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Bond reagents

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Bond reagents are a set of chemical compounds used in various laboratory applications. They facilitate the formation of stable bonds between different materials, enabling various analytical and experimental procedures. The core function of these reagents is to promote the adhesion and attachment of samples or analytes to the appropriate surfaces or substrates, as required by the specific laboratory protocol.

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Lab products found in correlation

Novocastra bond polymer refine detection, by Leica (5 mentions) Antibody diluent, by Leica (4 mentions) Bond rx, by Leica (3 mentions) Ab126745, by Abcam (2 mentions) Bond rx autostainer, by Leica (2 mentions) Pannoramic 250 flash scanner, by 3DHISTECH (2 mentions) Asp6025, by Leica (2 mentions) Caseviewer, by 3DHISTECH (2 mentions) Rabbit anti phospho egfr tyr1068, by Cell Signaling Technology (1 mentions) Rabbit anti phospho her2 erbb2 tyr1221 22, by Cell Signaling Technology (1 mentions) Mouse anti pten, by Agilent Technologies (1 mentions) Vectra automated quantitative pathology imaging system, by Zeiss (1 mentions) Stemi sv 11 stereoscope, by Zeiss (1 mentions) Zen software, by Zeiss (1 mentions) Rabbit anti γ h2ax ser139, by Cell Signaling Technology (1 mentions) Rabbit anti pten, by Cell Signaling Technology (1 mentions) Rabbit anti ki67, by Abcam (1 mentions) Apoptag peroxidase in situ apoptosis detection kit, by Merck Group (1 mentions) Axioskop 40, by Zeiss (1 mentions) P erk, by Cell Signaling Technology (1 mentions)

11 protocols using bond reagents

1

Automated IHC Staining and Imaging

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Sections were stained using the Bond RX autostainer (Leica Biosystems Inc., Buffalo Grove, IL, USA). Briefly, slides were baked at 65 °C for 15 min and the automated system performed dewaxing, rehydration, antigen retrieval, blocking, primary antibody incubation, post primary antibody incubation, detection (DAB), and counterstaining using Bond reagents (Leica). Samples were then removed from the machine, dehydrated through a series of ethanol and xylenes and mounted. Rabbit anti-γ-H2AX (Ser139) (1:800, #9718, Cell Signaling), rabbit anti-phospho-EGFR (Tyr1068) (1:50, #2234, Cell Signaling), rabbit anti-phospho-HER2/ErbB2 (Tyr1221/22) (1:400, #2243, Cell Signaling), rabbit anti-PTEN (1:150, #9559, Cell Signaling: used for mouse transplants and normal reduction mammoplasty samples), mouse anti-PTEN (1:100, #M3627, Dako: used for HER2 breast cancer patient cohort), rabbit anti-Ki67 (1:200, #ab16667, Abcam) were diluted in antibody diluent (Leica). TUNEL staining was performed using manufacturer’s recommendations (ApopTag Peroxidase In Situ Apoptosis Detection Kit, #S7100; EMD Millipore). All microscopic imaging was done using the VECTRA® Automated Quantitative Pathology Imaging system or an Axioskop 40 with ZEN Software (Zeiss, Germany). Whole tissue imaging was done using a Stemi SV 11 Stereoscope with ZEN Software (Zeiss).
Sizemore G.M., Balakrishnan S., Thies K.A., Hammer A.M., Sizemore S.T., Trimboli A.J., Cuitiño M.C., Steck S.A., Tozbikian G., Kladney R.D., Shinde N., Das M., Park D., Majumder S., Krishnan S., Yu L., Fernandez S.A., Chakravarti A., Shields P.G., White J.R., Yee L.D., Rosol T.J., Ludwig T., Park M., Leone G, & Ostrowski M.C. (2018). Stromal PTEN determines mammary epithelial response to radiotherapy. Nature Communications, 9, 2783.
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2

