Anti malt1

Manufactured by Santa Cruz Biotechnology

Sourced in United States

Anti-MALT1 is a laboratory reagent used for research purposes. It is an antibody that specifically binds to the MALT1 protein, which is involved in cellular signaling pathways. The core function of Anti-MALT1 is to facilitate the detection and study of MALT1 in biological samples.

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MALT1 (5 citations)

7 protocols using anti malt1

Characterization of MALT1 Isoforms in NF-kB Activation

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Expression vectors pCMV6/XL5/MALT1 [containing full length isoform A (824 aa) MALT1 cDNA] was purchased from ORIGENE Technologies Inc. (Rockville, Maryland). pcDNA3.1⁺/C-(k)DYk-MALT1B [containing full length isoform B (813 aa) MALT1 cDNA] was purchased from GenScript (Piscataway, NJ). Schematic representation of all MALT1 variants was shown in S1 Fig. Please also see the S1 Text for detailed construction information.
The following antibodies were used: anti-MALT1 (Santa Cruz Biotechnology, B-12 sc-46677, mouse monoclonal), anti-MALT1 (Santa Cruz Biotechnology, H-300 sc-28246, rabbit polyclonal), anti-BCL10 (Santa Cruz Biotechnology, 331.3 sc-5273, mouse monoclonal), anti-IκBα (Santa Cruz Biotechnology,C-15 sc-203, rabbit polyclonal), anti-phospho-IκBα (Cell Signaling Technology #9246, mouse monoclonal), anti-RelB (Cell Signaling Technology #4922, rabbit monoclonal), anti-Regnase-1 (MCPIP1) (R&D Systems #604421, mouse monoclonal), anti-HA (Santa Cruz Biotechnology, F-7 sc-7392, mouse monoclonal), anti-FLAG (Sigma M2, mouse monoclonal), anti-GAPDH (Santa Cruz Biotechnology, 6C5 sc-32233, mouse monoclonal), goat antiserum to human IgG (MP Biomedicals, LLC. #55087), peroxidase-labeled goat anti-mouse IgG (SeraCare Life Science, kPL 074–1806), peroxidase-conjugated goat anti-rabbit IgG (Jackson ImmunoResearch Inc. 111-035-003).

Wu C.H., Yang Y.H., Chen M.R., Tsai C.H., Cheng A.L, & Doong S.L. (2018). Autocleavage of the paracaspase MALT1 at Arg-781 attenuates NF-κB signaling and regulates the growth of activated B-cell like diffuse large B-cell lymphoma cells. PLoS ONE, 13(6), e0199779.

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Protein Interaction Analysis by Co-Immunoprecipitation

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Cell lysates were made in lysis buffer (150 mM NaCl, 20 mM HEPES, pH 7.4, 1% Triton X-100, 10% glycerol) and a mixture of proteases inhibitors (Protease Inhibitor Cocktail, Roche) according to the manufacturer’s instructions. Proteins were separated by SDS–PAGE, transferred onto nitrocellulose membrane, and incubated with primary antibodies followed by horseradish peroxidase-conjugated secondary antibodies (Amersham Biosciences Corp., Piscataway, NJ, USA). Blots were developed using the enhanced chemiluminescen (ECL) system (Amersham Biosciences Corp.). For co-immunoprecipitation experiments, cells were lysed in lysis buffer and immunocomplexes were bound to protein A/G (Amersham Biosciences) for 2 h at 4 °C. Immunocomplexes were extensively washed, resolved by SDS–PAGE, and analyzed by immunoblot assay. Antisera and monoclonal antibodies were the following: anti-FLAG, anti-β-Actin, (Sigma-Aldrich, St. Louis, MI, USA); anti-HA, anti-myc, anti-MALT1, anti-CARMA2, anti-NEMO, anti-ubiquitin, (Santa Cruz Biotechnology, Dallas, TX, USA); and anti-RNF7 (Abcam, Cambridge, UK). The anti-BCL10 antibody was described in [37 (link)].

