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Survivin

Survivin is a protein that plays a crucial role in cell division and apoptosis (programmed cell death).
It is often overexpressed in various types of cancer, making it a potential target for cancer therapies.
PubCommpare.ai's AI-driven platform can enhance the reproducibility and accuracy of Survivin research by helping researchers easily locate the best protocols from literature, pre-prints, and patents, and identify the optimal methods and products through intelligent comparisons.
This powerful tool can streamline Survivin research and accelerate the development of new treatments.

Most cited protocols related to «Survivin»

HNSCC Tissue Microarray Analysis

Cited 12 times

Tissue arrays of formalin-fixed tissues from human head and neck squamous cell carcinoma (HN803) were retrieved from Biomax US (Rockville, MD, USA). Clinical data, including pathological classification and TNM classification, were provided by Biomax. These tissue microarray slides included 57 confirmed cases of HNSCC, 10 cases of normal tongue mucosa, and 4 cases of lymph node metastasis in HNSCC tissue. Immunohistochemistry for Tgfbr1 (1:100), p-S6 (S235/236, 1:200), and Survivin (1:400) was stained in serial-cut tissue array sections.

Sun Z.J., Zhang L., Hall B., Bian Y., Gutkind J.S, & Kulkarni A.B. (2012). Chemopreventive and chemotherapeutic actions of mTOR inhibitor in genetically-defined head and neck squamous cell carcinoma mouse model. Clinical cancer research : an official journal of the American Association for Cancer Research, 18(19), 5304-5313.

Publication 2012

Formalin Homo sapiens Immunohistochemistry Lymph Node Metastasis Microarray Analysis Mucous Membrane Squamous Cell Carcinoma of the Head and Neck Survivin TGFBR1 protein, human Tissues Tissue Stains Tongue

Phylogenetic Analysis of IAP Proteins

Cited 11 times

Sequences were obtained for human (h) Survivin (Uniprot O15392), Bruce (Q9NR09), cIAP1 (Q13490), cIAP2 (Q13489), XIAP (P98170), ILP2 (Q96P09), MLIAP (Q96CA5), and NAIP (Q13075) with the individual BIR domains parsed. XIAP sequences for Drosophila (d, I6L9G1), Gallus (c, F6TJT0), Xenopus (x, A5D8Q0), Mus (m, Q60989), and Rattus (r, Q9R0I6) were additionally used. Sequence alignments were performed using Clustal Omega (Sievers et al., 2011 (link)) with default settings. A phylogenetic analysis of the domains was performed using maximum likelihood with the JTT matrix (Jones et al., 1992 (link)) and a consensus of 1000 bootstrap replicates (Felsenstein, 1985 (link)) using MEGA5 (Tamura et al., 2011 ). Initial tree for the heuristic search was obtained automatically by applying Neighbor-Join and BioNJ algorithms to a matrix of pairwise distances estimated using a JTT model, and then selecting the topology with superior log likelihood value. The analysis involved 31 amino acid sequences for 66 amino acids. Variants of XIAP associated with disease were identified in published literature, utilizing only single amino acid changes (including mutations to stop codons (X) and not mutations that result in a frameshift.

Prokop J., Jacob H, & Worthey E. (2017). Molecular Modeling in the Age of Clinical Genomics, The Enterprise of the Next Generation. Journal of molecular modeling, 23(3), 75.

Publication 2017

Acids Amino Acids Amino Acid Sequence BIRC2 protein, human BIRC3 protein, human Codon Drosophila Frameshift Mutation Homo sapiens Mutation NAIP protein, human Rattus Sequence Alignment Survivin Trees Xenopus laevis

Immunoblot Analysis of Apoptosis Regulators

Cited 9 times

Whole cell lysates were prepared and subjected to IB analysis using antibodies against SAG (monoclonal antibody raised againt the RING domain (AA44-113), Bax, Bad, cIAP2, (Cell signaling), pRB, Puma, Mcl-1 (Santa Cruz Biotechnology), XIAP, Bcl-XL, p21, (BD Transduction Laboratories), β-Actin (Sigma), Bak (Upstate), Bim (Imgenex), Noxa (Oncogene Science), Bcl-2, (Dako), and survivin (Novus biologicals).

Jia L., Yang J., Hao X., Zheng M., He H., Xiong X., Xu L, & Sun Y. (2010). Validation of SAG/RBX2/ROC2 E3 ubiquitin ligase as an anti-cancer and radio-sensitizing target. Clinical cancer research : an official journal of the American Association for Cancer Research, 16(3), 814.

Publication 2009

Actins Antibodies BCL2 protein, human Biological Factors BIRC3 protein, human Cells Monoclonal Antibodies Novus Oncogenes Puma Survivin

Genotyping Cre-deleted Survivin Allele

Cited 9 times

Mouse genotyping was performed by PCR of the tail DNA. For genotyping Cre-deleted flox survivin allele, three primers, Adv17, Adv25, and Adv28, were used for PCR. For the survivin flox allele, a fragment of 577 bp was generated with the pair of primers Adv25 and Adv 28 as described above. For the deleted allele, a fragment of 420 bp was generated with primers Adv17 and Adv28 (see Fig. 1, A, C, and D). Genotyping of survivin^+/− mice has been described (37 (link)).

