acid 20-700 of human CAPN2 was expressed in E.coli. It migrated to a band of 85-90 kDa on the reducing SDS-PAGE gel. Its purity was measured by up to 90%. The recombinant CAPN2 protein may be used as an immunogen for antibody production or in the studies of calpain-2-related cancers. In-stock CAPN2 proteins are available.

CAPN2, a large catalytic subunit, makes up the m-calpain with a small regulatory subunit CAPNS1. m-Calpain activation limits the extent of long-term potentiation (LTP) and is neurodegenerative. Extrasynaptic NMDAR (N-methyl-D-aspartate receptor) activation induces m-calpain activation, resulting in STEP degradation and subsequent activation of the p38 prodeath pathway, ultimately leading to neurotoxicity.

Customer Reviews and Q&A

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■ Q&A

I have contacted us regarding: Recombinant human Calpain-2 catalytic subunit, Cat#CSB-EP004496HU and asked the following:
Would you tell us whether this product has activity?

Very nice to receive your inquiry. That's all right. CSB-EP004496HU is a ready-to-ship protein but we haven't tested its activity yet. There is literature reporting that BP protein has activity. Here is the link:
https://www.jstage.jst.go.jp/article/biochemistry1922/124/5/124_5_957/_pdf The BP protein we provide is full-length which is more likely to be active.

I would like to know if your Recombinant human Calpain-2 catalytic subunit (CSB-EP004496HU) is active.
Do you know if this was tested and confirmed to be biologically active? If yes, please provide this information.

Thanks for your inquiry，It have activity in theory. But we haven't test it. So we can't guarantee. Pls refer to : http://www.uniprot.org/uniprot/P17655

Would you be able to advise if CUSABIO can produce active Recombinant Human and/or mouse Calpain 2 protein?

Thanks for your inquiry. We haven't tested the activity of this protein, cannot 100% guaranteed. But what we provide is the full length of mature protein, and it is purified under mild condition, it is active in theory. There is one article reported that protein derived from Baculovirus is active. For your reference: http://europepmc.org/articles/PMC15374

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

High CCNA2 expression is associated with gefitinib resistance in lung cancer. PMID: 30106446
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
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
Hyperactivated m-calpain induced cytoplasmic accumulation of truncated topoisomerase IIalpha in doxorubicin resistant T47D cells. PMID: 29425806
Results find that overexpression of hTau increases intracellular calcium, which in turn activates calpain-2 and induces degradation of alpha4 nAChR. PMID: 27277673
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
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
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
Calpain-2 upregulates PDGF-induced Akt phosphorylation in pulmonary vascular remodeling via an intracrine TGF-beta1/mTORC2 mechanism. PMID: 27099352
the expression of CAPN2 was elevated in prostate cancer tissues than that in normal control tissues. PMID: 28280729
Calpain 2-mediated cleavage of Atg3 and Atg7 accounts for the impaired autophagy. PMID: 27077802
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
Calpain-2 modulates pulmonary vascular remodeling in pulmonary arterial hypertension. PMID: 26248159
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
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
In a transgenic mouse model, hypoxia-triggered m-calpain activation is involved in endoplasmic reticulum stress-mediated Alzheimer's disease pathogenesis. PMID: 23889979
Small interfering RNA (siRNA)-mediated silencing of m-calpain expression significantly suppressed the adhesive, migrative and invasive potentials of human hepatoma cells. PMID: 23733271
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
The carboxyl tail of alpha-actinin-4 regulates its susceptibility to m-calpain and thus functions in cell migration and spreading. PMID: 23466492
data demonstrate that GSK-3beta plays an important role in regulating tRXRalpha production by calpain II in cancer cells PMID: 23389291
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
The results suggest that calpain-2 and calpastatin expression is important in pancreatic cancers, influencing disease progression PMID: 23140395
High expression of calpain-2 is significantly associated with resistance to platinum-based adjuvant chemotherapy. PMID: 22435971
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
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
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
cleavage of CPEB3 by NMDA-activated calpain 2 accounts for the activity-related translation of CPEB3-targeted RNAs PMID: 22711986
Staining intensity of calpain 2 in ovarian carcinoma decreased with increasing lymph node status. PMID: 22335024
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
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
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
Calpain 2-mediated hTOP1 proteolysis not only impacts its biochemical activities but also alters some cellular functions of hTOP1. PMID: 21086148
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
NHE1 might participate in HIF-1-induced angiogenesis due, at least in part, to the alteration of calpain activity. PMID: 21185840
Findings support the idea that calpain is involved in the turnover of LFA-1 adhesions at the rear of the cell. PMID: 21152086
In brain, calpain-2 plays critical roles in developmental and adult synaptic plasticity. PMID: 20924799
Knockdown of calpain 2 expression using shRNA or chemical inhibition of calpain activity reduced glioblastoma cell invasion by 90%. PMID: 20730561
m-Calpain activation is regulated by its membrane localization and by its binding to phosphatidylinositol 4,5-bisphosphate. PMID: 20729206
Data indicate that calpains are involved in the C-terminal truncation of aggrecan and might have a minor role in arthritic diseases. PMID: 20618160
High m-calpain expression is associated with rhabdomyosarcoma aggressiveness. PMID: 20193680
Overexpression of calpain-2 and low expression of calpastatin may involve in the pathological development of stress urinary incontinence. PMID: 19756344
analysis of a novel role for calpain proteolysis of FAK in regulating adhesion dynamics in motile cells PMID: 20150423
excessive TRPM7 channel activity causes oxidative and nitrosative stresses, producing cell rounding mediated by p38 MAPK/JNK-dependent activation of m-calpain PMID: 20070945
m-Calpain antagonizes RhoA overactivation and endothelial barrier dysfunction under disturbed shear conditions. PMID: 19752040
a higher calpain/calpastatin ratio collaborates with activated ERK to promote the generation of the low molecular weight-AR PMID: 19946123
Overactivation of Ca(2+)-calpain pathways contributes to beta cell dysfunction and apoptosis in type 2 diabetes. PMID: 19861418
Calpain activation in neurodegenerative diseases PMID: 12070670
colocalization with detergent-insoluble rafts on T-cells PMID: 12150984
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
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

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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

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