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Caspase 12

Caspase 12 is a member of the cysteine-aspartic acid protease (caspase) family, which play a central role in apoptosis, or programmed cell death.
This enzyme is primarily expressed in the endoplasmic reticulum and is thought to be involved in the cellular response to endoplasmic reticulum stress.
Caspase 12 has been implicated in neurodegenerative diseases and may also play a role in the immune response.
Researching the functions and regulation of this important protein can provide valuable insights into cellular processes and disease pathogenesis.
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Most cited protocols related to «Caspase 12»

Immunofluorescence analysis was performed as previously described 30 (link). Briefly, NP cells or tissues attached to slides were fixed with 4% paraformaldehyde, then permeabilized with 0.2% Triton X-100 in PBS. The slides were washed in PBS and blocked with 2% bovine serum albumin (BSA) in PBS for 2 h at 37 °C, and then incubated with primary antibodies against: GRP78 (1:50), GRP94 (1:50), CHOP (1:100), caspase-3 (1:50), or caspase-12 (1:100) (Proteintech). After washed twice, the slides were subsequently treated with secondary goat anti-rabbit antibody (Boster) at 37 °C for 2 h. Nuclei were co-stained for 5 min with 0.1 g/mL DAPI (Beyotime, Nantong, China), and images were captured under a microscope (Olympus, BX53; Melville, NY, USA).
Publication 2019
Antibodies Antibodies, Anti-Idiotypic Caspase 3 Caspase 12 Cell Nucleus Cells DAPI DDIT3 protein, human Fluorescent Antibody Technique Glucose Regulated Protein 78 kDa Goat GRP94 Microscopy paraform Rabbits Serum Albumin, Bovine Tissues Triton X-100
Immunoblot and dot-blot analysis of mice and human brain tissues were performed as previously described (Lee et al., 2002 (link); Li et al., 2004b (link); Li et al., 2005 (link); Martin et al., 2006 (link); Wang et al., 2008 (link)). For semi-quantitative analysis of protein expression, the chemiluminescence signal associated with antibody binding (Pierce, Rockford, IL) was captured using the Biorad Molecular Imager ChemiDoc XRS+ System system (Biorad, Hercules, CA) or on X-ray films. The intensities of the immunoreactive bands were determined using the Quantity One software (Biorad, Hercules, CA). For dot-blot analysis, lysates were spotted directly on the nitrocellulose membrane and let it dry completely. Immunoreactivity was visualized using chemiluminescence detection (Pierce, Rockford, IL) after incubations with the appropriate horseradish peroxidaseconjugated secondary antibody, using a CCD based Biorad Molecular Imager ChemiDoc XRS+ System (Biorad, Hercules, CA) or X-ray films. The intensities of the immunoreactive bands were determined by densitometry and the Quantity One software (Biorad, Hercules, CA).
Following antibodies were used: grp78, grp94, PDI, calnexin, syntaxin 6 (Stressgen, Ann Arbor, MI); p-eIF2α, eIF2α, caspase 9, caspase 3, synaptotagmin (Cell signaling Technology, Danvers, MA); syn-1, cytochrome C (BD Transduction Laboratories, Franklin Lakes, NJ); ATF4, CHOP, p38, caspase 12, ubiquitin, cathepsin D (Santa Cruz Biotechnology, Santa Cruz, CA); VDAC, NeuN, calnexin (Abcam, Cambridge, MA); pser129-αS (Fujiwara et al., 2002 (link)); syn303 (Duda et al., 2000 (link)); βS (Oncogene, Boston MA).
