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Survivin

Manufactured by Novus Biologicals
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Survivin is a lab equipment product offered by Novus Biologicals. It is a protein that plays a role in the regulation of cell division and programmed cell death. The core function of Survivin is to inhibit apoptosis, or programmed cell death, in cells.

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Lab products found in correlation

β actin, by Merck Group (4 mentions) Cyclin b1, by Cell Signaling Technology (2 mentions) Caspase 3, by Cell Signaling Technology (2 mentions) Tissuelyser, by Qiagen (1 mentions) Ripa buffer, by Thermo Fisher Scientific (1 mentions) Amersham ecl detection system, by Cytiva (1 mentions) Blocking one, by Nacalai Tesque (1 mentions) Amersham ecl, by Cytiva (1 mentions) Protease inhibitor, by Thermo Fisher Scientific (1 mentions) Dc protein assay, by Bio-Rad (1 mentions) Hrp labeled mouse anti rabbit igg, by Jackson ImmunoResearch (1 mentions) Fetal bovine serum (fbs), by Thermo Fisher Scientific (1 mentions) Dulbecco modified eagle medium (dmem), by Thermo Fisher Scientific (1 mentions) Hrp labeled goat anti rabbit igg, by Jackson ImmunoResearch (1 mentions) Coralite488 conjugated goat anti rabbit igg, by Proteintech (1 mentions) Histone h3, by Cell Signaling Technology (1 mentions) P44 p42 mapk, by Cell Signaling Technology (1 mentions) Aurora kinase a, by Cell Signaling Technology (1 mentions) N cadherin, by Merck Group (1 mentions) Hdac4, by Santa Cruz Biotechnology (1 mentions)

Spelling variants of this product

Anti-Survivin (13 citations) Anti-survivin antibody (4 citations) Rabbit polyclonal survivin (4 citations) Survivin antibody (2 citations) Anti-survivin (NB500-201) (2 citations) Rabbit anti-survivin (2 citations) Survivin (NB500-201, (2 citations)

17 protocols using survivin

1

Quantification of Survivin Protein Levels

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Tumor tissues were homogenized on ice with a homogenizer (Tissue Lyser, QIAGEN), or harvested cells were lysed with RIPA buffer (Thermo Scientific). Protein samples (30 μg) were separated by SDS-PAGE followed by electroblotting onto a polyvinylidene fluoride membrane. After blocking with Blocking One (Nacalai Tesque), the membrane was incubated overnight with primary antibodies against survivin (Novus Biologicals) and actin (Sigma), both at 1:1000 dilutions. The protein bands were detected using the Amersham ECL Detection System (Amersham Biosciences).
Wu X., Yamamoto H., Nakanishi H., Yamamoto Y., Inoue A., Tei M., Hirose H., Uemura M., Nishimura J., Hata T., Takemasa I., Mizushima T., Hossain S., Akaike T., Matsuura N., Doki Y, & Mori M. (2015). Innovative Delivery of siRNA to Solid Tumors by Super Carbonate Apatite. PLoS ONE, 10(3), e0116022.
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2

Quantitative Protein Analysis via Simple Western

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Protein analysis was performed using Simple Western (Protein Simple, San Jose, CA), a glass capillary based immunoassay system capable of accurate and reproducible separation and quantification of proteins, as recommended by the manufacturer (Protein Simple). Cells were lysed in RIPA lysis buffer with protease inhibitor (Thermo Fisher Scientific, Cat. 0078442), and protein concentration was determined by Bio-Rad DC Protein Assay (Bio-Rad). Proteins were detected with primary antibodies for Top2α (Cat. # ab12318, Abcam, Cambridge, United Kingdom) and survivin (Cat. # NB500–201, Novus Biologicals). Secondary antibodies were provided by the manufacturer (Protein Simple). Samples were processed according to manufacturer’s recommendations using 12–240 kDa plates. Data were analyzed using Compass software (Protein Simple; COMPASS, RRID:SCR_015874).
Mackay R.P., Weinberger P.M., Copland J.A., Mahdavian E, & Xu Q. (2022). YM155 induces DNA damage and cell death in anaplastic thyroid cancer cells by inhibiting DNA topoisomerase IIα at the ATP binding site. Molecular cancer therapeutics, 21(6), 925-935.
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3