Telesio G., Scudiero I., Pizzulo M., Mazzone P., Zotti T., Voccola S., Polvere I., Vito P, & Stilo R. (2017). The E3 Ubiquitin Ligase RNF7 Negatively Regulates CARD14/CARMA2sh Signaling. International Journal of Molecular Sciences, 18(12), 2581.

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Antibodies and Inhibitors for Signaling Pathways

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The antibody against linear ubiquitin chains and RBCK1 were described(13 (link)). Other antibodies were purchased as follows: anti-IKKβ, anti-phospho-IKKβ, anti-IκBα, anti-phospho-IκBα anti-CARD11 from Cell Signaling Technologies; anti-ubiquitin (P4D1), polyclonal anti-NEMO/IKKγ (FL–419) anti-β-actin, anti-IRAK1, anti-MALT1, anti-A20 from Santa Cruz Biotechnology; anti-RNF31, anti-SHARPIN, anti-myc-tag from Abcam; monoclonal anti-NEMO/IKKγ from BD Pharmingen; anti-human IgM from Jackson ImmunoResearch Lab. Isotype control antibodies were obtained from the same company as each experimental antibody. Secondary HRP-conjugated antibodies were obtained from GE Healthcare.
The Myc-tag elution peptide and Etoposide were obtained from Sigma. The IMiD compound lenalidomide was obtained from Celgene Corporation. The IKKβ inhibitor MLN120B was obtained from Millennium Pharmaceuticals. The BTK inhibitor (ibrutinib) was obtained from Pharmacyclics, Inc. The MALT1 inhibitor Z-VRPR-FMK was obtained from Enzo Life Sciences. Tissue culture grade DMSO vehicle control was obtained from Sigma-Aldrich.

Yang Y., Schmitz R., Mitala J., Whiting A., Xiao W., Ceribelli M., Wright G.W., Zhao H., Yang Y., Xu W., Rosenwald A., Ott G., Gascoyne R.D., Connors J.M., Rimsza L.M., Campo E., Jaffe E.S., Delabie J., Smeland E.B., Braziel R.M., Tubbs R.R., Cook J.R., Weisenburger D.D., Chan W.C., Wiestner A., Kruhlak M.J., Iwai K., Bernal F, & Staudt L.M. (2014). Essential Role of the Linear Ubiquitin Chain Assembly Complex in Lymphoma Revealed by Rare Germline Polymorphisms. Cancer discovery, 4(4), 480-493.

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Visualization of CARD11-BCL10-MALT1 Complex

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Purified primary B or T cells were adhered to poly-L-lysine coated slides and fixed for 30 min with 2% paraformaldehyde (Electron Microscopy Sciences), then permeabilized for 5 min in 0.1% Triton X-100/PBS. After blocking for 30 min in 1% FCS/PBS, cell spots were incubated overnight with the following Abs: anti-CARD11 (Abcam), anti-BCL10, anti-MALT1, anti-p65, anti-RelB (Santa Cruz Biotech), anti-phospho-IKKα/β (Cell Signaling Technology). Cell spots were washed 3x in PBS, then incubated with goat anti-rabbit or anti-mouse secondary Abs conjugated to AlexaFluor 488, 568, or 647 (Invitrogen) plus a 1:10000 dilution of Hoechst 33342 (30 min per Ab). Following 6x PBS washes, coverslips were attached using Fluoromount (Southern Biotech). Fluorescent images were acquired on a Zeiss 710 confocal laser scanning microscope using a 63x oil immersion objective, and analyzed using Zeiss ZEN software. Jurkat or BJAB cells transfected with Venus-CARD11 were prepared and analyzed in similar fashion; CARD11-FLAG was visualized after staining with an AlexaFluor 647-conjugated anti-FLAG Ab (Cell Signaling Technology).

Brohl A.S., Stinson J., Su H.C., Badgett T., Jennings C.D., Sukumar G., Sindiri S., Wang W., Kardava L., Moir S., Dalgard C.L., Moscow J.A., Snow A.L, & Khan J. (2014). Germline CARD11 mutation in a patient with severe congenital B cell lymphocytosis. Journal of clinical immunology, 35(1), 32-46.