Publication 2012
Antibodies ATF4 protein, human Brain Calnexin Caspase 3 Caspase 9 Caspase 12 Cathepsin D Chemiluminescence Cytochromes c' DDIT3 protein, human Densitometry Dot Immunoblotting Glucose Regulated Protein 78 kDa GRP94 Homo sapiens Horseradish Immunoblotting Immunoglobulins Mus Nitrocellulose Oncogenes Proteins Synaptotagmins Syntaxin 6 TCL1B protein, human Tissue, Membrane Tissues Ubiquitin X-Ray Film
Apoptotic and necrotic β-cells and INS-1E cells were counted in fluorescence microscopy following staining with the DNA-binding dyes propidium iodide (5 μg/ml) and Hoechst 33342 (10 μg/ml) (11 (link)). The percentage human islet cell death was determined as described (12 (link)). The apoptosis index was calculated as [(% apoptosis in ER stressor–treated cells under indicated conditions transfected with negative or target siRNA − % apoptosis in ER stressor–treated negative siRNA-transfected cells)/(100% − % apoptosis in ER stressor–treated negative siRNA-transfected cells)] × 100. Apoptosis was also assessed by the Cell Death Detection ELISAplus kit (Roche Diagnostics, Mannheim, Germany) (10 (link)). Forskolin did not modify INS-1E cell proliferation under the present experimental conditions (assessed by BrdU incorporation, data not shown).
To study cytochrome C release, cells were prepared as described in the online appendix supplementary Methods. After total protein quantification (Bio-Rad Laboratories, Munchen, Germany), equal amounts of protein were blotted using tubulin as cytoplasmic and apoptosis-inducing factor (AIF) as mitochondrial control.
Caspase 3 and 7 activation was measured with the Caspase-Glo 3/7 assay (Promega, Madison, WI) and caspase 12 activation with the CaspGlow Caspase-12 staining kit (Biovision, Mountain View, CA) (12 (link)).
Publication 2009
Apoptosis Apoptosis Inducing Factor Biological Assay Bromodeoxyuridine Caspase-7 Caspase 3 Caspase 12 Cell Death Cell Proliferation Cells Colforsin Cytochromes c' Cytoplasm Diagnosis Dyes HOE 33342 Homo sapiens Islets of Langerhans Microscopy, Fluorescence Necrosis Promega Propidium Iodide Proteins RNA, Small Interfering Tubulin
Tissues or cultured cells were rinsed in ice-cold PBS and were immediately homogenized in 5 vol Triton X-100 buffer (20 mM Hepes, pH 7.5, 150 mM NaCl, 1% Triton X-100, 10% glycerol, 1 mM EDTA, 10 mM tetrasodium pyrophosphate, 100 mM NaF, 17.5 mM β-glycerophosphate, 10 mM PMSF, 15 μg/ml aprotonin, and 6 μg/ml pepstatin A) using a motorized homogenizer. After incubating on ice for 15 min, the extracts were cleared by centrifugation at 14,000 rpm twice for 30 min each. The protein content of each extract was determined by protein assay (Bio-Rad Laboratories). The extracts (40 μg) were separated by SDS-PAGE and were transferred to nitrocellulose. The blots were incubated with primary antibody (see below), and the signal was revealed by chemiluminescence after reacting with HRP-conjugated second antibody. The following primary antibodies were used: anti–eIF-2α (1:500; Santa Cruz Biotechnology, Inc.); anti–p-eIF-2α (1:1,000; Cell Signaling Technology); anti–caspase-12 (1:500; Santa Cruz Biotechnology, Inc.); and antiactin (1:1,000; Sigma-Aldrich).
Publication 2005
Antibodies beta-glycerol phosphate Biological Assay Buffers Caspase 12 Centrifugation Chemiluminescence Cold Temperature Cultured Cells Edetic Acid Glycerin HEPES Immunoglobulins Nitrocellulose pepstatin Proteins SDS-PAGE Sodium Chloride sodium pyrophosphate Tissues Triton X-100
The liver tissue was homogenized as described previously.31 (link), 32 (link) Total liver lysates were then used to quantify GRP78, CHOP, total PERK and pPERK, total and peIF2α, ATF4, ATF6α, ATF6β, sXBP-1, TRAF2, cleaved caspase 3, caspase 12, cytochrome c, total and phospho-ERK, total and phospho-p38 MAPK, total and phospho-GSK3β, total and phospho-JNK, total and phospho-AKT, as well as total and phospho-VDAC by western blot. Cytosolic fractions were used to quantify cleaved caspase 9 and cytochrome c by western blot. Proteins were separated by SDS-PAGE and transferred into polyvinylidene fluoride membranes. Membranes were immunoblotted with antibodies directed against GRP78, CHOP, total and pPERK, total and peIF2α, ATF4, ATF6α, ATF6β, sXBP-1, β-actin (Santa Cruz Biotechnology, Santa Cruz, CA, USA) and TRAF2, cleaved caspase 3, cleaved 9 and caspase 12, cytochrome c, total and phospho-ERK, total and phospho-p38 MAPK, total and phospho-GSK3β, total and phospho-JNK and total and phospho-AKT (Cell Signalling Technology Inc., Beverly, MA, USA). The bands were visualized using an enhanced chemiluminescence kit (Bio-Rad Laboratories, Hercules, CA, USA). The values were obtained by densitometric scanning and the Quantity One software program (Bio-Rad Laboratories, Hercules, CA, USA). The scanning values for GRP78, CHOP, ATF4, ATF6α, ATF6β, sXBP-1, TRAF2, cleaved caspase 3, cleaved caspase 9, caspase 12 and cytochrome c were divided by the scanning values for β-actin, and those for phosphorylated PERK, eIF2α, GSK3β, VDAC, ERK, JNK and p38 MAPK by the total PERK, eIF2α, GSK3β, VDAC, ERK, JNK and p38 MAPK, respectively.
