Recombinant Human Caspase-3 (CASP3) Protein (His)

Name: Recombinant Human Caspase-3 (CASP3) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07437P
Price: 418.4 USD
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Caspase-3 (CASP3) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P42574
Target Symbol	CASP3
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	SGISLDNSYKMDYPEMGLCIIINNKNFHKSTGMTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELMRDVSKEDHSKRSSFVCVLLSHGEEGIIFGTNGPVDLKKITNFFRGDRCRSLTGKPKLFIIQACRGTELDCGIETDSGVDDDMACHKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCAMLKQYADKLEFMHILTRVNRKVATEFESFSFDATFHAKKQIPCIVSMLTKELYFYH
Expression Range	29-277aa
Protein Length	Partial
Mol. Weight	32.6 kDa
Research Area	Apoptosis
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. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-\|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage. Cleaves and inhibits serine/threonine-protein kinase AKT1 in response to oxidative stress. Cleaves XRCC4 and phospholipid scramblase proteins XKR4, XKR8 and XKR9, leading to promote phosphatidylserine exposure on apoptotic cell surface.
Subcellular Location	Cytoplasm.
Protein Families	Peptidase C14A family
Database References	HGNC: 1504 OMIM: 600636 KEGG: hsa:836 STRING: 9606.ENSP00000311032 UniGene: Hs.141125
Tissue Specificity	Highly expressed in lung, spleen, heart, liver and kidney. Moderate levels in brain and skeletal muscle, and low in testis. Also found in many cell lines, highest expression in cells of the immune system.

