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Rabbit anti caspase 1 p10

Manufactured by Santa Cruz Biotechnology
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Rabbit anti-caspase-1 p10 is a primary antibody that recognizes the p10 subunit of activated caspase-1. Caspase-1 is an enzyme involved in the processing and activation of inflammatory cytokines.

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Lab products found in correlation

Protease inhibitor cocktail, by Roche (2 mentions) Anti mouse il 1β, by R&D Systems (2 mentions) Goat anti rabbit igg hrp, by Merck Group (2 mentions) Rabbit anti actin antibody, by Santa Cruz Biotechnology (1 mentions) Image lab 3, by Bio-Rad (1 mentions) Enhanced chemi luminescence (ecl), by Thermo Fisher Scientific (1 mentions) Dc protein assay, by Bio-Rad (1 mentions) Pefabloc, by Roche (1 mentions) Rabbit anti eif2α, by Cell Signaling Technology (1 mentions) Rabbit anti ire1, by Cell Signaling Technology (1 mentions) Atp a6419, by Merck Group (1 mentions) Rabbit anti p erk, by Cell Signaling Technology (1 mentions) Rabbit anti asc, by Santa Cruz Biotechnology (1 mentions) Txnip, by Santa Cruz Biotechnology (1 mentions) Mouse anti xbp1s, by BioLegend (1 mentions) Rabbit anti nf κb p65 d14e12, by Cell Signaling Technology (1 mentions) Nigericin tlrl nig, by InvivoGen (1 mentions) Rabbit anti caspase 1, by Santa Cruz Biotechnology (1 mentions) Goat anti rabbit antibodies, by Jackson ImmunoResearch (1 mentions) Rabbit anti actin, by Merck Group (1 mentions)

Close spelling variants of this product

Caspase-1 (137 citations) Anti-caspase-1 (60 citations) Rabbit anti-caspase-1 (14 citations) Caspase-1 p10 (11 citations) Anti-caspase-1 p10 (9 citations) Rabbit anti-TM (2 citations) Rabbit anti-mouse caspase-1 (p10) clone M-20 (2 citations)

7 protocols using rabbit anti caspase 1 p10

1

SDS-PAGE Analysis of IL-1β and Caspase-1

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An equal amount of whole lung tissue were lysed in 2× Laemli buffer and separated in 14% Tris/glicine SDS gel, transferred to a nitrocellulose membrane, probed with rabbit anti-mouse IL-1β (Biolegend) or rabbit anti-caspase-1-p10 (Santa Cruz). Goat anti-rabbit IgG-HRP (Sigma-Aldrich) was used as secondary antibodies. Normalization was performed on rabbit anti-actin antibody (Santa Cruz) and quantification was obtained by densitometric image analysis using Image Lab 3.1.1 software (Bio-Rad) as previously described [47] (link).
Moretti S., Bozza S., Oikonomou V., Renga G., Casagrande A., Iannitti R.G., Puccetti M., Garlanda C., Kim S., Li S., van de Veerdonk F.L., Dinarello C.A, & Romani L. (2014). IL-37 Inhibits Inflammasome Activation and Disease Severity in Murine Aspergillosis. PLoS Pathogens, 10(11), e1004462.
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2

Characterization of BMDM Inflammatory Response

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BMDM cells were plated in 12-well microculture plates (at 3 × 106 cells/well), stimulated with LPS during 3 h and were washed and stimulated with particles during 6 h. Supernatants were collected and stored at −20 °C for further analysis. BMDMs were washed with cold PBS and scraped in lysis buffer solution (150 mM NaCl, 10 mM Tris pH 8, 1 mM EDTA, 0.2% SDS and 1% Nonidet P-40) supplemented with a protease inhibitor cocktail (1%) and pefabloc (0.1 mg/ml) (Roche Applied Science, Meylan, France). Lysis extracts and supernatants were collected and protein content was measured (DC protein assay, Bio-Rad, Munich, Germany). Proteins were denatured by boiling (95 °C, 5 min), separated by SDS–PAGE and transferred to nitrocellulose membranes. The membranes were immunoblotted with a primary goat anti-IL-1β antibody (Sigma Aldrich) or rabbit anti-caspase-1 p10 (Santa Cruz Biotechnology) and proteins were detected with appropriate secondary antibody followed by enhanced chemiluminescence (ECL, Fisher, Illkirch, France).
Baron L., Gombault A., Fanny M., Villeret B., Savigny F., Guillou N., Panek C., Le Bert M., Lagente V., Rassendren F., Riteau N, & Couillin I. (2015). The NLRP3 inflammasome is activated by nanoparticles through ATP, ADP and adenosine. Cell Death & Disease, 6(2), e1629-.
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3