Publication 2010
Actins Antibodies ATF4 protein, human Caspase 3 Caspase 9 Caspase 12 Chemiluminescence Cytochromes c Cytosol DDIT3 protein, human Glucose Regulated Protein 78 kDa GSK3B protein, human Liver Mitogen-Activated Protein Kinase p38 polyvinylidene fluoride Proteins SDS-PAGE Tissue, Membrane Tissues TNF Receptor Associated Factor 2 Western Blot

Most recents protocols related to «Caspase 12»

Anti-PERK (3192), anti-p-PERK (3179S), anti-CHOP (2895), anti-caspase-4 (4450), anti-cleaved caspase-3 (Cleaved caspase-3) (9664) and anti-GAPDH (5174) antibodies were obtained from Cell Signaling (Danvers, USA). Anti-CHOP (15204-1-AP), anti-78-kDa glucose-regulated protein (GRP78) (66574-1-Ig), anti-Nuclear respiratory factor 2 (Nrf2) (16396-1-AP), anti-Keap1 (60027-1-Ig), anti-GAPDH (10494-1-AP) and anti-β-actin (20536-1-AP) were obtained from Proteintech (Chicago, USA). Anti-apelin (ab125213) and anti-caspase-12 (ab62484) were obtained from Abcam (Cambridge, UK). Anti-β-tubulin (GB11017) was obtained from Servicebio (Wuhan, China). All secondary antibodies were obtained from Abcam (Cambridge, UK). Apelin-13 (A6469, purity ≥ 95.0%) and 4-phenylbutyrate (4-PBA) (P21005) were purchased from Sigma-Aldrich (St. Louis, USA). GSK2656157 (5.04651) was purchased from EMD Millipore (Massachusetts, USA). Tunicamycin (TM) (ab120296) was purchased from Abcam (Cambridge, UK). Iohexol was purchased from GE Healthcare (Shanghai, China).
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Publication 2023
4-PBA 4-phenylbutyrate Actins Antibodies apelin-13 peptide APLN protein, human CASP4 protein, human Caspase 3 Caspase 12 DDIT3 protein, human GA-Binding Protein Transcription Factor GAPDH protein, human Glucose Regulated Protein 78 kDa GSK2656157 Iohexol KEAP1 protein, human Tubulin Tunicamycin
Anti-PERK (3192), anti-p-PERK (3179S), anti-CHOP (2895), anti-caspase-4 (4450), anti-cleaved caspase-3 (Cleaved caspase-3) (9664) and anti-GAPDH (5174) antibodies were obtained from Cell Signaling (Danvers, USA). Anti-CHOP (15204-1-AP), anti-78-kDa glucose-regulated protein (GRP78) (66574-1-Ig), anti-Nuclear respiratory factor 2 (Nrf2) (16396-1-AP), anti-Keap1 (60027-1-Ig), anti-GAPDH (10494-1-AP) and anti-β-actin (20536-1-AP) were obtained from Proteintech (Chicago, USA). Anti-apelin (ab125213) and anti-caspase-12 (ab62484) were obtained from Abcam (Cambridge, UK). Anti-β-tubulin (GB11017) was obtained from Servicebio (Wuhan, China). All secondary antibodies were obtained from Abcam (Cambridge, UK). Apelin-13 (A6469, purity ≥ 95.0%) and 4-phenylbutyrate (4-PBA) (P21005) were purchased from Sigma-Aldrich (St. Louis, USA). GSK2656157 (5.04651) was purchased from EMD Millipore (Massachusetts, USA). Tunicamycin (TM) (ab120296) was purchased from Abcam (Cambridge, UK). Iohexol was purchased from GE Healthcare (Shanghai, China).