Gene Functions References

The optimal melatonin concentration (3 mM) significantly decreased the intracellular reactive oxygen species levels, caspase-3 activity and the percentage of both dead and apoptotic-like sperm cells and increased the vitality, progressive motility and total motility and AKT phosphorylation compared with the control group. PMID: 29196809
As phosphorylation of the serine residue of this tetra-peptide could yield a motif similar to the caspase-3 binding recognition sequence DEVD/E, the region from a representative PE_PGRS protein (PE_PGRS45) was docked to human caspase-3. PMID: 30207307
within the modified loop, Ser(150) evolved with the apoptotic caspases, whereas Thr(152) is a more recent evolutionary event in mammalian caspase-3. Substitutions at Ser(150) result in a pH-dependent decrease in dimer stability, and localized changes in the modified loop propagate to the active site of the same protomer through a connecting surface helix. PMID: 29414778
Caspase-3 and -8 and annexin V may serve as diagnostic markers in Ovarian cancer , also explained that the decrement in control of the S phase in the cell cycle may considered one of the significant factors in the development of ovarian tumors PMID: 30197345
Study seems to indicate a direct connection between SNPS in CASP3 gene and prostate cancer (PCa) risk in the Galician population after stratification. Also, individual susceptibility to PCa becomes more evident when assessing gene-environment interactions. Alleles G and T, in rs1049216 and rs2705897 respectively, are related to an increased risk of PCa in smokers overweight individuals. PMID: 30176316
Low CASP3 expression is associated with Colorectal Cancer. PMID: 29801534
overexpressed miR-337-3p and miR-17-5p/miR-132-3p/-212-3p can regulate executioner caspases-3 and -7, respectively. PMID: 29659498
Caspase-8 and Caspase-3 expressions in tumor tissues are novel candidate prognostic markers for colorectal cancer patients PMID: 29355114
The new findings of this work were that an association between serum caspase-3 concentrations during the first week, apoptosis degree, sepsis severity, and sepsis mortality exists. PMID: 29119350
our data demonstrate that WT1 protein undergoes proteolytic processing by caspase-3 in chemotherapeutic drugs-induced apoptosis. This processing is associated with a reduction of WT1 protein. PMID: 28395566
Increased baseline gene expressions of RUNX2, p21 and caspase 3 in the peripheral blood might predict better responses to methotrexate therapy. PMID: 28741869
The caspase-3-mediated movement of PUS10 and the release of mitochondrial contents enhancing caspase-3 activity creates a feedback amplification loop for caspase-3 action. Therefore, any defect in the movement or interactions of PUS10 would reduce the TRAIL sensitivity of tumor cells. PMID: 28981101
a prolonged anti-apoptotic intervention targeting caspase-3 should be considered with caution due to the potential adverse effects in mitochondria dynamics resulting from a novel potential functional role of procaspase-3 in mitochondrial biogenesis via regulating the expression of mitochondrial biogenesis activators. PMID: 28585712
knockdown of RPA1 suppressed cell clone formation, induced cell cycle arrest at the G1 phase and promoted cell apoptosis by regulating the protein level of Caspase 3 PMID: 29601890
The phosphorylation level of p38 was upregulated by MA1 treatment, and the inhibitor of p38, SB203580, attenuated the MA1-induced p38 phosphorylation as well as caspase3 and PARP activation. These results indicate that MA1 treatment alters invasive and oncogenic phenotypes of human colorectal cancer cells through the stimulation of the p38 signaling pathway PMID: 28713983
Overexpression of full-length AIFM1 suppresses proliferation and induces apoptosis of HepG2 and Hep3B cells. Caspase 3 and DRAM are involved in full-length AIFM1-induced apoptosis in HepG2 and Hep3B cells. PMID: 29501488
Here the authors show that sublethal activation of Caspase-3 plays an essential, facilitative role in Myc-induced genomic instability and oncogenic transformation. PMID: 28691902
we show that ABT-737 and TQ activate PKA in a caspase-3-dependent manner, which correlates with platelet inhibition and apoptosis and therefore potentially contributes to the bleeding risk in chemotherapy patients PMID: 28661475
MiR-221 might represent a candidate biomarker of likelihood of response to Sorafenib in HCC patients to be tested in future studies. Caspase-3 modulation by miR-221 participates to Sorafenib resistance PMID: 28096271
In the present study, galangin was found to suppress laryngeal cancer cell proliferation. Also, flow cytometry, immunohistochemical and western blot analysis indicated that cell apoptosis was induced for galangin administration, promoting caspase-3 expression through regulating PI3K/AKT/NF-kappaB. PMID: 28677816
1,4-BQ evidently induced mitochondria-mediated apoptosis and increased pro-apoptotic genes (Caspase-9 and Caspase-3) expression in a dose-dependent manner. PMID: 27425441
GGN played a tumor-promoting role in bladder cancer through regulation of NFkappaB/caspase3-mediated apoptosis signaling. PMID: 29412153
Serum caspase-3 concentrations are increased in ICH patients as well as correlate with clinical severity and prognosis PMID: 28526532