Immunohistochemical Determination of ADAR1-p150

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Human breast formalin fixed paraffin embedded tissue array sections (5μm) on positively charged slides were obtained from US Biomax Inc. (Derwood, MD USA, BC081116d). For immunohistochemistry, sections were stained using a Bond RXm autostainer (Leica, Buffalo Grove, IL USA). Briefly, slides were baked at 65°C for 15min and automated software performed dewaxing, rehydration, antigen retrieval, blocking, primary antibody incubation, post primary antibody incubation, detection (DAB), and counterstaining using Bond reagents (Leica). Samples were then removed from the machine, dehydrated through ethanols and xylenes, mounted and cover-slipped. An antibody specifically recognizing ADAR1-p150 (Abcam ab126745) was diluted 1:100 in Antibody Diluent (Leica). Intensity of p150 was scored on a scale of 0 to 3 (range established by samples with the strongest and weakest staining) by increments of 0.5. Any sample scored >1.0 was considered p150-high.
Kung C.P., Cottrell K.A., Ryu S., Bramel E.R., Kladney R.D., Bross E.A., Freeman E.C., Sabloak T., Maggi L J.r, & Weber J.D. (2020). Evaluating the therapeutic potential of ADAR1 inhibition for triple-negative breast cancer. Oncogene, 40(1), 189-202.
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3

Histological Analysis of Mammary Glands

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Inguinal mammary glands for were fixed in 10% neutral-buffered formalin solution for 48 hr and transferred to 70% ethanol. Tissues were processed, embedded in paraffin, cut in 5 m sections on positively charged slides, de-paraffinized, rehydrated, and stained with H&E. For immunohistochemistry, all sections were stained using a Bond Rx autostainer (Leica). Briefly, slides were baked at 65°C for 15min and automated software performed dewaxing, rehydration, antigen retrieval, blocking, primary antibody incubation, post primary antibody incubation, detection (DAB), and counterstaining using Bond reagents (Leica). Samples were then removed from the machine, dehydrated through ethanols and xylenes, mounted and coverslipped. Antibodies for the following markers were diluted in antibody diluent (Leica): rabbit antibodies- Ki67 (1:200, Abcam), CC3 (1:800, Cell Signaling Technology), pERK (1:400, Cell Signaling Technology).
Liu H., Dowdle J.A., Khurshid S., Sullivan N.J., Bertos N., Rambani K., Mair M., Daniel P., Wheeler E., Tang X., Toth K., Lause M., Harrigan M.E., Eiring K., Sullivan C., Sullivan M.J., Chang S.W., Srivastava S., Conway J.S., Kladney R., McElroy J., Bae S., Lu Y., Tofigh A., Saleh S.M., Fernandez S.A., Parvin J.D., Coppola V., Macrae E.R., Majumder S., Shapiro C.L., Yee L.D., Ramaswamy B., Hallett M., Ostrowski M.C., Park M., Chamberlin H.M, & Leone G. (2017). Discovery of stromal regulatory networks that suppress Ras-sensitized epithelial cell proliferation. Developmental cell, 41(4), 392-407.e6.
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4

Immunohistochemical Detection of CD68

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Dissected tissues were fixed in 10% neutral-buffered formalin solution for 48h and transferred to 70% ethanol. Tissues were processed, embedded in paraffin, cut in 5μm sections on positively charged slides, de-paraffinized, rehydrated, and stained with H&E. For immunohistochemistry, all sections were stained using a Bond Rx autostainer (Leica). Briefly, slides were baked at 65oC for 15min and automated software performed dewaxing, rehydration, antigen retrieval, primary antibody incubation, post primary antibody incubation, detection (DAB), and counterstaining using Bond reagents (Leica). Samples were then removed from the machine, dehydrated through ethanols and xylenes, mounted and coverslipped. A RTU mouse antibody was used for CD68 (Leica).
Casadei L., Calore F., Creighton C.J., Guescini M., Batte K., Iwenofu O.H., Zewdu A., Braggio D.A., Lynn Bill K., Fadda P., Lovat F., Lopez G., Gasparini P., Chen J.L., Kladney R.D., Leone G., Lev D., Croce C.M, & Pollock R.E. (2017). Exosome-derived miR-25-3p and miR-92a-3p stimulate liposarcoma progression. Cancer research, 77(14), 3846-3856.
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5