Molecular Mechanisms of Endoplasmic Reticulum Stress

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Primary antibodies used were as follows: mouse anti-XBP1s (Biolegend, 647502), rabbit anti-IRE1 (Cell Signaling, 3294), rabbit anti-PERK (Cell Signaling Technology, 3192), rabbit anti-eIF2α (Cell Signaling Technology, 5324), rabbit anti-p(S51)-eIF2α (Cell Signaling Technology, 3398), mouse anti-ATF6 (CosmoBio, BAM-73-500-EX), rabbit anti-NLRP3 D2P5E (Cell signaling technology, 13158), rabbit anti-NF-κB p65 (D14E12) (Cell signaling technology, 8242), mouse anti-IL-1β (R&D Systems, MAB601), rabbit anti-ASC (Santa Cruz, sc-22514-R), rabbit anti-caspase 1 (Santa Cruz, sc-622), rabbit anti-caspase-1 p10 (Santa Cruz, sc-515), TXNIP (Santa Cruz, sc-166234), and rabbit anti-Actin (Sigma, A2066). Secondary antibodies were horseradish peroxidase-tagged goat anti-mouse (Jackson Laboratories, 115-035-003) and goat anti-rabbit antibodies (Jackson Laboratories, 111-035-003). Tunicamycin (T7765), Phorbol 12-myristate 13-acetate (PMA) (P8139), LPS (L2630), and ATP (A6419) were purchased from Sigma-Aldrich while nigericin (tlrl-nig) was obtained from Invivogen. IRE1 inhibitor MKC8866 was provided by Fosun Orinove.
Talty A., Deegan S., Ljujic M., Mnich K., Naicker S.D., Quandt D., Zeng Q., Patterson J.B., Gorman A.M., Griffin M.D., Samali A, & Logue S.E. (2019). Inhibition of IRE1α RNase activity reduces NLRP3 inflammasome assembly and processing of pro-IL1β. Cell Death & Disease, 10(9), 622.
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4

Western Blot Analysis of Cell Apoptosis

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Cell lysates were obtained by lysing cells in 1% SDS lysis buffer containing 1% β-mercaptoethanol (Gibco). The lysates were immediately boiled for 10 min to minimize protein degradation. Supernatants were diluted in SDS buffer and boiled for 10 min prior to loading. Western blot analysis was performed using the following antibodies: rabbit anti-cleaved caspase-1 (89332S; Cell Signaling Technology), rabbit anti-gasdermin D (39754S; Cell Signaling Technology), rabbit anti-mouse cleaved caspase-8 (8592P; Cell Signaling Technology), mouse anti-RipK1 (610459; BD Biosciences), rabbit anti-RipK3 (2283; ProSci Inc), rabbit anti-phospho RipK3 (91702S; Cell Signaling Technology), rabbit anti-phospho MLKL (37333S; Cell Signaling Technology), rabbit anti-caspase-1 p10 (SC-514; Santa Cruz Biotechnology), mouse anti-caspase-1 (sc-56036; Santa Cruz Biotechnology), mouse anti-β-actin (SC-81178; Santa Cruz Biotechnology), goat anti-mouse IgG HRP (172-1011; Bio-Rad Laboratories Inc), and goat anti-rabbit IgG HRP (A6154; MilliporeSigma). The blots were subsequently detected by chemiluminescence with SuperSignal West Pico PLUS Chemiluminescent Substrate (Thermo Fisher Scientific Inc) on a ChemiDoc MP imager (Bio-Rad Laboratories Inc).
Cai D., Brickey W.J., Ting J.P, & Sad S. (2021). Isolates of Salmonella typhimurium circumvent NLRP3 inflammasome recognition in macrophages during the chronic phase of infection. The Journal of Biological Chemistry, 298(1), 101461.
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5

