Recombinant Human Caspase-2 (CASP2)

Code CSB-EP004547HU
MSDS
Size $224
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP004547HU 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 CSB-EP004547HU could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) CASP2.
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Product Details

Purity
Greater than 90% as determined by SDS-PAGE.
Target Names
CASP2
Uniprot No.
Research Area
Cancer
Alternative Names
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)
Source
E.coli
Expression Region
2-452aa
Target Protein Sequence
AAPSAGSWSTFQHKELMAADRGRRILGVCGMHPHHQETLKKNRVVLAKQLLLSELLEHLLEKDIITLEMRELIQAKVGSFSQNVELLNLLPKRGPQAFDAFCEALRETKQGHLEDMLLTTLSGLQHVLPPLSCDYDLSLPFPVCESCPLYKKLRLSTDTVEHSLDNKDGPVCLQVKPCTPEFYQTHFQLAYRLQSRPRGLALVLSNVHFTGEKELEFRSGGDVDHSTLVTLFKLLGYDVHVLCDQTAQEMQEKLQNFAQLPAHRVTDSCIVALLSHGVEGAIYGVDGKLLQLQEVFQLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQDGKNHAGSPGCEESDAGKEKLPKMRLPTRSDMICGYACLKGTAAMRNTKRGSWYIEALAQVFSERACDMHVADMLVKVNALIKDREGYAPGTEFHRCKEMSEYCSTLCRHLYLFPGHPPT
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
66.6kDa
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 6xHis-SUMO-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
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.
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.

Customer Reviews and Q&A

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Target Background

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.
Gene References into Functions
  1. these data identify a novel caspase-2-interacting factor, FAN, and expand the role for the enzyme in seemingly non-apoptotic cellular mechanisms. PMID: 29621545
  2. Results suggest that TG-induced macrophage cell death is mediated via the caspase-2. PMID: 28768565
  3. 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
  4. 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
  5. There results support a special role for miR-149 in malignant glioma by targeting Caspase-2 PMID: 27049919
  6. 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
  7. This study shows that human procaspase-2 interaction with 14-3-3 zeta is governed by phosphorylation at both S139 and S164. PMID: 28943433
  8. NPM1-dependent nucleolar PIDDosome is a key initiator of the caspase-2 activation cascade. PMID: 28432080
  9. Sensitization of colon carcinoma cells to radiation-induced cell death and DNA-damage by HuR knockdown critically depends on caspase-2. PMID: 28219770
  10. 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
  11. CASP2 down-regulation had a reverse relationship with miR-383 down-regulation in regulating epithelial ovarian cancer development. PMID: 27567588
  12. 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
  13. These findings indicate that miR-125a-5p decreases after HOTAIR knockdown to promote cancer cell apoptosis by releasing caspase 2. PMID: 26962687
  14. these studies elucidate a Caspase-2-p53 signaling network that impacts lung tumorigenesis and chemotherapy response in vivo. PMID: 25301067
  15. We have also demonstrated that these correlations are tissue specific being reduced (CASP9 and CASP10) or different (CASP2) in the liver PMID: 25330190
  16. the initiator caspase-2 is required for robust death of ovarian cancer cells induced by FASN inhibitors PMID: 25151963
  17. HuR sensitizes adenocarcinoma cells to the intrinsic apoptotic pathway by upregulating the translation of caspase-2. PMID: 25010987
  18. Authors have demonstrated in vitro and in vivo that loss of function of caspase-2 allows to escape oncogenic stress induced senescence. PMID: 25114039
  19. Data strongly argue against a critical role for caspase-2 in ER-stress-induced apoptosis. PMID: 24292555
  20. axon regeneration promoted by suppression of CASP2 and CASP6 is CNTF-dependent and mediated through the JAK/STAT signalling pathway PMID: 24727569
  21. Our results reveal a novel mechanism of caspase-2 pre-mRNA splicing. PMID: 24321384
  22. TRIM16 can promote apoptosis by directly modulating caspase-2 activity in cancer cells. PMID: 23404198
  23. The role of caspase-2 isoforms in the progression of breast cancer may considerably differ between pre- and post-chemotherapy patients. PMID: 23469978
  24. MiR-708 may act as an oncogene and induce the carcinogenicity of bladder cancer by down-regulating Caspase-2 level. PMID: 23568547
  25. caspase-2 has a role as an initiator caspase in lipoapoptosis PMID: 23553630
  26. Data indicate induction of caspase-2 by sorting nexin 5 (SNX5) in papillary thyroid carcinoma PMID: 22486813
  27. 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
  28. 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
  29. These results revealed a thus far unknown, obligatory role for caspase-2 as an initiator caspase during pore-forming toxins -mediated apoptosis. PMID: 22531785
  30. 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
  31. Tumor-suppressing function of caspase-2 requires catalytic site Cys-320 and site Ser-139 in mice. PMID: 22396545
  32. 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
  33. 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
  34. Findings suggest that XPC enhances DNA damage-induced apoptosis through inhibition of caspase-2 (casp-2S) transcription. PMID: 22174370
  35. Studies indicate that DNA damage may trigger caspase 2 activation. PMID: 22077397
  36. somatic mutation of caspase-2 is rare in gastric and colorectal carcinomas. PMID: 21940110
  37. ras-induced down-regulation of caspase-2 represents a novel mechanism by which oncogenic Ras protects malignant intestinal epithelial cells from anoikis PMID: 21903589
  38. Structural and enzymatic insights into caspase-2 protein substrate recognition and catalysis. PMID: 21828056
  39. 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
  40. analyzed cancer tissues from acute leukemias, breast cancers, lung cancers, and liver cancers for the detection of caspase-2 somatic mutations PMID: 21332795
  41. The changes of caspase-2 and caspase-5 activities could be indicative of their involvement in the cervical malignancy mechanisms. PMID: 21051981
  42. Activation of caspase-9, but not caspase-2 or caspase-8, is essential for heat-induced apoptosis in Jurkat cells. PMID: 20978129
  43. 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
  44. caspase-2 activation is commonly associated with induction of IFN-beta-induced apoptosis in IFN-beta-sensitive melanoma cells PMID: 20187765
  45. 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
  46. The expressions of PIDD and RAIDD are upregulated during tumour progression in renal cell carcinomas. PMID: 20208132
  47. caspase 2 functions as an endogenous inhibitor of NFkappaB-dependent cell survival and this mechanism may contribute to tumor suppression in humans. PMID: 19935698
  48. Data show that the N-t-boc-Daidzein induced apoptosis is characterized by caspase activation, XIAP and AKT degradation. PMID: 19738422
  49. 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
  50. role in cytochrome C release and apoptosis from the nucleus PMID: 11823470

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Protein Families
Peptidase C14A family
Tissue Specificity
Expressed at higher levels in the embryonic lung, liver and kidney than in the heart and brain. In adults, higher level expression is seen in the placenta, lung, kidney, and pancreas than in the heart, brain, liver and skeletal muscle.
Database Links

HGNC: 1503

OMIM: 600639

KEGG: hsa:835

STRING: 9606.ENSP00000312664

UniGene: Hs.368982

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