Recombinant Human Caspase-7 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0591

Recombinant Human Caspase-7 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0591
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Product Overview

Tag His
Host Species Human
Accession P55210
Synonym CASP-7, CMH-1, ICE-LAP3, LICE2, MCH3
Background Caspase 7, also known as caspase-7 and MCH3, belongs to the cysteine-aspartic acid protease (caspase) family. Caspases play a role in the signal transduction pathways of apoptosis, necrosis and inflammation. There are two major classes of caspases: initiators and effectors. The initiator isoforms (caspases-1,-4,-5,-8,-9,-1,-11,-12) are activated by, and interact with, upstream adaptor molecules through protein-protein interaction domains known as CARD and DED. Effector caspases (-3,-6,-7) are responsible for cleaving downstream substrates and are sometimes referred to as the executioner caspases. Caspase 7 exists in lung, skeletal muscle, liver, kidney, spleen and heart, and moderately in testis. Caspase 7 cannot be detected in the brain. Caspase 7 functions in the activation cascade of caspases responsible for apoptosis execution. It cleaves and activates sterol regulatory element binding proteins (SREBPs). It proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp- -Gly-217' bond. Overexpression promotes programmed cell death.
Description A DNA sequence encoding the human CASP7 (P55210-1) (Met 1-Gln 303) was fused with a His tag at the C-terminus.
Source E.coli
Predicted N Terminal Ala 24 & Ala 207
AA Sequence Met 1-Gln 303
Molecular Weight The full length of recombinant human CASP7 comprises 313 a.a. and has a calculated molecular mass of 35KDa. As a result of proteolytic cleavage, the apparent molecular mass of the protein is approximately 20 & 11 kDa ,corresponding to the N-reminal P20 subunit and the C-teminal p11 subunit respectively in SDS-PAGE under reducing conditions.
Purity >90% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile 20mM HEPES, 100mM NaCl, 1mM EDTA, 0.10% Sucrose, 0.1% chaps, pH 7.5.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Overexpression promotes programmed cell death. Cleaves phospholipid scramblase proteins XKR4, XKR8 and XKR9.; Lacks enzymatic activity.
Subcellular Location Cytoplasm.
Protein Families Peptidase C14A family
Database References
Tissue Specificity Highly expressed in lung, skeletal muscle, liver, kidney, spleen and heart, and moderately in testis. No expression in the brain.

