Recombinant Human Caspase-7 Protein (His Tag)

Name: Recombinant Human Caspase-7 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-0591
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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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	HGNC: 1508 OMIM: 601761 KEGG: hsa:840 STRING: 9606.ENSP00000358327 UniGene: Hs.9216
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

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
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
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
Caspase-7 regions involved in the interaction with Hsp90 co-chaperone p23 and substrate recognition. PMID: 28863261
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
Low expression of CASP7 is associated with non-small cell lung cancer. PMID: 26307684
Compared with the TT genotype, the rs10787498GT genotype was associated with an increased cervical cancer risk. PMID: 25784056
Phosphorylate caspase-7 bu Src at multiple tyrosine sites enhanced its cellular apoptotic effect. PMID: 24407236
Potentially functional polymorphisms in the CASP7 gene contribute to gastric adenocarcinoma susceptibility in an eastern Chinese population. PMID: 24040159
showed that CASP7 is downregulated in primary prostate tumors and metastatic lesions across multiple data sets PMID: 22986525
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
genetic polynorphism is associated with the risk of childhood leukemia PMID: 22548721
XIAP does not function as a NEDD8-E3 ligase for caspase-7 in vivo PMID: 22584050
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
identify serine 118 in the transactivation domain of YY1 as the site of CK2alpha phosphorylation, proximal to a caspase 7 cleavage site PMID: 22184066
Caspase-7 cleaves human TERT at residues E286 and D628 as part of the apoptosis pathway in cultured cells. PMID: 21936563
highly expressed PAK2 mediates chemotherapeutic resistance in human breast invasive ductal carcinoma by negatively regulating caspase-7 activity PMID: 21555521
The RIPK1 and CASP7 polymorphisms can be considered as possible prognostic markers for survival after curative resection in patients with colorectal cancer. PMID: 20567846
Caspase-8 and caspase-7 sequentially mediate proteolytic activation of acid sphingomyelinase in TNF-R1 receptosomes. PMID: 21157428
Single Nucleotide Polymorphisms in CASP7 is asspciated with lung cancer. PMID: 20661084
caspase 7 cleavage of ORF57 may represent a cellular function against lytic KSHV infection PMID: 20159985
Specifically interfering with caspase-7 activation may hold therapeutic value for the treatment of cancer and inflammatory ailments. PMID: 19782763
Pro-CASP7 was detected in mitochondria, cytosol, nucleus, and microsomes of U937 cells. During TPA-induced differentiation, it moved to the mitochondria. PMID: 12145703
caspase 9 by itself can activate caspase 7 in the absence of the caspase 3-dependent pathway in TNF-alpha-induced apoptosis PMID: 12804035
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
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
caspase-7 is involved earlier than other effector caspases in apoptosis PMID: 14583630
cleavage of Claspin by caspase-7 inactivates the Chk1 signaling pathway PMID: 16123041
Caspase 7 activation is a prominent feature in periodontitis-associated tissue injury. PMID: 16213496
Promoters of CASP7 genes are modulated by prohibitin. PMID: 16918502
AIF overexpression specifically resulted in the activation of caspase-7, thereby amplifying the inhibition of protein synthesis including eIF3g cleavage. PMID: 17094969
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
crystal structures show that the S2 pocket of caspase-7 can accommodate diverse residues PMID: 17697120
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
These results revealed that caspase-7 has a novel role during cell cycle progression at mitosis. PMID: 18459962
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
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
Modulation of effector caspase-7 cleavage determines response of breast and lung tumor cell lines to chemotherapy. PMID: 19241192
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
These findings suggest that genetic variants in caspase-3 and caspase-7 may play a role in endometrial cancer susceptibility. PMID: 19531679
Dissecting an allosteric switch in caspase-7 using chemical and mutational probes. PMID: 19581639
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.

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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.

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