Differential Gene Expression in MVA-Infected Cells

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BHK21 tk-ts13 cells were cultured in DMEM containing 10% FBS (Gibco) and exposed to rMVA or WT-MVA at an MOI of 10. At 24 h post-infection, cells were harvested and gene expression was detected via western blotting and immunocytochemical staining using primary antibodies of survivin (1:1000, Novus-Biologicals) and MUC1 VNTR (1:1000, BD Pharmingen). For western blotting, HRP-labeled goat anti-rabbit IgG (Jackson ImmunoResearch) and HRP-labeled rabbit anti-mouse IgG (Jackson ImmunoResearch) were used as the secondary antibody. For immunocytochemical staining, CoraLite488-conjugated goat anti-rabbit IgG (Proteintech, 1:500) and Cy5-labeled goat anti-mouse IgG (Bioss) were used.
Guo Q., Wang L., Xu P., Geng F., Guo J., Dong L., Bao X., Zhou Y., Feng M., Wu J., Wu H., Yu B., Zhang H., Yu X, & Kong W. (2020). Heterologous prime-boost immunization co-targeting dual antigens inhibit tumor growth and relapse. Oncoimmunology, 9(1), 1841392.
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4

Protein Expression Profiling in Cell Lysates

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Cell lysates were prepared using a buffer containing 10 mmol/L Tris-HCl at pH 7.4 and 1% sodium dodecyl sulfate (SDS). Protein concentration was determined using the Pierce Bicinchoninic Acid (BCA) Assay Kit (Thermo Fisher Scientific). Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) was then performed on the cell lysates, transferred to polyvinylidene fluoride membranes, and immunostained overnight using antibodies as described below. The following antibodies were purchased from Cell Signaling Technology: p21 (dilution at 1:1,000), p27 (1:1,000), cyclinB1 (1:1,000), aurora kinase A (AURKA; 1:1,000), polo-like kinase 1 (PLK1; 1:1,000), cyclin-dependent kinase 1 (CDK1; 1:1,000), E-cadherin (1:1,000), Vimentin (1:1,000), acetyl-histone H3 (1:1,000), histone H3 (1:1,000), p44/p42 MAPK (ERK1/2; 1:1,000), p-p44/p42 MAPK (ERK1/2; 1:1,000), p-AKT1 (1:1,000), and AKT1 (1:1,000). Aurora kinase B (AURKB; 1:1,000) and HDAC2 (1:1,000) antibodies were purchased from Abcam. Survivin (1:1,000) was obtained from Novus Biologicals, N-cadherin (1:1,000) from EMD Millipore, HDAC1 (1:1,000) from Thermo Fisher Scientific, and HDAC10 from BioVision. The following antibodies were purchased from Santa Cruz Biotechnology: p27(1:1,000), HDAC4(1:1,000), HDAC6 (1:1,000), and GAPDH (1:5,000). Band densitometry analysis was performed using ImageJ software (NCI).
Kotian S., Zhang L., Boufraqech M., Gaskins K., Gara S.K., Quezado M., Nilubol N, & Kebebew E. (2017). Dual Inhibition of HDAC and Tyrosine Kinase Signaling Pathways with CUDC-907 Inhibits Thyroid Cancer Growth and Metastases. Clinical cancer research : an official journal of the American Association for Cancer Research, 23(17), 5044-5054.
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5