Gene Functions References

  1. Pyrin signaling is dispensable for Clostridium difficile infection (CDI) associated intestinal epithelial cells death and for in vivo pathogenesis; C. difficile enterotoxins induce activation of executioner caspases 3/7 via the intrinsic apoptosis pathway indicating that caspase-3/7-mediated intestinal epithelial cells apoptosis is critical for in vivo host defense during early stages of CDI. PMID: 30451870
  2. CASP8: rs1045494 (C > T), PIK3R1: rs3756668 (A > G) and CASP7: rs4353229 (T > C), were associated with longer overall survival in limited disease-small cell lung cancer patients after chemoradiotherapy PMID: 26988918
  3. Results show that caspase-7 is phosphorylated by PAK2 at S239 which inhibits its activity by two divergent mechanisms prior to and following caspase activation: initial phosphorylation allosterically slows activation by upstream initiator caspases by impeding cleavage at the intersubunit linker and a second phosphorylation site directly blocks substrate binding. PMID: 27889207
  4. Caspase-7 regions involved in the interaction with Hsp90 co-chaperone p23 and substrate recognition. PMID: 28863261
  5. Study provides evidence that a loss-of-function variant rs10553596 in CASP7 associates with significantly reduced Alzheimer's disease incidence in elder populations. PMID: 27358062
  6. Low expression of CASP7 is associated with non-small cell lung cancer. PMID: 26307684
  7. Compared with the TT genotype, the rs10787498GT genotype was associated with an increased cervical cancer risk. PMID: 25784056
  8. Phosphorylate caspase-7 bu Src at multiple tyrosine sites enhanced its cellular apoptotic effect. PMID: 24407236
  9. Potentially functional polymorphisms in the CASP7 gene contribute to gastric adenocarcinoma susceptibility in an eastern Chinese population. PMID: 24040159
  10. showed that CASP7 is downregulated in primary prostate tumors and metastatic lesions across multiple data sets PMID: 22986525
  11. Genetic variations of CASP7 may modulate overall survival and progress-free survival of patients with advanced non-small cell lung cancer treated with platinum-based chemotherapy. PMID: 22441531
  12. genetic polynorphism is associated with the risk of childhood leukemia PMID: 22548721
  13. XIAP does not function as a NEDD8-E3 ligase for caspase-7 in vivo PMID: 22584050
  14. Cellular expression of caspase-7 lacking the critical lysine residues resulted in less-efficient PARP and p23 cleavage compared with cells expressing the wild-type peptidase. PMID: 22451931
  15. identify serine 118 in the transactivation domain of YY1 as the site of CK2alpha phosphorylation, proximal to a caspase 7 cleavage site PMID: 22184066
  16. Caspase-7 cleaves human TERT at residues E286 and D628 as part of the apoptosis pathway in cultured cells. PMID: 21936563
  17. highly expressed PAK2 mediates chemotherapeutic resistance in human breast invasive ductal carcinoma by negatively regulating caspase-7 activity PMID: 21555521
  18. The RIPK1 and CASP7 polymorphisms can be considered as possible prognostic markers for survival after curative resection in patients with colorectal cancer. PMID: 20567846
  19. Caspase-8 and caspase-7 sequentially mediate proteolytic activation of acid sphingomyelinase in TNF-R1 receptosomes. PMID: 21157428
  20. Single Nucleotide Polymorphisms in CASP7 is asspciated with lung cancer. PMID: 20661084
  21. caspase 7 cleavage of ORF57 may represent a cellular function against lytic KSHV infection PMID: 20159985
  22. Specifically interfering with caspase-7 activation may hold therapeutic value for the treatment of cancer and inflammatory ailments. PMID: 19782763
  23. Pro-CASP7 was detected in mitochondria, cytosol, nucleus, and microsomes of U937 cells. During TPA-induced differentiation, it moved to the mitochondria. PMID: 12145703
  24. caspase 9 by itself can activate caspase 7 in the absence of the caspase 3-dependent pathway in TNF-alpha-induced apoptosis PMID: 12804035
  25. the N-peptide of caspase 7 serves to physically sequester the caspase-7 zymogen in a cytosolic location that prevents access by upstream activators PMID: 12824163
  26. our data suggest that the inactivating mutations of the CASPASE-7 gene might lead to the loss of its apoptotic function and contribute to the pathogenesis of some human solid cancers PMID: 12970753
  27. caspase-7 is involved earlier than other effector caspases in apoptosis PMID: 14583630
  28. cleavage of Claspin by caspase-7 inactivates the Chk1 signaling pathway PMID: 16123041
  29. Caspase 7 activation is a prominent feature in periodontitis-associated tissue injury. PMID: 16213496
  30. Promoters of CASP7 genes are modulated by prohibitin. PMID: 16918502
  31. AIF overexpression specifically resulted in the activation of caspase-7, thereby amplifying the inhibition of protein synthesis including eIF3g cleavage. PMID: 17094969
  32. observation indicates that neither CASP7 nor CASP8 mutation may occur in gastrointestinal lymphomas, and suggests that neither of them may play an important role in the development of gastrointestinal lymphomas PMID: 17532763
  33. crystal structures show that the S2 pocket of caspase-7 can accommodate diverse residues PMID: 17697120
  34. A reticulon protein is identified as one out of a selected number of caspase targets during apoptosis and as a novel substrate for Cdk1 and 2.[ PMID: 18072206
  35. These results revealed that caspase-7 has a novel role during cell cycle progression at mitosis. PMID: 18459962
  36. Valosin-containing protein was cleaved by both capspase-7 and caspase-3 in vitro and during apoptosis; degradomic approach to caspase-7 provides new candidate substrates and valuable clues to the specific function of caspase-7 in apoptosis PMID: 18596415
  37. CASP7 (caspase 7) rs2227309 SNP was not associated with rheuatoid arthritis (RA) in a European Caucasian population. CASP7 isoforms alpha and beta could have an involvement in the apoptosis process in RA PMID: 18785314
  38. Modulation of effector caspase-7 cleavage determines response of breast and lung tumor cell lines to chemotherapy. PMID: 19241192
  39. Results show that caspase 7, as an SREBP-1/2 target, can be induced under mevalonate-restricting conditions, which might help overcome its shortage. PMID: 19323650
  40. These findings suggest that genetic variants in caspase-3 and caspase-7 may play a role in endometrial cancer susceptibility. PMID: 19531679
  41. Dissecting an allosteric switch in caspase-7 using chemical and mutational probes. PMID: 19581639
  42. there is an an association between HCV core and HAX-1, which promotes 5-FU mediated p53-dependent caspase-7 activation and hepatocyte growth inhibition PMID: 19605487


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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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