Anti ki 67 mib 1

Manufactured by Agilent Technologies

Sourced in Denmark, United States, United Kingdom

The Anti-Ki-67 (MIB-1) is a monoclonal antibody used in immunohistochemical procedures to detect the Ki-67 protein, which is a marker of cell proliferation. It is commonly used in research and diagnostic applications to assess the proliferative activity of cells in various tissues and specimens.

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Lab products found in correlation

Histofine dab substrate kit, by Nichirei Biosciences (1 mentions) Anti sox2 d6d9, by Cell Signaling Technology (1 mentions) Anti oct 3 4 c 10, by Santa Cruz Biotechnology (1 mentions) Bz 2 analyzer, by Keyence (1 mentions) Biotinylated goat anti mouse igg, by Vector Laboratories (1 mentions) Biotinylated goat anti rabbit igg, by Vector Laboratories (1 mentions) Envision system hrp, by Agilent Technologies (1 mentions) Vectastain elite abc standard kit, by Vector Laboratories (1 mentions) Anti phospho 4ebp1, by Cell Signaling Technology (1 mentions) Anti phospho akt, by Cell Signaling Technology (1 mentions) Anti phospho p70s6k, by Cell Signaling Technology (1 mentions) Exiaqua, by Nikon (1 mentions) Eclipse 80i microscope, by Nikon (1 mentions) Anti cd68 pg m1, by Agilent Technologies (1 mentions) Anti cd31, by Agilent Technologies (1 mentions) Anti sox2, by R&D Systems (1 mentions) Anti cd34, by Abcam (1 mentions) Anti cd44, by Cell Signaling Technology (1 mentions) Anti nestin, by Santa Cruz Biotechnology (1 mentions) Vectastain elite kit, by Vector Laboratories (1 mentions)

Spelling variants of this product

MIB-1 (247 citations) Ki-67 (MIB-1; (57 citations) Anti-Ki-67 antibody (clone MIB-1, (9 citations) Anti-human Ki-67 (clone MIB-1, (6 citations) Mouse anti-human Ki-67 (clone MIB-1, (6 citations) Ki-67 (5 citations) Ready-to-use anti-Ki-67 mouse monoclonal antibody (clone MIB-1, (3 citations) Anti-Ki-67 monoclonal antibody (MIB-1, (3 citations) Monoclonal Mouse anti-Human Ki-67 Clone MIB-1 (3 citations) Anti-TM (1 citations)

19 protocols using anti ki 67 mib 1

Immunohistochemical Analysis of CCA Tissues

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Hematoxylin and eosin staining of the original CCA tissues and transplanted tumors was performed regularly. For immunohistochemistry staining, a standard protocol using citrate buffer retrieval buffer was used. Signals were enhanced by EnVision-system-HRP (Dako, Glostrup, Denmark) or the Vectastain Elite ABC standard kit (Vector Laboratories, Burlingame, CA, USA). Detection was performed using the Histofine^® DAB substrate kit (Nichirei Bioscience, Tokyo, Japan).
The sources of antibodies were as follows: anti-CK19 (HPA002465,) was from Sigma-Aldrich, anti-Ki-67 (MIB-1) was from Dako, anti-epithelial cell adhesion molecule (EpCAM, C-10) and anti-Oct-3/4 (C-10) were from Santa Cruz Biotechnology (Dallas, TX, USA), anti-Sox2 (D6D9) was from Cell Signaling Technology (Danvers, MA, USA), and biotinylated goat anti-mouse IgG and biotinylated goat anti-rabbit IgG were from Vector Laboratories.
The comparison of tissue architecture between the original CCA tissue and transplanted tissue was made by the pathologists. The images were taken by the BZ-8100 Biozero fluorescent microscope. For the quantitation, the immunoreactivity signals were quantified by BZ-II Analyzer (Keyence, Osaka, Japan) as previously described [36 (link)].

Vaeteewoottacharn K., Pairojkul C., Kariya R., Muisuk K., Imtawil K., Chamgramol Y., Bhudhisawasdi V., Khuntikeo N., Pugkhem A., Saeseow O.T., Silsirivanit A., Wongkham C., Wongkham S, & Okada S. (2019). Establishment of Highly Transplantable Cholangiocarcinoma Cell Lines from a Patient-Derived Xenograft Mouse Model. Cells, 8(5), 496.