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Western Blot Protein Detection

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Whole-cell lysates extracted with RIPA buffer or immunoprecipitation elution were separated by SDS-PAGE gels and followed by transferring to PVDF membranes. Membranes were incubated with the indicated primary antibodies: anti-FLAG (Sigma-Aldrich; cat. #F3165, RRID:AB_259529), anti-MALT1 (Santa Cruz Biotechnology; cat. #sc-46677, RRID:AB_627909), anti-CARD11 (Abcam; cat. #ab113409, RRID:AB_10861854), anti–β-Actin (AC-15, Sigma-Aldrich), and then mouse/rabbit peroxidase-conjugated secondary antibodies (Cell Signaling Technology). Protein intensity was detected with enhanced chemiluminescence using the ChemiDoc imaging system (Bio Rad).

Xia M., David L., Teater M., Gutierrez J., Wang X., Meydan C., Lytle A., Slack G.W., Scott D.W., Morin R.D., Onder O., Elenitoba-Johnson K.S., Zamponi N., Cerchietti L., Lu T., Philippar U., Fontan L., Wu H, & Melnick A.M. (2022). BCL10 Mutations Define Distinct Dependencies Guiding Precision Therapy for DLBCL. Cancer Discovery, 12(8), 1922-1941.

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Western Blot Analysis of Immune Signaling

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Whole cell lysates extracted with RIPA buffer or IP elution were separated by SDS-PAGE gels and followed by transferring to PVDF membranes. Membranes were incubated with indicated primary antibodies: anti-Flag (Sigma-Aldrich Cat# F3165, RRID:AB_259529), anti-MALT1 (Santa Cruz Biotechnology Cat# sc-46677, RRID:AB_627909), anti-CARD11 (Abcam Cat# ab113409, RRID:AB_10861854), anti-β-Actin (AC-15, Sigma-Aldrich), and then mouse/rabbit peroxidase-conjugated secondary antibodies (Cell Signaling Technology). Protein intensity was detected with enhanced chemiluminescence using ChemiDoc imaging system (Bio Rad).

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Western Blot Protein Expression Analysis

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Western blots were performed as described from our previous studies [47 (link),48 (link)]. Specific primary antibody: anti-IkBα (Santa Cruz Biotechnology, Dallas, TX, USA) or anti-NF-kB p65 (Santa Cruz Biotechnology) or anti-TRAF6 (Santa Cruz Biotechnology) or anti-αsma (Santa Cruz Biotechnology) or anti-MCPIP1 (Santa Cruz Biotechnology) or anti-MALT1 (Santa Cruz Biotechnology) were mixed in 1× PBS, 5% w/v nonfat dried milk, 0.1% Tween-20, and incubated at 4 °C, overnight. After, blots were incubated with peroxidase-conjugated bovine anti-mouse IgG secondary antibody or peroxidase-conjugated goat anti-rabbit IgG (1:2000, Jackson Immuno Research, West Grove, PA, USA) for 1 h at room temperature. To verify that membranes were loaded with equal amounts of protein, they were also incubated with the antibody against laminin (1:1000; Santa Cruz Biotechnology) and GADPH (1:1000; Santa Cruz Biotechnology). Signals were detected with enhanced chemiluminescence detection system reagent according to manufacturer’s instructions (Super- Signal West Pico Chemiluminescent Substrate, Pierce, Altrincham, UK). The relative expression of the protein bands was quantified by densitometry with ChemiDoc XRS software (Bio-Rad, Perth, UK) and standardized tob-actin levels. Images of blot signals (8-bit/600-dpi) were imported to analysis software (Image Quant TL, v2003, Altrincham, UK).

Fusco R., Siracusa R., D’Amico R., Cordaro M., Genovese T., Gugliandolo E., Peritore A.F., Crupi R., Di Paola R., Cuzzocrea S, & Impellizzeri D. (2020). Mucosa-Associated Lymphoid Tissue Lymphoma Translocation 1 Inhibitor as a Novel Therapeutic Tool for Lung Injury. International Journal of Molecular Sciences, 21(20), 7761.

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