Multiplex Immunofluorescence Staining Protocol

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UW mCRPC TAN TMA (Prostate Cancer Biorepository Network) and FDA normal organ TMA (US Biomax Inc.) were used for mIF studies (Tables S1, S2, and S3). Slides were stained on a Leica BOND Rx stainer (Leica, Buffalo Grove, IL) using Leica Bond reagents for antigen retrieval, antibody stripping (Epitope Retrieval Solution 2), and rinsing after each step (Bond Wash Solution). A high stringency wash was performed after the secondary and tertiary applications using high-salt TBST solution (0.05 M Tris, 0.3 M NaCl, and 0.1% Tween-20, pH 7.2–7.6). Opal Polymer HRP Mouse plus Rabbit (PerkinElmer, Hopkington, MA) was used for all secondary applications.
DeLucia D.C., Cardillo T.M., Ang L., Labrecque M.P., Zhang A., Hopkins J.E., De Sarkar N., Coleman I., da Costa R.M., Corey E., True L.D., Haffner M.C., Schweizer M.T., Morrissey C., Nelson P.S, & Lee J.K. (2020). Regulation of CEACAM5 and therapeutic efficacy of an anti-CEACAM5-SN38 antibody-drug conjugate in neuroendocrine prostate cancer. Clinical cancer research : an official journal of the American Association for Cancer Research, 27(3), 759-774.
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6

Immunohistochemical Determination of ADAR1-p150

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Human breast formalin fixed paraffin embedded tissue array sections (5μm) on positively charged slides were obtained from US Biomax Inc. (Derwood, MD USA, BC081116d). For immunohistochemistry, sections were stained using a Bond RXm autostainer (Leica, Buffalo Grove, IL USA). Briefly, slides were baked at 65°C for 15min and automated software performed dewaxing, rehydration, antigen retrieval, blocking, primary antibody incubation, post primary antibody incubation, detection (DAB), and counterstaining using Bond reagents (Leica). Samples were then removed from the machine, dehydrated through ethanols and xylenes, mounted and cover-slipped. An antibody specifically recognizing ADAR1-p150 (Abcam ab126745) was diluted 1:100 in Antibody Diluent (Leica). Intensity of p150 was scored on a scale of 0 to 3 (range established by samples with the strongest and weakest staining) by increments of 0.5. Any sample scored >1.0 was considered p150-high.
Kung C.P., Cottrell K.A., Ryu S., Bramel E.R., Kladney R.D., Bross E.A., Freeman E.C., Sabloak T., Maggi L J.r, & Weber J.D. (2020). Evaluating the therapeutic potential of ADAR1 inhibition for triple-negative breast cancer. Oncogene, 40(1), 189-202.
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7

Immunofluorescence and IHC Analysis of Tumor Samples

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Tumors were collected in 10% neutral buffered formalin and fixed for 48 h prior to transfer to 70% ethanol for further analysis. Tissues were embedded in Paraffin wax and cut at 5 μm sections prior to staining. The immunofluorescence detections of c-myc and PD-L1 were performed at Molecular Cytology Core Facility of Memorial Sloan Kettering Cancer Center using Discovery XT processor (Ventana Medical Systems, Roche-AZ). Detailed procedures can be found in the Supplementary Information. IF quantification was done in imageJ using mean fluorescence intensity on random selected tissue areas and normalized by total selected area. IHC was performed on a Leica Bond RX automated stainer using Bond reagents (Leica Biosystems, Buffalo Grove, IL), including a polymer detection system (DS9800, Novocastra Bond Polymer Refine Detection, Leica Biosystems). Further details can be found in the Supplementary Data, along with a table with specific antibodies and concentrations.
Henry K.E., Mack K.N., Nagle V.L., Cornejo M., Michel A.O., Fox I.L., Davydova M., Dilling T.R., Pillarsetty N, & Lewis J.S. (2021). ERK Inhibition Improves Anti-PD-L1 Immune Checkpoint Blockade in Preclinical Pancreatic Ductal Adenocarcinoma. Molecular cancer therapeutics, 20(10), 2026-2034.
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8