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Publication 2023
4-PBA 4-phenylbutyrate Actins Antibodies apelin-13 peptide APLN protein, human CASP4 protein, human Caspase 3 Caspase 12 DDIT3 protein, human GA-Binding Protein Transcription Factor GAPDH protein, human Glucose Regulated Protein 78 kDa GSK2656157 Iohexol KEAP1 protein, human Tubulin Tunicamycin
For immunoprecipitation, cells were lysed with NP40 lysis buffer (50 mM Tris-HCl pH 7.5, 100 mM NaCl, 1% NP-40, 1 mM EDTA, 1 mM DTT, 10% glycerol) containing protease inhibitors. After centrifugation, the supernatants were incubated with antibody overnight and then Protein A/G agarose for 2 h at 4 °C. Immunocomplexes were washed and analyzed by Western blot. For Western blot, the proteins from lysed cells were denatured and separated with SDS-PAGE. Then, the proteins were transferred to PVDF membranes, blocked and incubated with the corresponding primary and secondary antibodies. The specific bands were analyzed by the Western blot infrared imaging system (LI-COR Biosciences). The following antibodies were used: EVA1A: A8070, ABclonal; CHOP: 2895, Cell signaling Technology (CST); IRE1: 14C10, CST; ATF6: 65880 T, CST; Actin: AC026, ABclonal; Flag: 20543-1-AP, Proteintech; Caspase 8: 4927, CST; C-Caspase 9: 9509, CST; C-Caspase 3: 9664, CST; Caspase 12: 2202, CST; C-Parp: 9548, CST; GFP: ab290, Abcam; MCL1: 94296, CST; Bak: 12105, CST; LC3: 27543,Sigma; P62: 18420-1-AP, Proteintech; BNIP3: ab10433, Abcam; TIM23: 111263-A, Proteintech; TOM20: ab56783, Abcam.
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Publication 2023
Actins activating transcription factor 6, human Antibodies Buffers Caspase-8 Caspase 3 Caspase 9 Caspase 12 Centrifugation DDIT3 protein, human Edetic Acid G-substrate Glycerin GTP-Binding Proteins Immunoglobulins Immunoprecipitation MCL1 protein, human Nonidet P-40 polyvinylidene fluoride Protease Inhibitors Proteins SDS-PAGE Sepharose Sodium Chloride Staphylococcal Protein A Tissue, Membrane Tromethamine Western Blot
Total protein was extracted using RIPA kit (AS1004, ASPEN), and protease inhibitors (AS1008, ASPEN) were added during protein extraction to prevent protein degradation. After electrophoresis, coating and sealing, the indexes to be detected were incubated with primary antibody and secondary antibody, and finally immunolabeled with enhanced chemiluminescence reagent (AS1059, ASPEN). Antibodies against caspase-3 (#9662), caspase-12 (#9671), phosphorylated PERK (p-PERK, Thr980, #3179), PERK (#3192), phosphorylated eIF2α (p-eIF2α, Ser51, #3597), eIF2α (#2103), GRP78 (#3183), CHOP (#2895), and HO-1 (#43966) were obtained from cell signing technology corporation (Massachusetts, USA). Anti-β-tubulin (#ab6046), anti-β-actin (#ab8226), and anti-Nrf-2 (#ab137550) were purchased from Abcam (Cambridge, USA). Antihistone H3 (EM1108) was purchased from ELK Biotechnology (Wuhan, China).
