Recombinant Human Caspase-2 (CASP2) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-10132P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) CASP2.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) CASP2.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) CASP2.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) CASP2.
Greater than 90% as determined by SDS-PAGE.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) CASP2.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) CASP2.

Recombinant Human Caspase-2 (CASP2) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-10132P
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Product Overview

Description Recombinant Human Caspase-2 (CASP2) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P42575
Target Symbol CASP2
Synonyms CASP 2; CASP-2; Casp2; CASP2_HUMAN; Caspase 2; Caspase 2 apoptosis related cysteine peptidase; Caspase-2 subunit p12; Caspase2; ICH 1; ICH 1 protease; ICH 1L; ICH1; ICH1 protease; ICH1L; NEDD-2; NEDD2; Neural precursor cell expressed developmentally down-regulated protein 2; PPP1R57; Protease ICH-1; Protein phosphatase 1 regulatory subunit 57
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence AAPSAGSWSTFQHKELMAADRGRRILGVCGMHPHHQETLKKNRVVLAKQLLLSELLEHLLEKDIITLEMRELIQAKVGSFSQNVELLNLLPKRGPQAFDAFCEALRETKQGHLEDMLLTTLSGLQHVLPPLSCDYDLSLPFPVCESCPLYKKLRLSTDTVEHSLDNKDGPVCLQVKPCTPEFYQTHFQLAYRLQSRPRGLALVLSNVHFTGEKELEFRSGGDVDHSTLVTLFKLLGYDVHVLCDQTAQEMQEKLQNFAQLPAHRVTDSCIVALLSHGVEGAIYGVDGKLLQLQEVFQLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQDGKNHAGSPGCEESDAGKEKLPKMRLPTRSDMICGYACLKGTAAMRNTKRGSWYIEALAQVFSERACDMHVADMLVKVNALIKDREGYAPGTEFHRCKEMSEYCSTLCRHLYLFPGHPPT
Expression Range 2-452aa
Protein Length Full Length of Mature Protein
Mol. Weight 66.6kDa
Research Area Cancer
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 Involved in the activation cascade of caspases responsible for apoptosis execution. Might function by either activating some proteins required for cell death or inactivating proteins necessary for cell survival. Associates with PIDD1 and CRADD to form the PIDDosome, a complex that activates CASP2 and triggers apoptosis in response to genotoxic stress.
Protein Families Peptidase C14A family
Database References