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Histopathological Lung Tissue Analysis

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Lung specimens were fixed in 10% formaldehyde, embedded in paraffin, and stained with haematoxylin-eosin (HE) and Elastica-Masson (EMa). Specimens from patients 1 and 2 were examined immunohistochemically using the following commercially available antibodies: anti-p53 (DO-7, 1/200 dilution; Leica Biosystems, Nussloch, Eisfeld, Germany), anti-CEA (II-7, 1/50 dilution; Dako, Santa Clara, CA, USA), anti-Ki-67 (MIB1, 1/200 dilution; Dako), anti-melanosome (HMB45, 1/100 dilution; Dako), anti-phospho-AKT (#3787, 1/25 dilution; Cell Signaling Technology, Danvers, MA, USA), anti-phospho-p70S6K (#9206, 1/50 dilution; Cell Signaling Technology), and anti-phospho-4E-BP1 (#2855, 1/25 dilution; Cell Signaling Technology) antibodies.

Shoji T., Konno S., Niida Y., Ogi T., Suzuki M., Shimizu K., Hida Y., Kaga K., Seyama K., Naka T., Matsuno Y, & Nishimura M. (2019). Familial multifocal micronodular pneumocyte hyperplasia with a novel splicing mutation in TSC1: Three cases in one family. PLoS ONE, 14(2), e0212370.

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Immunofluorescent Staining and Imaging

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Cells were placed on glass coverslips in 6-well plates. After the indicated treatment, cells were fixed with absolute methanol at −20°C for 5 min. Cells were blocked in 0.5% (v/v) Triton X-100 in PBS and 3% (w/v) bovine serum albumin (BSA) and then incubated with anti-Ki67 (MIB-1) (Dako, Glostrup, Denmark) or anti-p65 (ser15, Cell Signaling Technology). Cells were then washed three times, incubated with FITC-conjugated secondary antibody and stained with Hoechst 33342 for visualization of DNA content and mitotic figures. Images were taken using a QImaging ExiAqua monochrome digital camera attached to a Nikon Eclipse 80i Microscope (Nikon, Melville, NY, USA) and visualized with QCapturePro software.

Wagner V.P., Martins M.A., Martins M.D., Warner K.A., Webber L.P., Squarize C.H., Nör J.E, & Castilho R.M. (2016). Overcoming adaptive resistance in mucoepidermoid carcinoma through inhibition of the IKK-β/IκBα/NFκB axis. Oncotarget, 7(45), 73032-73044.

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Immunohistochemical Analysis of Tumor-Associated Macrophages

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Sections (3‐μm thick) obtained from paraffin‐embedded tumor samples were immunohistochemically stained. The following mouse monoclonal antibodies were used: anti‐CD204 (SRA‐E5; TransGenic), anti‐CD163 (10D6; Novocastra, Newcastle, UK), anti‐CD68 (PG‐M1; DAKO, Glostrup, Denmark) and anti‐Ki‐67(MIB‐1; DAKO, Glostrup, Denmark).20 After the samples were reacted with these first antibodies, the samples were incubated with HRP‐labeled secondary anti‐mouse antibody (Nichirei, Tokyo, Japan). The reaction was visualized using the Diaminobenzidine (DAB) system (Nichirei). Normal mouse immunoglobulin (DAKO) was used as a negative control and no signal was observed in these sections. CD68‐, CD163‐ and CD204‐positive cells were counted in four randomly selected areas of a high power field (×200) of a microscope by two pathologists (S.T. and M.Y.) who were blinded to information about the patients’ backgrounds or their prognosis. The data of the Ki‐67 labeling index was previously counted by our research group.21, 22 Double immunostaining of CD204, CD68, CD163 and Ki‐67 was performed as previously described.14 In brief, the sections were reacted with anti‐Ki‐67, CD163 or CD204 antibodies and visualized with DAB. After the sections were washed with citrate buffer (pH 2.2), they were reacted with anti‐CD68 or CD204 antibodies and visualized with HistoGreen (Linaris, Heiderberg, Germany).