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Publication 2023
Actins Antibodies Caspase 3 Caspase 12 Cells Chemiluminescence DDIT3 protein, human Electrophoresis GA-Binding Protein Transcription Factor Glucose Regulated Protein 78 kDa Immunoglobulins Protease Inhibitors Proteins Proteolysis Radioimmunoprecipitation Assay Tubulin
Antibodies against the following proteins were used in this study: Bip (3177 s, Cell Signaling Technology [CST]), eIF2α (5324P, CST), Phospho-eIF2α (3398P, CST), SAPK/JNK (9252S, CST), Phospho-SAPK/JNK (9255S, CST), Caspase-12(2202S, CST), Cleaved Caspase-3 (9661S, CST), Cleaved PARP (9541S, CST), Phospho-EGFR and EGFR (11862S, CST), GAPDH (60,004–1-Ig, Proteintech). PE anti-human EGFR Antibody (352,904, Biolegend). The kinase inhibitor library was purchased from Shanghai Topscience Co., Ltd (Shanghai, China). Afatinib (HY-10261) were purchased from MCE.
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Publication 2023
Afatinib Antibodies Antibodies, Anti-Idiotypic CASP3 protein, human Caspase 12 cDNA Library EGFR protein, human GAPDH protein, human Homo sapiens Phosphotransferases Proteins

Top products related to «Caspase 12»

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Caspase-12 is a laboratory tool used to detect and quantify the presence of the Caspase-12 protein in biological samples. Caspase-12 is an enzyme involved in the process of apoptosis, or programmed cell death. This product can be utilized in various research applications that require the measurement or analysis of Caspase-12 levels.
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Caspase-12 is an enzyme involved in the process of programmed cell death, known as apoptosis. It plays a role in the activation of the apoptotic pathway in response to certain cellular stresses. Caspase-12 is primarily found in the endoplasmic reticulum and is considered a key player in the endoplasmic reticulum stress-induced apoptotic pathway.
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Anti-caspase-12 is a primary antibody that specifically binds to and detects caspase-12, a member of the caspase family of proteases. Caspase-12 is involved in apoptosis, or programmed cell death, and is implicated in various cellular processes.
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Ab62484 is a rabbit polyclonal antibody that recognizes the CD44 antigen. CD44 is a cell-surface glycoprotein involved in cell-cell interactions, cell adhesion and migration.
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Cleaved caspase-3 is an antibody that detects the activated form of caspase-3 protein. Caspase-3 is a key enzyme involved in the execution phase of apoptosis, or programmed cell death. The cleaved caspase-3 antibody specifically recognizes the active, cleaved form of the enzyme and can be used to monitor and quantify apoptosis in experimental systems.
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Bcl-2 is a protein that plays a key role in regulating apoptosis, or programmed cell death. It functions as an anti-apoptotic protein, helping to prevent cell death by inhibiting the activity of pro-apoptotic proteins.
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Caspase-3 is a key enzyme involved in the execution phase of cell apoptosis (programmed cell death). It plays a central role in the apoptotic pathway by cleaving various cellular substrates, leading to the characteristic morphological and biochemical changes associated with apoptosis.
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GRP78 is a molecular chaperone protein that plays a crucial role in the endoplasmic reticulum (ER) of eukaryotic cells. It is involved in the folding and assembly of proteins within the ER, helping to maintain ER homeostasis and prevent the accumulation of misfolded proteins.

More about "Caspase 12"

Caspase-12, a member of the cysteine-aspartic acid protease (caspase) family, plays a central role in apoptosis, or programmed cell death.
This enzyme is primarily expressed in the endoplasmic reticulum (ER) and is thought to be involved in the cellular response to ER stress.
Caspase-12 has been implicated in neurodegenerative diseases and may also play a role in the immune response.
Researching the functions and regulation of this important protein can provide valuable insights into cellular processes and disease pathogenesis.
Caspase-12 is a key regulator of the apoptotic pathway, and its dysregulation has been linked to a variety of disease states, including Alzheimer's disease, Parkinson's disease, and ischemic brain injury.
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Unlock access to protocols from literature, pre-prints, and patents, and leverage intelligent comparisons to identify the best strategies and products for your research.
Discover the power of PubCompare.ai's cutting-edge tools and unleash your potential in understanding the role of Caspase-12 in cellular processes and disease pathogenesis.
Delve deeper into the world of Caspase-12 by exploring related topics such as Anti-caspase-12, PVDF membranes, Ab62484, Cleaved caspase-3, Bcl-2, FBS, and Caspase-3.
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