Log In Sign up
The largest database of trusted experimental protocols

Survivin

Manufactured by R&D Systems
Visit Supplier
Sourced in United States, Germany, United Kingdom

Survivin is a recombinant protein produced in E. coli. It is a member of the Inhibitor of Apoptosis Protein (IAP) family, which plays a role in regulating cell division and programmed cell death. Survivin is involved in the regulation of cell cycle and apoptosis.

Automatically generated - may contain errors

Lab products found in correlation

β actin, by Merck Group (5 mentions) Mcl 1, by Cell Signaling Technology (3 mentions) Cyclin a, by Cell Signaling Technology (2 mentions) Beclin 1, by Cell Signaling Technology (2 mentions) P stat3, by Cell Signaling Technology (2 mentions) P akt, by Cell Signaling Technology (2 mentions) Bcl2 associated x (bax), by Cell Signaling Technology (2 mentions) Bcl 2, by Cell Signaling Technology (2 mentions) E cadherin, by Cell Signaling Technology (2 mentions) Snail, by Cell Signaling Technology (2 mentions) Mmp 9, by Cell Signaling Technology (2 mentions) P mtor, by Cell Signaling Technology (2 mentions) Caspase 3, by Cell Signaling Technology (2 mentions) β actin, by Cell Signaling Technology (2 mentions) N cadherin, by Cell Signaling Technology (2 mentions) Supersignal west dura extended duration substrate, by Thermo Fisher Scientific (2 mentions) Cleaved parp, by Cell Signaling Technology (2 mentions) Cyclin b1, by Cell Signaling Technology (2 mentions) P akt ser473, by Cell Signaling Technology (2 mentions) Ciap1, by R&D Systems (2 mentions)

Close spelling variants of this product

Anti-survivin (13 citations) Anti-survivin antibodies (6 citations) Survivin antibody (5 citations) Anti-Survivin (AF886, (4 citations) Rabbit anti-Survivin IgG (3 citations) Rabbit anti‐survivin (2 citations) Antibodies against Survivin (2 citations) Anti-human survivin antibody (2 citations) Antibodies against c-Myc and survivin (2 citations) Surveyor™ IC Human Total Survivin Immunoassay (2 citations)

21 protocols using survivin

1

Antibody Validation for Cell Signaling

Check if the same lab product or an alternative is used in the 5 most similar protocols
The following antibodies and dilutions were used: Sox9 (#ab185966, abcam, Cambridge, UK) 1:5000 for western blot (WB); 1:500 for immunofluorescence (IF); Sox2 (#MAB2016, R&D Systems, Wiesbaden, Germany) 1:1000 (WB) and 1:250 (IF); Olig2 (#AF2418, R&D Systems) 1:10,000 (WB) and 1:5000 (IF); GAPDH (#CB1001, Calbiochem, Darmstadt, Germany) 1:20,000; CHK1 (#2360, Cell Signaling Technologies (CST), Frankfurt am Main, Germany) 1:1000; phosphoCHK1 (CST #2348), 1:1000; CHK2 (CST #2662S) 1:1000; Survivin (R&D #AF886) 1:1000; TP53BP1 (NB #100-304, Novus Biologicals, Wiesbaden, Germany) 1:1000; γH2AFXSer139 (#05-636, clone JBW301, Merck Millipore, Darmstadt, Germany) 1:1000; F(ab′)2-Goat anti-Rabbit IgG (H + L) Cross-Adsorbed Secondary Antibody, Alexa Fluor 488 (A-11070, Thermo Fisher) 1:500; F(ab′)2-Goat anti-mouse IgG (H + L) Cross-Adsorbed Secondary Antibody, Alexa Fluor 594 (A-11020, Thermo Fisher) 1:500; F(ab′)2-donkey anti-goat IgG (H + L) Cross-Adsorbed Secondary Antibody, Alexa Fluor 488 (A-11055, Thermo Fisher) 1:500; donkey anti-goat IgG (sc2042, Santa Cruz, Dallas, TX, USA) 1:10,000.
Linder B., Wehle A., Hehlgans S., Bonn F., Dikic I., Rödel F., Seifert V, & Kögel D. (2019). Arsenic Trioxide and (−)-Gossypol Synergistically Target Glioma Stem-Like Cells via Inhibition of Hedgehog and Notch Signaling. Cancers, 11(3), 350.
+ Open protocol
+ Expand
2