High caspase-3 expression is significantly associated with adverse breast cancer-specific survival. High caspase-3 expression was significantly associated with HER2 positive tumours.The prognostic significance of caspase-3 expression in different breast cancer phenotypes was also examined.There was a significant association in receptor positive (ER, PR or HER2) and non-basal like subgroups. PMID: 27798717
UV phototoxicity-induced pre-elafin inside keratinocytes prior to cornified envelope formation could be involved in UV-induced keratinocyte apoptosis via cystatin-A downregulation resulting in pro-caspase-3 activation. PMID: 28119996
Overexpression of CASP3 is associated with Breast Cancer. PMID: 26932709
Results show that CASP3 expression is regulated by HOXC13 which represses its transcription by directly targeting its promotor region. PMID: 29168599
Data show that selective histone deacetylase 6 (HDAC6) inhibition or knockdown of HDAC6 expression was able to prevent caspase 3 activation in lung endothelial cells and maintain lung endothelial cell-cell junctions. PMID: 27419634
Genetic variations in the CASP3 gene and the joint effects of working time and CASP3 polymorphisms may modify the risk of developing noise-induced hearing loss PMID: 28738811
Data indicate that through upregulating the expression of caspase-3, the TT genotype of caspase-3 rs1049216 can be associated with not only the risk of cervical cancer but also the progression of this cancer. PMID: 28114230
In conclusion, our findings firstly revealed that GSDME switches chemotherapy drug-induced caspase-3 dependent apoptosis into pyroptosis in gastric cancer cells. PMID: 29183726
Everolimus also induced higher levels of caspase-3/-7 activation in GR over GS cells, and everolimus-mediated mTOR inhibition lead to G2 arrest in GR cells but G1 arrest in GS cells. PMID: 28165150
Results Grb7 and Hax1 may colocalize partially to mitochondria in EGF-treated SKBR3 cells and their interaction can affect Caspase3 cleavage of Hax1 supporting an inhibitory role of Grb7 on Casp3 cleavage function by interfering with the association of Casp3 and Hax1. PMID: 26869103
caspase-3 inhibitors also suppressed the attenuation of cell adhesion and phosphorylation of p38 MAPK by EGF-F9. Our data indicated that EGF-F9 activated signals for apoptosis and induced de-adhesion in a caspase-3 dependent manner. PMID: 27129300
Data indicate that E-cadherin and caspase-3 were targets of miR-421, which was up-regulated by HIF-1alpha. PMID: 27016414
findings suggest that caspase-3 activation can trigger necrosis by cleaving GSDME and offer new insights into cancer chemotherapy PMID: 28459430
These results demonstrate that hyperglycemic-induced endothelial microparticles increase endothelial cell active caspase-3. This apoptotic effect may be mediated, at least in part, by a reduction in miR-Let-7a expression. PMID: 28942148
Epigallocatechin-3-Gallate protects against Ang II-induced HUVEC apoptosis by decreasing oxidative stress and ameliorating mitochondrial injury via activation of Nrf2/casp3 signaling pathway. PMID: 28942440
Prolonged treatment of human PMNs or mice bone marrow derived neutrophils (BMDN) with nitric oxide led to enhanced reactive oxygen species generation, caspase-8/caspase-3 cleavage, reduced mitochondrial membrane potential and finally cellular apoptosis. PMID: 27584786
cleaved caspase-3 and caspase-3/8/9 could be biomarkers for tumorigenesis in oral tongue squamous cell carcinoma patients. PMID: 28700659
TT genotype of CASP3 rs4643701 polymorphisms showed risk in CAD. CASP3 rs4647601 creates a new exon splicing enhancer. PMID: 28633917
These findings shed some light on how a tumor cell may avert apoptosis using Hsp60 and point to the anti-cancer potential of drugs, such as CubipyOXA, which interfere with Hsp60/pC3 complex formation, and thus allow the apoptotic cascade to proceed. PMID: 28212901
Here the authors show that in macrophages SipA induces increased caspase-3 activation early in infection. PMID: 28630067
SASH1 is cleaved by caspase-3 following Ultraviolet C-induced apoptosis. PMID: 27831555
Caspase 3 activation in dying glioma cells unfavorably supported post-irradiation angiogenesis. PMID: 27826040
CASP3 is a direct target of specific Epstein-Barr virus BART miRNAs. PMID: 27565721
Data suggest that EV71 infection in enterocytes does not inhibit phosphorylation of STAT1/2 induced by IFN-beta, but p-STAT1/2 transport into the nucleus is significantly blocked; EV71 infection in enterocytes down-regulates expression of KPNA1 and induces degradation of cellular KPNA1 via caspase-3. [EV17 = Enterovirus 71] PMID: 28455446
our results identified that mammalian sterile 20-like kinase 1 is a novel downstream target of pyruvate kinase M2, and knockdown of pyruvate kinase M2 contributes apoptosis via promoting nuclear translocation of mammalian sterile 20-like kinase 1 by enhancing Caspase-3-dependent cleavage. PMID: 28656802
High levels of FADD and caspase-8, but not caspase-3, were associated with increased incidence of coronary events in subjects from the general population. PMID: 28302628
Interestingly, EspC-induced apoptosis was triggered through a dual mechanism involving both independent and dependent functions of its EspC serine protease motif, the direct cleavage of procaspase-3 being dependent on this motif. PMID: 27329750

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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.

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