Inflammasome Activation in Lung Fibroblasts

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The following antibodies were used in explant cultures and were obtained from R&D Systems: anti-IL1β, anti-TNFα, goat IgG, and rat IgG. Gel-purified Escherichia coli LPS (O55:B5) was purchased from Sigma-Aldrich. The Caspase-1 Inhibitor I (Ac-Tyr-Val-Ala-Asp-CHO; YVAD) was purchased from Calbiochem. The following antibodies were used for immunoblotting and immunofluorescence: rat anti-CD68 (Acris), rabbit anti-caspase 1 p10 (Santa Cruz Biotechnology), rabbit anti-NALP1/NLRP1 (Santa Cruz Biotechnology), rabbit anti-ASC (Abcam), and rabbit anti-Cryopyrin (NLRP3, Santa Cruz Biotechnology). ProLong Gold with DAPI mounting media and Alexa-conjugated secondary antibodies (AF488, AF555) were obtained from Invitrogen. The nuclear stain DRAQ5 was purchased from Thermo Scientific. Fetal lung mesenchymal cells were treated with recombinant IL1β (rIL1β, R&D Systems), recombinant TNFα (rTNFα, R&D Systems), recombinant IL18 (rIL18, MBL International Corporation), and Pam3Cys-Ser-(Lys)4 (Millipore). Luciferase activity was measured with a luciferase assay system from Promega. Cells were cultured in media from Corning’s Cellgro and 10% FBS (Thermo Scientific). DNase I from bovine pancreas type IV (DNase) and collagenase from clostridium histolyticum type XI were purchased from Sigma-Aldrich.
Stouch A.N., McCoy A.M., Greer R.M., Lakhdari O., Yull F.E., Blackwell T.S., Hoffman H.M, & Prince L.S. (2016). Interleukin-1β and Inflammasome Activity Link Inflammation to Abnormal Fetal Airway Development. Journal of immunology (Baltimore, Md. : 1950), 196(8), 3411-3420.
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6

Macrophage response to silica and rCC16

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THP-1 cells were seeded in 6-well plates, induced to a mature macrophage-like state by PMA. After treated with silica particles and/or rCC16, the macrophages were washed by PBS and then scraped into 1.5-mL EP tubes.
Total cell lysates, cytosolic or nuclear extracts were separated by sodium dodecyl sulfate-polyacrylamide gels (SDS-PAGE) and then transferred onto polyvinylidene difluoride (PVDF) membranes. Nuclear and cytosolic extracts was extracted with a Nuclear and Cytoplasmic Protein Extraction kit (P0028, Beyotime Biotechnology, Shanghai, China) in accordance with the manufacturer's instructions. After blockade with 5% BSA, PVDF membranes were incubated overnight at 4°C with corresponding primary antibodies and followed by incubation with appropriate secondary antibodies. The primary antibodies used in this study included: rabbit anti-NF-κB p65, rabbit anti-NLRP3 (both from Cell Signaling Technology, Danvers, MA, USA), mouse anti-IL-1β (R&D Systems, Minneapolis, MN, USA), rabbit anti-caspase-1 p10, rabbit anti-β-actin and rabbit anti-Histone H3 antibodies (all from Santa Cruz Biotechnology, Santa Cruz, CA, USA). Secondary antibodies were horseradish peroxidase-conjugated anti-mouse and Santi-rabbit IgG (both from Santa Cruz Biotechnology).
Cui X., Xu R., Zhang H., Peng Z., Feng M., Yu B., Wang Y., Shi T., Zhou Y, & Liu Y. (2020). Exogenous Clara cell protein 16 attenuates silica particles-induced inflammation in THP-1 macrophages by down-regulating NF-κB and caspase-1 activation. The Journal of toxicological sciences, 45(10).
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7

Western Blot for SIRT1, Caspase-1, p16

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Cell lysates were obtained using RIPA buffer (150 mM NaCl, 10 mM Tris, pH 7.2, 0.1% SDS, 1.0% Triton X-100, 5 mM EDTA, pH 8.0) with protease inhibitor Cocktail (Roche Applied Science, Indianapolis, IN, USA). Protein concentration for each sample was evaluated by Bradford assay. Proteins (30 μg) were analysed by SDS-PAGE, and then transferred to nitrocellulose membrane (Bio-Rad, Hercules, CA, USA). 5% skim milk was used to block the membrane that was then incubated overnight with the primary antibody.
Mouse anti-SIRT1 (Abcam), rabbit anti-Caspase-1 p10 (Santa Cruz Biotechnology), mouse anti-p16ink4a (Santa Cruz) and, rabbit anti-α-tubulin (Cell Signaling), were used as primary antibodies.
Secondary horseradish peroxidase-conjugated anti-mouse and anti-rabbit antibodies were from horse and goat respectively (Vector laboratories, CA, USA). Protein bands were visualized using Clarity ECL chemiluminescence substrate (Bio-Rad) with Uvitec Imager (UVItec,Cambridge,UK) and then quantified using ImageJ software.
Caspase 1 activity was measured as the ratio between band intensity of the pro-Caspasi-1 and of the cleaved Caspasi-1. Each measure was normalized with α-tubulin.
Matacchione G., Gurău F., Silvestrini A., Tiboni M., Mancini L., Valli D., Rippo M.R., Recchioni R., Marcheselli F., Carnevali O., Procopio A.D., Casettari L, & Olivieri F. (2021). Anti-SASP and anti-inflammatory activity of resveratrol, curcumin and β-caryophyllene association on human endothelial and monocytic cells. Biogerontology, 22(3), 297-313.
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