Western Blot Analysis of Key Proteins

Check if the same lab product or an alternative is used in the 5 most similar protocols
Cells were lysed using Triton-X-100 sample buffer, and proteins were separated by SDS-PAGE. Detection was done by using specific antibodies against β-actin (Biovision through BioCat GmbH, Heidelberg, Germany), SLC35F2 (Santa Cruz Biotechnology, Dallas, TX, USA), ABCB1, Chk2, phosphorylated Chk2 (Thr68), Baculoviral IAP repeat containing 3 (cIAP-2), histone H2AX, phosphorylated histone H2AX (Ser139) (γH2AX), myeloid cell leukemia sequence-1 (Mcl-1), p21, cleaved PARP, XIAP (all from Cell Signaling via New England Biolabs, Frankfurt, Germany), p53 (Enzo Life Sciences, Lörrach, Germany), survivin and Baculoviral IAP repeat containing 2 (cIAP-1) (R&D Systems, Minneapolis, MN, USA). Protein bands were visualized by laser-induced fluorescence using infrared scanner for protein quantification (Odyssey, Li-Cor Biosciences, Lincoln, NE, USA).
Voges Y., Michaelis M., Rothweiler F., Schaller T., Schneider C., Politt K., Mernberger M., Nist A., Stiewe T., Wass M.N., Rödel F, & Cinatl J. (2016). Effects of YM155 on survivin levels and viability in neuroblastoma cells with acquired drug resistance. Cell Death & Disease, 7(10), e2410-.
+ Open protocol
+ Expand
3

Evaluating Apoptotic and Cell Cycle Markers

Check if the same lab product or an alternative is used in the 5 most similar protocols
Cells were treated with DMSO, TA, VCR or combination for 24 and 48 h. Total cellular protein extracts and western blotting was then done using the previously described method (Abdelrahim et al., 2006 (link)). Proteins of interest were probed by specific primary antibodies of apoptotic markers, cleaved poly-ADP-ribose polymerase (c-PARP, Cell Signaling Technology, Danvers, MA) and survivin (R&D Systems, Minneapolis, MN), and cell cycle markers cyclin A, cyclin D3 (Cell Signaling Technology), cyclin B1 and cyclin dependent kinases 4/6 (CDK4/6, Santa Cruz Biotechnology, Santa Cruz, CA). The expression of β-actin (Sigma) was used as a loading control.
Patil S., Sankpal U.T., Hurtado M., Bowman W.P., Murray J., Borgmann K., Ghorpade A., Sutphin R., Eslin D, & Basha R. (2019). Combination of clotam and vincristine enhances anti-proliferative effect in medulloblastoma cells. Gene, 705, 67-76.
+ Open protocol
+ Expand
4

Protein Expression Analysis of Signaling Pathways

Check if the same lab product or an alternative is used in the 5 most similar protocols
Equal amounts of the protein samples were separated by 10–12% SDS-PAGE. Blots were incubated with primary antibodies against STAT3, p-STAT3 (Ser727, Tyr705), Bcl-2, Bax, caspase 3, mTOR, p-mTOR, Akt, p-Akt, BECLin-1, LC3A, LC3B, E-cadherin, Snail, MMP-9 (Cell Signaling Technology, USA) and Survivin (R&D Systems Inc.). Horseradish peroxidase-labeled anti-rabbit antibody was used as a secondary antibody (Beijing Zhong Shan Biotech Co., Ltd. Beijing, China). Blots were visualized using enhanced chemiluminescence (ECL; Millipore). The band of β-actin (Beijing Zhong Shan Biotech Co., Ltd. Beijing, China) was served as a loading control. Band density was quantified by Image J software.
Ma Y., Zhang X., Xu X., Shen L., Yao Y., Yang Z, & Liu P. (2015). STAT3 Decoy Oligodeoxynucleotides-Loaded Solid Lipid Nanoparticles Induce Cell Death and Inhibit Invasion in Ovarian Cancer Cells. PLoS ONE, 10(4), e0124924.
+ Open protocol
+ Expand
5

Whole-cell Protein Extraction and Western Blot

Check if the same lab product or an alternative is used in the 5 most similar protocols
To obtain whole-cell extracts, cells were lysed with Pro-prep buffer (Intron Biotechnology, Seoul, Korea) containing protease inhibitors. Protein extracts (10–60 μg) were resolved by sodium dodecyl sulfate polyacrylamide gel electrophoresis and transferred to polyvinylidene difluoride membranes. These membranes were probed with SURVIVIN (#AF886, R&D Systems, Waltham, MA), BMI-1 (#sc-10745, Santa Cruz, CA, USA), Caspase-3 (#9662, Cell Signaling, MA, USA), PARP (#9542, Cell Signaling, MA, USA), E-cadherin (#610181, BD Bioscience, San Jose, CA), N-cadherin (#4061, Cell Signaling, MA, USA), VIMENTIN (#sc-32322, Santa Cruz, CA, USA), MMP2 (#13132, Cell Signaling, MA, USA), phospho AKT (#4060, Cell Signaling, MA, USA), AKT (#4691, Cell Signaling, MA, USA), phospho ERK (#612358, BD Bioscience, San Jose, CA), ERK (#9102, Cell Signaling, MA, USA), MCL-1 (#4572, Cell Signaling, MA, USA), FBW7 (#ab10752, Abcam, Cambridge, MA), and β-actin (#3700, Cell Signaling, MA, USA) primary antibodies, followed by incubation with secondary antibodies conjugated to horseradish peroxidase (Santa Cruz Biotechnology, CA, USA). β-actin was used as a loading control for western blot analysis.
Lee Y.S., Song S.J., Hong H.K., Oh B.Y., Lee W.Y, & Cho Y.B. (2020). The FBW7-MCL-1 axis is key in M1 and M2 macrophage-related colon cancer cell progression: validating the immunotherapeutic value of targeting PI3Kγ. Experimental & Molecular Medicine, 52(5), 815-831.
+ Open protocol
+ Expand
6