Immunohistochemical Profiling of Tissue Microarray

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Immunohistochemistry was performed on 4-µm-thick sections of tissue microarray blocks that included 192 surgicallyremoved samples. Tissue sections were deparaffinized and rehydrated following standard procedures. Heat-induced antigen retrieval was carried out and sections were incubated with primary antibodies for 32 minutes at 37°C at a dilution of 1:50 for HBME1 and cyclin D1, 1:100 for Gal-3 and SFN/14-3-3 δ, 1:200 for CK19, HMGA2 and CEACAM6, and 1:600 for survivin. Monoclonal antibodies were used for Gal-3 (clone 9C4, Novocastra, Newcastle, United Kingdom), HBME1 (clone HBME-1, Dako, Carpinteria, CA, USA), CK19 (clone RCK108, Dako), cyclin D1 (clone SP4, Thermo Fisher Scientific, Waltham, MA, USA), CEACAM6 (clone 9A6, Abcam, Cambridge, MA, USA) and SFN/14-3-3 δ (clone 5D7, Santacruz, Dalla, TX, USA). Polyclonal antibodies were used for HMGA2 (Biocheck, Foster city, CA, USA) and survivin (Novus Biologicals, Littleton, CO, USA). All immunohistochemical staining was carried out in a BenchMark XT autostainer (Ventana Medical Systems, Tucson, AZ, USA) using the DAB detection kit (Ventana Medical Systems).
Jang M.H., Jung K.C, & Min H.S. (2015). The Diagnostic Usefulness of HMGA2, Survivin, CEACAM6, and SFN/14-3-3 δ in Follicular Thyroid Carcinoma. Journal of Pathology and Translational Medicine, 49(2), 112-117.
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6

Synthesis and In Vitro Evaluation of HDAC Inhibitors

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The HDAC inhibitors AR-42 and SAHA were synthesized as described [10 (link)]. Stock solutions AR-42 and SAHA were prepared in DMSO and diluted in the indicated culture medium for treatment of cells in vitro. Antibodies against Akt, pAkt-Ser473, phosphor-glycogen synthase kinase-3 (GSK3)β, caspase-3, Bcl-xl, α-tubulin, cyclin D1, phosphor-p70 ribosomal protein S6 kinase (p70S6K), p-mTOR and PTEN were purchased from Cell Signaling Technologies (Beverly, MA). Additional polyclonal rabbit antibodies used were acetylated histones H3 (N-terminus) and H4 (Lys5/8/12/16) (Upstate Biotechnology, Inc., Lake Placid, NY), β-actin (Sigma, St. Louis, MO), and survivin (Novus Biologicals, Littleton, CO).
Murahari S., Jalkanen A.L., Kulp S.K., Chen C.S., Modiano J.F., London C.A, & Kisseberth W.C. (2017). Sensitivity of osteosarcoma cells to HDAC inhibitor AR-42 mediated apoptosis. BMC Cancer, 17, 67.
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7

Quantitative Western Blot Analysis of Apoptosis-Related Proteins

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Whole-cell lysates were obtained from breast cancer cells using RIPA buffer (Santa Cruz Biotechnology Inc., Dallas, TX, USA) and 25 μg protein was subjected to 10% SDS-PAGE and transferred to Hybond-P membranes (GE Healthcare Europe GmbH, Freiburg, Germany). Filters were incubated with primary antibodies raised against β-actin (Sigma-Aldrich Srl, Milan, Italy), Bcl-2 (Santa Cruz Biotechnology Inc., Dallas, TX, USA), XIAP (Cell Signaling Technology, Danvers, MA), Survivin (Novus Biologicals, Littleton, CO), IAP1 (Cell Signaling Technology, Danvers, MA). An enhanced chemiluminescence detection kit (SuperSignal West Femto Maximum Sensitivity Substrate, Thermo Scientific) and the Versa DOC imaging system (BioRad) were used to visualized hybridization.
Immunoblots were quantified by densitometry, the data were expressed as arbitrary units (protein/β-actin) [35 (link)].
Bonaccorsi P.M., Labbozzetta M., Barattucci A., Salerno T.M., Poma P, & Notarbartolo M. (2019). Synthesis of Curcumin Derivatives and Analysis of Their Antitumor Effects in Triple Negative Breast Cancer (TNBC) Cell Lines. Pharmaceuticals, 12(4), 161.
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8