Miyasato Y., Shiota T., Ohnishi K., Pan C., Yano H., Horlad H., Yamamoto Y., Yamamoto‐Ibusuki M., Iwase H., Takeya M, & Komohara Y. (2017). High density of CD204‐positive macrophages predicts worse clinical prognosis in patients with breast cancer. Cancer Science, 108(8), 1693-1700.

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Immunohistochemical Profiling of Tumor Samples

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Formalin-fixed tumor samples were embedded in paraffin and 7-μm-thick
sections were obtained. Hematoxylin and eosin staining was performed using standard
procedures. Immunohistochemistry was performed using antigen retrieval with microwave
treatment in 1 mM EDTA (pH 8, for CD31) or 10mM sodium citrate buffer (pH 6, for all the
other antibodies) and Vectastain elite kit (Vector Laboratories, Burlingame, CA), as
described previously (34 , 35 (link)). Primary antibodies used include: anti-HIF-1α (Santa
Cruz Biotechnology, Santa Cruz, CA), anti-CD34 (Abcam, Cambridge, MA), anti-CD31 (Dako,
Carpinteria, CA), anti-nestin (Santa Cruz Biotechnology), anti-CD44 (Cell Signaling
Technology, Beverly, MA), anti-Sox2 (R&D Systems) and anti-Ki-67 (MIB-1, Dako).
Signals were visualized with diaminobenzidine (Dako). Hematoxylin was used to counterstain
nuclei. All specimens were examined under a microscope (Nikon) equipped with a digital
camera (RT Color SPOT) connected to SPOT imaging software (Diagnostic Instruments Inc.,
Sterling Heights, MI).

Nigim F., Cavanaugh J., Patel A.P., Curry WT J.r., Esaki S.I., Kasper E.M., Chi A.S., Louis D.N., Martuza R.L., Rabkin S.D, & Wakimoto H. (2015). Targeting Hypoxia-inducible Factor 1α in a New Orthotopic Model of Glioblastoma Recapitulating the Hypoxic Tumor Microenvironment. Journal of neuropathology and experimental neurology, 74(7), 710-722.

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Immunohistochemistry for YAP/TAZ and Ki-67

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Formalin-Fixed Paraffin embedded sections of 4 μm were deparaffinized through a series of xylen ethanol baths. Antigen retrieval was performed through microwaving in a 0.01 M citrate buffer for 30 minutes. After inactivation of endogenous peroxidases, primary antibodies were applied on the section overnight at 4°C. After the staining with primary and secondary peroxidase-labeled antibodies, the immunoreaction was visualized by the Ultraview-DAB system and slides were counterstained with hematoxylin. Specificity was checked by control staining performed in the absence of primary antibody and with positive tissue. Antibodies used are anti-YAP/TAZ antibody (Cell signaling 8418, dilution 1/200) or anti Ki-67 MIB1 (Dako M7240 dilution 1/50). Scoring and percentage of immunoreactive cells for each marker was done independently by two experienced pathologists from our team (F.R and E.L).

Corvaisier M., Bauzone M., Corfiotti F., Renaud F., Amrani M.E., Monté D., Truant S., Leteurtre E., Formstecher P., Van Seuningen I., Gespach C, & Huet G. (2016). Regulation of cellular quiescence by YAP/TAZ and Cyclin E1 in colon cancer cells: Implication in chemoresistance and cancer relapse. Oncotarget, 7(35), 56699-56712.

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Evaluating Tumor Cell Proliferation and Angiogenesis

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For the evaluation of ET-743 effects on tumor xenografts, tissue sections were stained with anti-Ki67/MIB1 (Dako) and anti-CD31 (BD) antibodies, followed by incubation with secondary antibody (Invitrogen). Ki67 expression was evaluated in 10 fields for each section at 40x by ImageJ; CD31 quantification was performed on 10 z-stack images for each slide at 20× magnification by calculating the positively stained vessel area. Expression values of treated and untreated xenografts were compared by two tailed unpaired T-test, assuming a p-value <0.05 (C.I. 95%) as statistically significant.

Peraldo-Neia C., Cavalloni G., Soster M., Gammaitoni L., Marchiò S., Sassi F., Trusolino L., Bertotti A., Medico E., Capussotti L., Aglietta M, & Leone F. (2014). Anti-cancer effect and gene modulation of ET-743 in human biliary tract carcinoma preclinical models. BMC Cancer, 14, 918.