Proteomic Analysis of PaCa Cell Response to Cu-TA

Check if the same lab product or an alternative is used in the 5 most similar protocols
PaCa cells were treated with DMSO (control) or IC50 dose of Cu-TA. After 48 h, cells were harvested to prepare whole cell lysates. Total cellular protein was extracted using cell lysis buffer and protein quantification was done using the Pierce BCA Micro-Protein Assay Kit (Thermo Scientific, Waltham, MA). Protein samples were then separated through 10% sodium dodecyl sulfate-polyacrylamide gel and then transferred to a nitrocellulose membrane. Next, the membranes were blocked with 5% milk in tris-buffered saline with 1% Tween. Protein expression of TP53 (Cell Signaling Technology, Danvers, MA), ErbB2 (Thermo Scientific), Sp1 (Santa Cruz Biotechnology, Dallas, TX), cleaved PARP (Cell Signaling Technology, Danvers, MA), survivin (R&D Systems, Minneapolis, MN), and STAT3 (Cell Signaling Technology) were evaluated using specific antibodies while the expression of β-actin was used as a loading control. Blots were incubated with primary antibody overnight and incubated with secondary antibody for one hour the following day. Bands were detected using SuperSignal West Dura Extended Duration Substrate (Thermo Scientific).
Hurtado M., Prokai L., Sankpal U.T., Levesque B., Maram R., Chhabra J., Brown D.T., Gurung R.K., Holder A.A., Vishwanatha J.K, & Basha R. (2019). Next generation sequencing and functional pathway analysis to understand the mechanism of action of copper-tolfenamic acid against pancreatic cancer cells. Process biochemistry (Barking, London, England), 89, 155-164.
+ Open protocol
+ Expand
7

Comprehensive Antibody Immunoblotting Assay

Check if the same lab product or an alternative is used in the 5 most similar protocols
The following antibodies were used: beta‐actin (1:10,000, mouse), BIRC8 (mouse, Abnova # H00112401‐B01), cIAP1/2, cleaved caspase‐3‐5A1E (1:300, rabbit, Cell Signaling #9664), CUL1 (1:500, mouse, Invitrogen #32‐2400), cyclin A (1:1,000, mouse, Santa Cruz #sc‐751), cyclin B1 (1:1,000, mouse, Cell Signaling #4138), cyclin E (1:1,000, mouse, kind gift of M. Pagano), FLAG (1:1,000, rabbit, Sigma #F7425), FLAG‐M2 (1:1,000, mouse, Sigma #F3165), HA‐16B12 (1:2,000, mouse, Covance #MMS‐101P), human MCL1 (1:500, rabbit, BD Pharmingen #554103), murine MCL1 (1:1,000, rabbit, A&D Serotec AHP1249), ML‐IAP (mouse, Santa Cruz #sc‐71592), NIAP (rabbit, Abcam #ab25968), PARP1/2 (1:1,000, rabbit, Santa Cruz #sc‐7150), pHH3 (S10) (1:300, rabbit, Cell Signaling #9701), PLK1 (1:500, rabbit, Invitrogen #33‐1700), survivin (1:3,000, rabbit, R&D Systems #AF886), USP7 (rabbit, Bethyl Lab. #A300‐033A), USP9X (1:4,000, rabbit, Bethyl Laboratories #A301‐351A), USP10 (rabbit, Bethyl Lab. #A300‐900A), USP24 (Proteintech Europe, #13126‐1‐AP), USP28 (rabbit, Bethyl Lab. #A300‐898A), V5 (1:1,000, rabbit, Sigma #V8137), XIAP (1:1,000, mouse, BD Biosciences #610716), XIAP (1:1,000, rabbit, Cell Signaling #2042), and XIAP (1:1,000, R&D Systems #AF8221).
Engel K., Rudelius M., Slawska J., Jacobs L., Ahangarian Abhari B., Altmann B., Kurutz J., Rathakrishnan A., Fernández‐Sáiz V., Brunner A., Targosz B., Loewecke F., Gloeckner C.J., Ueffing M., Fulda S., Pfreundschuh M., Trümper L., Klapper W., Keller U., Jost P.J., Rosenwald A., Peschel C, & Bassermann F. (2016). USP9X stabilizes XIAP to regulate mitotic cell death and chemoresistance in aggressive B‐cell lymphoma. EMBO Molecular Medicine, 8(8), 851-862.
+ Open protocol
+ Expand
8