Immunophenotyping of PBMCs using Flow Cytometry

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PBMCs were washed once with phosphate-buffered saline (PBS) solution, fixed in 4% paraformaldehyde at room temperature for 40 min, and incubated in 0.2% Triton X-100 (Sangon Corp., Shanghai, China) for 10 min and 5% calf serum at 4°C for 10 min. PBMCs were then incubated in PBS containing survivin (1:1,000; Novus Biologicals, Inc., Littleton, CO, USA), CD4 (1:100), CD8 (1:100), CD44 (1:100) (all from Boster Biotechnology Co., Wuhan, China), VEGF (1:200), and ICAM-1 (1:200; Santa Cruz Biotechnology, Inc., Dallas, TX, USA) antibody overnight at 4°C. After washing, the PBMCs were incubated in appropriate fluorescein isothiocyanate (FITC) (survivin) and/or Cy3 (CD4, CD8, CD44, VEGF and ICAM-1)-conjugated secondary antibodies. Flow cytometric analysis was conducted using a Coulter Epics XL flow cytometer (Beckman Coulter, Brea, CA, USA), and the percentage of positive cells was calculated.
XU Y., TAN X., WANG D., WANG W., LI Y., WU M., CHEN S., WU Y, & TAN C. (2015). Elevated survivin expression in peripheral blood mononuclear cells is central to collateral formation in coronary chronic total occlusion. International Journal of Molecular Medicine, 35(6), 1501-1510.
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9

Feline Oral Squamous Cell Carcinoma Cell Lines

Cited 1 time
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Feline OSCC lines SCCF1, SCCF2 and SCCF3 were previously established and characterized by one of the investigators (TJR) [27 (link), 28 (link)]. The SCCF1, SCCF2 and SCCF3 cell lines were derived from a laryngeal, bone-invasive gingival and lingual SCC, respectively. Cell lines were maintained in DMEM supplemented with 10 % FBS, non-essential amino acids, sodium pyruvate, penicillin, streptomycin, L-glutamine, and HEPES (4-(2-hydroxythyl)-1-piperazineethanesolfonic acid) at 35 °C, supplemented with 5 % CO2. LLL12 was synthesized and purified as previously described and provided by Dr. Chenglong Li (College of Pharmacy, The Ohio State University) [24 (link)]. Aliquots of the stock solution were stored at -20 °C until use. The proteasome inhibitor MG132 was purchased from Calbiochem (Billerica, MA). The following antibodies were used for Western blotting and/or immunohistochemistry experiments: pSTAT3 (Y705, Cell Signaling Technology, Danvers, MA), STAT3 (Cell Signaling Technology), survivin (Novus Biologicals, Littleton, CO), pAKT (Ser473, Cell Signaling Technology), AKT (BD Biosciences, San Jose, CA) and β-actin (Santa Cruz Biotechnology, Santa Cruz, CA).
Brown M.E., Bear M.D., Rosol T.J., Premanandan C., Kisseberth W.C, & London C.A. (2015). Characterization of STAT3 expression, signaling and inhibition in feline oral squamous cell carcinoma. BMC Veterinary Research, 11, 206.
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10

Keratinocyte Subpopulations Immunofluorescence

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Freshly isolated keratinocyte subpopulations were fixed in 4% buffered PFA and cytospun onto glass slides. Cells were permeabilized with Triton × 100 0.1%, stained for K10 (clone EP1607Y, Epitomics, Burlingame, CA, USA), K15 (EPR1614Y, Epitomics), and Involucrin (clone I9018, Sigma) and then labeled with Alexa Fluor secondary antibodies, Alexa Fluor 546 and 488-conjugated goat IgGs (Invitrogen, Waltham, MA, USA). Then slides were stained with 1 μg/mL Dapi (Sigma). Immunofluorescence on skin equivalent slides was performed as in IHC methods except for the different primary antibodies: K10, K15, and Survivin (Novus Biologicals, Littleton, CO, USA) and the secondary antibodies Alexa Fluor 546 and 488-conjugated goat IgGs (Invitrogen). Micrographs were taken on a Confocal Scanning Laser Microscopy (Leica TCS4D) (Leica, Exton, PA, USA). Quantification of immunofluorescence staining was performed by analyzing 6 representative fields for each staining sample, using ImageJ software. Scoring was made by means of positive cell counting.
Lotti R., Palazzo E., Quadri M., Dumas M., Schnebert S., Biondini D., Bianchini M.A., Nizard C., Pincelli C, & Marconi A. (2022). Isolation of an “Early” Transit Amplifying Keratinocyte Population in Human Epidermis: A Role for the Low Affinity Neurotrophin Receptor CD271. Stem Cells, 40(12), 1149-1161.
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