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Comprehensive Immunohistochemical Analysis of Tissue

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Sections of formalin-fixed, paraffin-embedded tissue blocks were cut at a 3–4-μm thickness for immunohistochemical analysis using an extensive panel of antibodies, including anti-p53 (DO7; DAKO, Copenhagen, Denmark), anti-MUC2 (Ccp58; Novocastra Laboratories, Newcastle, UK), anti-MUC5AC (CLH2; Novocastra Laboratories), anti-MUC6 (CLH5; Novocastra Laboratories), anti-CD10 (56C6; Novocastra Laboratories), anti-caudal-related homeobox transcription factor 2 (CDX2; DAK-CDX2, ready to use; Agilent Technologies), anti-β-catenin (clone 14; Becton Dickinson), and anti-Ki-67 (MIB1, monoclonal; DAKO) antibodies. The sections were prepared, dried, deparaffinized, and rehydrated before subjecting to microwave treatment (H2500, Microwave Processor; Bio-Rad Laboratories, Hercules, CA, USA) in citrate buffer (pH 6.0) for 5 min. The slides were counterstained with hematoxylin, dehydrated, and then mounted. Immunohistochemical staining was examined using the Envision+ System (DAKO).

Sugai T., Uesugi N., Habano W., Sugimoto R., Eizuka M., Fujita Y., Osakabe M., Toya Y., Suzuki H, & Matsumoto T. (2020). The clinicopathological and molecular features of sporadic gastric foveolar type neoplasia. Virchows Archiv, 477(6), 835-844.

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Immunohistochemical Analysis of SUMO Pathway

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IHC was performed as previously described [26 (link)]. For IHC co-stain, FFPE samples were deparaffinized, antigens retrieved at 99°C for 40 minutes, incubated with the first stain antibody (UBC9) O/N at 4°C, and visualized using the 3,3’-diaminobenzidine (DAB) chromogen. Then, samples were treated with Denaturing Solution (Biocare) to avoid cross-reaction, stained with the second antibody (SUMO1), and visualized with LSAB-AP and Vulcan Fast Red. Finally, slides were counterstained with haematoxylin and coverslipped. The following primary antibodies were used: anti-UBC9 (H-81, Santa Cruz Biotechnology), anti-SUMO1 (Santa Cruz Biotechnology), anti-SUMO2/3 (Abcam), anti-p62 (2C11, Abnova), anti-Ki-67(MIB-1, Dako). Images were generated with a BX51 Upright Microscopes from Olympus America Inc at 20x magnification. For morphological pathologist assessment, the Low Grade or High Grade dysplasia were obtained using morphological grading system and the percentage of positive staining in the tumor cells was quantified by blinded reading of the slide. Computational analysis was carried out as previously described [26 (link)].

Mattoscio D., Casadio C., Miccolo C., Maffini F., Raimondi A., Tacchetti C., Gheit T., Tagliabue M., Galimberti V.E., De Lorenzi F., Pawlita M., Chiesa F., Ansarin M., Tommasino M, & Chiocca S. (2017). Autophagy regulates UBC9 levels during viral-mediated tumorigenesis. PLoS Pathogens, 13(3), e1006262.

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Immunohistochemical Staining for Ki-67

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Immunohistochemical staining was performed using the Immunostainer BENCHMARK XT (Ventana medical systems, Tucson, AZ, USA) according to the manufacturer’s instructions. Anti-Ki-67 (MIB1, Dako, 1:200) was used as the primary antibody. Briefly, 4 µm-thick sections of paraffin-embedded tissue were transferred onto poly-l-lysine coated adhesive slides and dried at 62 °C for 30 min. After epitope retrieval, the samples were incubated with primary antibody followed by biotinylated secondary antibody, and signals were developed using peroxidase-labeled streptavidin and 3,3′-diaminobenzidine (DAB). Slides were counterstained with Harris’ hematoxylin. Positive control samples were stained with each batch.

Kim E., Kim M., So K., Park Y.S., Woo C.G, & Hyun S.H. (2020). Characterization and comparison of genomic profiles between primary cancer cell lines and parent atypical meningioma tumors. Cancer Cell International, 20, 345.

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