Immunohistochemistry Analysis of CD3, CD8a, and PD-L1

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Tissue were fixed in 10% neutral buffered formalin, processed in ethanol and xylene, and infiltrated with paraffin in a Leica ASP6025 tissue processor. Paraffin blocks were sectioned at 5 μm thickness and immunohistochemistry was performed with anti-CD3, anti-CD8a, anti-PD-L1 antibodies. Immunohistochemistry was carried out on a Leica Bond RX automated stainer using Bond reagents (Leica Biosystems, Buffalo Grove, IL), including a polymer detection system (DS9800, Novocastra Bond Polymer Refine Detection, Leica Biosystems). The chromogen was 3,3 diaminobenzidine tetrachloride (DAB), and sections were counterstained with hematoxylin. Details for each marker are shown in the Table S3. The slides were scanned with a 20x/0.8NA plan-apochromat objective in a 3DHistech Pannoramic 250 Flash Scanner (3DHISTECH). The scanned images were evaluated with Case Viewer (3DHISTECH). The number of PD-L1 positive cells were counted in the setting of 20x in Case Viewer from five areas of five tumors in each group.
Taniguchi H., Caeser R., Chavan S.S., Zhan Y.A., Chow A., Manoj P., Uddin F., Kitai H., Qu R., Hayatt O., Shah N.S., Villalonga Á.Q., Allaj V., Nguyen E.M., Chan J., Michel A.O., Mukae H., de Stanchina E., Rudin C.M, & Sen T. (2022). WEE1 inhibition enhances the antitumor immune response to PD-L1 blockade by the concomitant activation of STING and STAT1 pathways in SCLC. Cell reports, 39(7), 110814.
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9

Immunohistochemical Staining of Paraffin Sections

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Paraffin embedded sections were deparaffinized and rehydrated at the Laboratory of Comparative Pathology at WCM. The sections were stained using the following antibodies: CD3 (Abcam ab135372, 1:250 following heat-induced epitope retrieval (HIER) in a pH 6.0 buffer); myeloperoxidase (Dako A0398, 1:1000, HIER pH 6.0); and F4/80 (Abcam, ab6640, 1:100, HIER in 10mM citrate buffer, pH6.0). IHC was performed on a Leica Bond RX automated stainer using Bond reagents (Leica Biosystems, Buffalo Grove, IL), including a polymer detection system (DS9800, Novocastra Bond Polymer Refine Detection, Leica Biosystems). The chromogen was 3,3 diaminobenzidine tetrachloride (DAB), and sections were counterstained with hematoxylin.
Sokhi U.K., Xia Y., Sosa B., Turajane K., Nishtala S.N., Pannellini T., Bostrom M.P., Carli A.V., Yang X, & Ivashkiv L.B. (2022). Immune Response to Persistent Staphyloccocus aureus Periprosthetic Joint Infection in a Mouse Tibial Implant Model. Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research, 37(3), 577-594.
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10

Immunohistochemical Analysis of Apoptosis and NK Cells

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IHC was performed on a Leica Bond RX automated stainer using Bond reagents (Leica Biosystems, Buffalo Grove, IL), including a polymer detection system (DS9800, Novocastra Bond Polymer Refine Detection, Leica Biosystems). The chromogen was 3,3 diaminobenzidine tetrachloride (DAB), and sections were counterstained with hematoxylin. Staining for cleaved caspase 3 (CC3) used primary antibody (Cell signaling, Cat.9961) at 1:250 dilution and biotinylated anti-Rabbit IgG (H+L) as secondary antibody (Vector, Cat. BA1000) at 1:100 dilution. Staining for mouse NKp46 used primary antibody (R&D Systems, Cat. AF2225) at 1:1000 dilution and biotinylated anti-Goat IgG (H+L) (Vector, Cat. BA5000). Both markers used heat induced, pH 6.0 for epitope retrieval.
Nixon B.G., Chou C., Krishna C., Dadi S., Michel A.O., Cornish A.E., Kansler E.R., Do M.H., Wang X., Capistrano K.J., Rudensky A.Y., Leslie C.S, & Li M.O. (2022). Cytotoxic granzyme C-expressing ILC1s contribute to antitumor immunity and neonatal autoimmunity. Science immunology, 7(70), eabi8642.
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