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Anti bzlf1

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Anti-BZLF1 is a laboratory antibody product produced by Santa Cruz Biotechnology. It is designed to recognize and bind to the BZLF1 protein, which is involved in the regulation of the Epstein-Barr virus (EBV) lytic cycle. The core function of this antibody is to provide a tool for researchers to study the expression and role of BZLF1 in EBV-related cellular processes.

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Lab products found in correlation

Anti bmrf1, by Merck Group (2 mentions) Anti h3k4me1, by Abcam (1 mentions) Control igg antibody, by Merck Group (1 mentions) Anti h3, by Abcam (1 mentions) Lightcycler 480, by Roche (1 mentions) Complete protease inhibitor cocktail, by Roche (1 mentions) Nucleospin extract 2 kit, by Macherey-Nagel (1 mentions) Anti ifi16, by Santa Cruz Biotechnology (1 mentions) Tgf β, by Merck Group (1 mentions) 12 o tetradecanoylphorbol 13 acetate tpa, by Merck Group (1 mentions) Hrp labeled donkey anti goat antibody, by Santa Cruz Biotechnology (1 mentions) Anti p18, by Thermo Fisher Scientific (1 mentions) Anti involucrin, by Merck Group (1 mentions) Anti blimp1, by Cell Signaling Technology (1 mentions) Anti δnp63, by BioLegend (1 mentions) Anti klf4, by Cell Signaling Technology (1 mentions) Hrp labeled goat anti mouse antibody, by Thermo Fisher Scientific (1 mentions) Anti c myc, by Abcam (1 mentions) Anti lmp2a, by Santa Cruz Biotechnology (1 mentions) Anti actin, by Merck Group (1 mentions)

6 protocols using anti bzlf1

1

Pathologist-Verified EBV-LPD Tumor Samples

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De-identified, pathologist-verified EBV-LPD tumor samples were obtained from The Ohio State University Pathology Core Facility (Columbus, OH). Patient and hu-PBL-SCID EBV-LPD tumors were stained with anti-BZLF1 (1:300) (Santa Cruz) and visualized by immunohistochemistry according to IRB-approved protocol.
Hartlage A.S., Liu T., Patton J.T., Garman S.L., Zhang X., Kurt H., Lozanski G., Lustberg M.E., Caligiuri M.A, & Baiocchi R.A. (2015). The Epstein-Barr virus lytic protein BZLF1 as a candidate target antigen for vaccine development. Cancer immunology research, 3(7), 787-794.
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2

ChIP-Seq Protocol with Antibodies

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All ChIP experiments were performed in triplicates as described previously (Woellmer et al, 2012 (link)) using anti-H3 (#1791; Abcam), anti-H3K4me1 (#8895; Abcam), anti-BZLF1 (#17503; Santa Cruz) antibodies, or control IgG antibody (#PP64B; Millipore). All buffers were supplemented with the cOmplete protease inhibitor cocktail (Roche), and all steps were performed at 4°C if not noted otherwise. Details of the ChIP and ReChIP protocols can be found in the Materials and Methods section of the Supplementary Information.
Immunoprecipitated DNA was purified with the NucleoSpin Extract II kit (Macherey-Nagel) according to the manufacturer’s protocol and eluted in 60 μl elution buffer. The samples were analyzed by qPCR with a LightCycler 480 (Roche) instrument.
Schaeffner M., Mrozek-Gorska P., Buschle A., Woellmer A., Tagawa T., Cernilogar F.M., Schotta G., Krietenstein N., Lieleg C., Korber P, & Hammerschmidt W. (2019). BZLF1 interacts with chromatin remodelers promoting escape from latent infections with EBV. Life Science Alliance, 2(2), e201800108.
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3

Immunofluorescence Assay for Lytic Reactivation

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Cells were plated in 6-well dishes containing coverslips and treated as described in each experiment. Cells were fixed, permeabilized and blocked as described previously [74 (link)]. To detect lytic reactivation, coverslips were incubated with anti-BZLF1 (Santa Cruz, sc-53904, 1:200) for 1 hour at room temperature, washed with PBS, and incubated with anti-Mouse Alexa Fluor 488 at a 1:700 dilution. Cover slips were mounted onto slides and images were acquired as described previously [74 (link)].
De La Cruz-Herrera C.F., Tatham M.H., Siddiqi U.Z., Shire K., Marcon E., Greenblatt J.F., Hay R.T, & Frappier L. (2023). Changes in SUMO-modified proteins in Epstein-Barr virus infection identifies reciprocal regulation of TRIM24/28/33 complexes and the lytic switch BZLF1. PLOS Pathogens, 19(7), e1011477.
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4