Protein Expression Analysis in Pancreatic Cancer Cells

Check if the same lab product or an alternative is used in the 5 most similar protocols
MIA PaCa-2 and Panc1 cells were plated in 10 cm petri dishes containing 750,000 cells in 10 ml of media. Cell were treated with either DMSO, Cu-TA (MIA PaCa-2: 29 μM; Panc1: 27 μM) or equimolar TA. After 24 and 48 h treatments, cell lysates were collected and prepared. Total cellular protein was extracted using cell lysis buffer and protein quantification was done using the Pierce BCA Protein Assay Kit (Thermo Scientific, Waltham, MA). Protein samples were then separated through 10% sodium dodecyl sulfate-polyacrylamide gel and then transferred to a nitrocellulose membrane. Next, the membranes were blocked with 5% milk in Tris-Buffered Saline with 1% Tween. Blots were incubated with primary antibody overnight and incubated with secondary antibody for one hour the following day. Bands were detected using SuperSignal West Dura Extended Duration Substrate (Thermo Scientific). Protein expression of Sp1 (Santa Cruz Biotechnology, Dallas, TX), Sp3 (Santa Cruz Biotechnology), cleaved PARP (Cell Signaling Technology, Danvers, MA), survivin (R&D Systems, Minneapolis, MN), cyclin B1 (Cell Signaling Technology), and cyclin A (Cell Signaling Technology) were evaluated using specific antibodies while the expression of β-actin (Sigma-Aldrich Corporation) was used as a loading control.
Hurtado M., Sankpal U.T., Kaba A., Mahammad S., Chhabra J., Brown D.T., Gurung R.K., Holder A.A., Vishwanatha J.K, & Basha R. (2018). Novel Survivin Inhibitor for Suppressing Pancreatic Cancer Cells Growth via Downregulating Sp1 and Sp3 Transcription Factors. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology, 51(4), 1894-1907.
+ Open protocol
+ Expand
9

Colorectal Cancer and Cardiomyocyte Cultures

Check if the same lab product or an alternative is used in the 5 most similar protocols
Human colorectal cancer cell lines, HCT116 and HT29 and cardiomyocytes H9C2 were purchased from the American Type Culture Collection (ATCC, Manassas, VA). Colon cancer cells were grown in McCoy's 5A medium, H9C2 cells were grown in DMEM medium and supplemented with fetal bovine serum and maintained in a humidified incubator at 37°C in an atmosphere of 5% CO2.
Tolfenamic acid, curcumin, and DMSO were purchased from Sigma (St. Louis, MO). Antibodies against cPARP and NF-κB were obtained from Cell Signaling Technologies (Beverly, MA), Sp1 and HRP-conjugated mouse anti-rabbit antibody from Santa Cruz (Santa Cruz, CA), survivin from R&D (Minneapolis, MN), and β-actin from Sigma.
Sankpal U.T., Nagaraju G.P., Gottipolu S.R., Hurtado M., Jordan C.G., Simecka J.W., Shoji M., El-Rayes B, & Basha R. (2015). Combination of Tolfenamic acid and curcumin induces colon cancer cell growth inhibition through modulating specific transcription factors and reactive oxygen species. Oncotarget, 7(3), 3186-3200.
+ Open protocol
+ Expand
10

Protein Expression Analysis by Immunoblotting

Check if the same lab product or an alternative is used in the 5 most similar protocols
Cells were lysed using Triton-X-100 sample buffer, and proteins were separated by SDS-PAGE. Detection occurred by using specific antibodies against β-actin (Biovision through BioCat GmbH, Heidelberg Germany), ABCB1, poly (ADP-ribose) polymerase (PARP) (both from Cell Signaling via New England Biolabs, Frankfurt, Germany), MYCN (abcam, Cambridge, UK), and survivin (R&D Systems, Minneapolis, MN, USA). Protein bands were visualised by laser-induced fluorescence using infrared scanner for protein quantification (Odyssey, Li-Cor Biosciences, Lincoln, NE, USA).
Michaelis M., Voges Y., Rothweiler F., Weipert F., Zia-Ahmad A., Cinatl J., von Deimling A., Westermann F., Rödel F., Wass M.N, & Cinatl J J.r. (2020). Testing of the Survivin Suppressant YM155 in a Large Panel of Drug-Resistant Neuroblastoma Cell Lines. Cancers, 12(3), 577.
+ Open protocol
+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required

Sign up now

Revolutionizing how scientists
search and build protocols!