HGNC: 1503

OMIM: 600639

KEGG: hsa:835

STRING: 9606.ENSP00000312664

UniGene: PMID: 29621545

  • Results suggest that TG-induced macrophage cell death is mediated via the caspase-2. PMID: 28768565
  • study demonstrates that apoptosis inhibitor 5 (API5/AAC11) is an endogenous and direct inhibitor of caspase-2. API5 protein directly binds to the caspase recruitment domain (CARD) of caspase-2 and impedes dimerization and activation of caspase-2. PMID: 28336776
  • This peptide, Ac-VDTTD-AFC, was efficiently cleaved by purified caspase-2 and auto-activating caspase-2 in mammalian cells, and exhibited better selectivity for caspase-2 relative to caspase-3 than reagents that are currently available. PMID: 27919034
  • There results support a special role for miR-149 in malignant glioma by targeting Caspase-2 PMID: 27049919
  • Whole exome sequencing (WES) of an affected fetus, and subsequent Sanger sequencing of the second fetus, revealed a homozygous frameshift variant in CRADD, which encodes an adaptor protein that interacts with PIDD and caspase-2 to initiate apoptosis PMID: 28686357
  • This study shows that human procaspase-2 interaction with 14-3-3 zeta is governed by phosphorylation at both S139 and S164. PMID: 28943433
  • NPM1-dependent nucleolar PIDDosome is a key initiator of the caspase-2 activation cascade. PMID: 28432080
  • Sensitization of colon carcinoma cells to radiation-induced cell death and DNA-damage by HuR knockdown critically depends on caspase-2. PMID: 28219770
  • BCL9L dysfunction contributes to aneuploidy tolerance in both TP53-WT and mutant cells by reducing basal caspase-2 levels and preventing cleavage of MDM2 and BID. PMID: 28073006
  • CASP2 down-regulation had a reverse relationship with miR-383 down-regulation in regulating epithelial ovarian cancer development. PMID: 27567588
  • Results suggest that mutations at all three cleavage sites of caspase-2 protein neither affect the macromolecular core complex assembly, nor modify caspase-2 activity upon DNA damage. Consequently, caspase-2 activation occurs in the macromolecular complex without its dissociation. PMID: 27193717
  • These findings indicate that miR-125a-5p decreases after HOTAIR knockdown to promote cancer cell apoptosis by releasing caspase 2. PMID: 26962687
  • these studies elucidate a Caspase-2-p53 signaling network that impacts lung tumorigenesis and chemotherapy response in vivo. PMID: 25301067
  • We have also demonstrated that these correlations are tissue specific being reduced (CASP9 and CASP10) or different (CASP2) in the liver PMID: 25330190
  • the initiator caspase-2 is required for robust death of ovarian cancer cells induced by FASN inhibitors PMID: 25151963
  • HuR sensitizes adenocarcinoma cells to the intrinsic apoptotic pathway by upregulating the translation of caspase-2. PMID: 25010987
  • Authors have demonstrated in vitro and in vivo that loss of function of caspase-2 allows to escape oncogenic stress induced senescence. PMID: 25114039
  • Data strongly argue against a critical role for caspase-2 in ER-stress-induced apoptosis. PMID: 24292555
  • axon regeneration promoted by suppression of CASP2 and CASP6 is CNTF-dependent and mediated through the JAK/STAT signalling pathway PMID: 24727569
  • Our results reveal a novel mechanism of caspase-2 pre-mRNA splicing. PMID: 24321384
  • TRIM16 can promote apoptosis by directly modulating caspase-2 activity in cancer cells. PMID: 23404198
  • The role of caspase-2 isoforms in the progression of breast cancer may considerably differ between pre- and post-chemotherapy patients. PMID: 23469978
  • MiR-708 may act as an oncogene and induce the carcinogenicity of bladder cancer by down-regulating Caspase-2 level. PMID: 23568547
  • caspase-2 has a role as an initiator caspase in lipoapoptosis PMID: 23553630
  • Data indicate induction of caspase-2 by sorting nexin 5 (SNX5) in papillary thyroid carcinoma PMID: 22486813
  • activated human caspase-2 shares remarkably overlapping protease specificity with the prototype apoptotic executioner caspases-3 and -7, suggesting that caspase-2 could function as a proapoptotic caspase once released from the activating complex. PMID: 22825847
  • IRE1alpha regulates translation of a proapoptotic protein, Caspase-2, through terminating microRNA biogenesis, and noncoding RNAs are part of the ER stress response PMID: 23042294
  • These results revealed a thus far unknown, obligatory role for caspase-2 as an initiator caspase during pore-forming toxins -mediated apoptosis. PMID: 22531785
  • caspase-2 acts upstream of caspase-3 and that caspase-2 functions in response to DNA damage in both PhSe-T- and MeSe-T-induced apoptosis. PMID: 22002103
  • Tumor-suppressing function of caspase-2 requires catalytic site Cys-320 and site Ser-139 in mice. PMID: 22396545
  • TAp73alpha represses caspase-2 enzymatic activity and by this means reduce caspase-2 induced Bax activation, loss of mitochondrial transmembrane potential and resulting apoptosis in small cell lung carcinoma cells. PMID: 22201672
  • Data suggest that this novel role of caspase-2 as a translational regulator of p21 expression occurs not only independently of its enzymatic activity but also does not require known caspase-2-activating platforms. PMID: 21475302
  • Findings suggest that XPC enhances DNA damage-induced apoptosis through inhibition of caspase-2 (casp-2S) transcription. PMID: 22174370
  • Studies indicate that DNA damage may trigger caspase 2 activation. PMID: 22077397
  • somatic mutation of caspase-2 is rare in gastric and colorectal carcinomas. PMID: 21940110
  • ras-induced down-regulation of caspase-2 represents a novel mechanism by which oncogenic Ras protects malignant intestinal epithelial cells from anoikis PMID: 21903589
  • Structural and enzymatic insights into caspase-2 protein substrate recognition and catalysis. PMID: 21828056
  • Caspase-2 directly cleaves the E3 ubiquitin ligase Mdm2 at Asp 367, leading to loss of the C-terminal RING domain responsible for p53 ubiquitination. PMID: 21726810
  • analyzed cancer tissues from acute leukemias, breast cancers, lung cancers, and liver cancers for the detection of caspase-2 somatic mutations PMID: 21332795
  • The changes of caspase-2 and caspase-5 activities could be indicative of their involvement in the cervical malignancy mechanisms. PMID: 21051981
  • Activation of caspase-9, but not caspase-2 or caspase-8, is essential for heat-induced apoptosis in Jurkat cells. PMID: 20978129
  • This review discusses recent advances that have been made to help elucidate the true role of caspase 2 and the potential contribution of caspase-2 to the pathology of human diseases including cancer. PMID: 20158568
  • caspase-2 activation is commonly associated with induction of IFN-beta-induced apoptosis in IFN-beta-sensitive melanoma cells PMID: 20187765
  • we suggest that caspase-2 and/or -8 plays an important role in regulating gamma-secretase and may possibly provide a basis for the development of therapeutics targeting apoptosis PMID: 20143425
  • The expressions of PIDD and RAIDD are upregulated during tumour progression in renal cell carcinomas. PMID: 20208132
  • caspase 2 functions as an endogenous inhibitor of NFkappaB-dependent cell survival and this mechanism may contribute to tumor suppression in humans. PMID: 19935698
  • Data show that the N-t-boc-Daidzein induced apoptosis is characterized by caspase activation, XIAP and AKT degradation. PMID: 19738422
  • Data indicate that caspase activity was not essential for docetaxel-induced cytotoxicity since cell death associated with lysosomal membrane permeabilization still occurred in the presence of caspase inhibitors. PMID: 19715609
  • role in cytochrome C release and apoptosis from the nucleus PMID: 11823470

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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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