Western Blot and Immunofluorescence Antibody Protocol

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The following antibodies were used in Western blotting and immunofluorescence studies: anti-IFI16 (mouse) and anti-BZLF1; Zebra (mouse) (Santa Cruz Biotechnology, Inc., Santa Cruz, CA); EBV Ea-D p52/p50 and anti-IFI16 (rabbit) (Millipore, Billerica, MA); mouse monoclonal D.1.17.G38 (against gp350/220) was generated in the laboratory [21 (link)]. Secondary anti-rabbit-IgG and anti-mouse-IgG antibodies linked to horseradish peroxidase, Alexa Fluor-488, and Alexa Fluor-594 were from KPL, Inc., Gaithersburg, MD, or Molecular Probes, Eugene, OR. 12-O-tetradecanoyl-phorbol-13-acetate (TPA) and phosphonoacetic acid (PAA) were purchased from Millipore-Sigma (Billerica, MA). TGF-β was purchased from Sigma-Aldrich (St. Louis, MO).
Pisano G., Roy A., Ahmed Ansari M., Kumar B., Chikoti L, & Chandran B. (2017). Interferon-γ-inducible protein 16 (IFI16) is required for the maintenance of Epstein-Barr virus latency. Virology Journal, 14, 221.
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5

Detailed Antibody Use for Immunoblot Analysis

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The following antibodies were used for immunoblot analyses in this study: anti-R rabbit polyclonal antibody directed against the R peptide (peptide sequence EDPDEETSSQAVKALREMAD 1: 2500), anti-p63ɑ (Cell Signaling Technologies catalog # 13109 1:1000), anti-ΔNp63 (Biolegend, catalog #619001), anti-KLF4 (Cell Signaling Technologies, catalog #4038 1: 1000), anti-BZLF1 (Santa Cruz, catalog # sc-53904, 1:500), anti-BMRF1 (Millipore, catalog # MAB8186, 1: 2500), anti-p18 (Thermo-Fisher Scientific, # PA1-73003, 1:2000), anti-BLIMP1 (Cell Signaling Technologies catalog # 9115S 1:1000), anti-involucrin (Sigma, catalog #19018, 1:3000), anti-c-myc (Abcam catalog# ab32072, 1:10000), p38 MAPK14 antibody (Cell Signaling Technologies catalog#9218 1:1000) and phospho-p38 MAPK (Cell Signaling Technologies catalog #9211 1:1000), anti-EBV SM polyclonal rabbit antibody (1:750), a generous gift from Sankar Swaminathan of the University of Utah, anti-Tristetraprolin (Cell Signaling Technologies catalog# #71632 1:1000). The secondary antibodies used were Horseradish peroxide (HRP)- labeled goat anti-mouse antibody (Thermo Scientific# 31430, 1:5000), HRP- labeled donkey anti-goat antibody (Santa Cruz#sc-2056, 1:5000), and HRP- labeled goat anti-rabbit antibody (Fisher Scientific 1:10000).
Van Sciver N., Ohashi M., Nawandar D.M., Pauly N.P., Lee D., Makielski K.R., Bristol J.A., Tsao S.W., Lambert P.F., Johannsen E.C, & Kenney S.C. (2021). ΔNp63α promotes Epstein-Barr virus latency in undifferentiated epithelial cells. PLoS Pathogens, 17(11), e1010045.
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6

Antibodies for Immunoblot Analysis

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The following antibodies were used for immunoblot analyses in this study: anti-R rabbit polyclonal antibody directed against the R peptide (peptide sequence EDPDEETSSQAVKALREMAD), anti-BZLF1 (Santa Cruz #sc-53904), anti-BMRF1 (Millipore #MAB8186), anti-IRF4 (Santa Cruz #sc-56713), anti-EBF1 (Biotechne #AF5165), anti-CD11C (Cell Signaling #45581), anti-caspase 1 (Abclonal #A0964), anti-ENPP2 (Proteintech #14243-1-AP), anti-Runx1 (Cell Signaling #4336S), anti-RUNX3 (Cell Signaling #13089), anti-NFATc1 (Santa Cruz #sc-7294), anti-NFATc2 (Cell Signaling #4389), anti-FYN (Santa Cruz #sc-434), anti-TNFRSF9 (Cell Signaling #34594), anti-CD9 (Cell Signaling #13174), anti-HLA DR/MHC class II (Santa Cruz #sc—53319), anti-AHR (Biotechne #AF6185), anti-CYP1B (Proteintech #18505-1-AP), anti-phospho-ERK (Cell Signaling #9101), anti-Tubulin (Sigma #T5168), anti-actin (Sigma #A5441), anti-V5 (Santa Cruz #sc—58052), and anti LMP2A (Santa Cruz #sc-101314). The secondary antibodies used were Horseradish peroxide (HRP)- labeled goat anti-mouse antibody (Fisher Scientific# 31431, 1:5000), HRP- labeled donkey anti-goat antibody (Fisher Scientific # A16005, 1:5000), HRP- labeled goat anti-rabbit antibody (Fisher Scientific# PI32460, 1:10000), and HRP-labeled goat anti-rat light-chain specific antibody (Millipore# AP202P).
Bristol J.A., Brand J., Ohashi M., Eichelberg M.R., Casco A., Nelson S.E., Hayes M., Romero-Masters J.C., Baiu D.C., Gumperz J.E., Johannsen E.C., Dinh H.Q, & Kenney S.C. (2022). Reduced IRF4 expression promotes lytic phenotype in Type 2 EBV-infected B cells. PLoS Pathogens, 18(4), e1010453.
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