Xing Z., Conway E.M., Kang C, & Winoto A. (2004). Essential Role of Survivin, an Inhibitor of Apoptosis Protein, in T Cell Development, Maturation, and Homeostasis. The Journal of Experimental Medicine, 199(1), 69-80.

Publication 2004

Alleles Mice, Laboratory Oligonucleotide Primers Survivin Tail

Quantitative Microscopy of Mitotic Regulators

Cited 9 times

Immunofluorescence, immunoblotting, and immunoprecipitations were all done as described previously (Taylor et al., 2001 (link)) using antibodies against the following: phosphohistone H3 (Upstate Biotechnology); cyclin B1 (Upstate Biotechnology); tubulin (TAT1); centromere/kinetochores (human ACA); BubR1 (SBR1.1); Bub1 (4B12); Aurora A (RAA.1); and Myc-tag (9E10). Aurora B was detected using either the anti-AIM-1 mouse mAb (Transduction Laboratories) or a sheep anti–human Aurora B pAb (unpublished data). For localization of Mad2 and Survivin, we used DLD-1 cell lines stably expressing Myc-tagged hMad2 or hSurvivin ORFs (unpublished data). For IP kinase assays, beads were equilibrated in kinase buffer (10 mM Tris, pH7.5, 5 mM KCl, 1 mM NaF, 0.24 mM DTT, and 2.5 mM MnCl) and were then incubated at RT for 1 h in kinase buffer supplemented with 2.5 μM ATP, 5 μCi γ[³²P]ATP, and 3 μM biotinyl-Ahx-tetra (LRRWSLG) peptide substrate. Reactions were stopped with 20% phosphoric acid, and were then spotted onto P30 filtermat (Whatman). After five washes in 0.5% phosphoric acid, bound radiolabel was quantitated by scintillation counting. Deconvolution microscopy and pixel intensity quantitation were performed as described previously (Taylor et al., 2001 (link)). In brief, kinetochore fluorescence values were determined using softWoRx imaging software (Applied Precision). Background readings were subtracted, and the values were then normalized against the ACA signal to account for any variations in staining or image acquisition. SoftWoRx was used to measure interkinetochore distances using either ACA or Bub1 foci as indicated to determine kinetochore position.

Ditchfield C., Johnson V.L., Tighe A., Ellston R., Haworth C., Johnson T., Mortlock A., Keen N, & Taylor S.S. (2003). Aurora B couples chromosome alignment with anaphase by targeting BubR1, Mad2, and Cenp-E to kinetochores. The Journal of Cell Biology, 161(2), 267-280.

Publication 2003

Antibodies AURKA protein, human AURKB protein, human Biological Assay BUB1 protein, human Buffers Cell Lines Centromere Cyclin B1 Domestic Sheep Fluorescence Homo sapiens Immunofluorescence Immunoprecipitation Kinetochores Microscopy Mus Open Reading Frames Peptides Phosphoric Acids Phosphotransferases Survivin Tetragonopterus Tromethamine Tubulin

Most recents protocols related to «Survivin»

Western Blot Analysis of Signaling Pathways

A549 cells cultured in 2D monolayer or 3D aggregates were harvested and lysed in cell signaling lysis buffer (Merck Millipore) containing protease/phosphatase inhibitor cocktail (Cell Signaling Technology, Inc.). Protein quantification was performed using a Bradford assay kit (Bio-Rad Laboratories, Inc.). A total of 20 µg protein per lane was separated by 10% SDS-PAGE, electroblotted onto Immobilon-P Transfer Membranes (Merck Millipore) and blocked for 1 h at room temperature with 3% BSA (Sigma-Aldrich; Merck KGaA) in TBS-T (0.1% Tween-20). The membranes were then probed with the indicated primary antibodies: phosphorylated (p)-STAT3 (Y705; 1:250; rabbit, monoclonal; cat. no. 9145), STAT3 (1:3,000; rabbit, polyclonal; cat. no. 4904), p-Akt (1:250; rabbit, polyclonal; cat. no. 9271), Akt (1:1,000; rabbit, polyclonal; cat. no 9272), p-ERK (1:10,000; rabbit, polyclonal; cat. no. 9101), ERK (1:4,000; rabbit, polyclonal; cat. no. 9102), p-p38 (T180/Y182; 1:250; rabbit, polyclonal; cat. no. 9211), p38 (1:1,000; rabbit, polyclonal; cat. no. 9212), p-FAK (1:200; rabbit, monoclonal; cat. no. 8556), FAK (1:1,000; rabbit, polyclonal; cat. no. 3285), Mcl-1 (1:250; rabbit, polyclonal; cat. no. 4572), survivin (1:200; rabbit, polyclonal; cat. no. 2803), puma (1:500; rabbit, polyclonal; cat. no. 4976), cyclin D1 (1:250; rabbit, polyclonal; cat. no. 2922), cyclin D3 (1:1,000; mouse, monoclonal; cat. no. 2936), CDK2 (1:1,000; rabbit, monoclonal; cat. no. 2546) (all from Cell Signaling Technology, Inc.), MYLK (1:200; mouse, monoclonal; cat. no. sc-365352; Santa Cruz Biotechnology, Inc.) and GAPDH (1:50,000; rabbit, monoclonal; cat. no. ab190480; Abcam) at 4°C overnight. The membranes were washed and incubated for 1 h at room temperature in a 1:5,000 dilution of HRP-conjugated goat anti-rabbit (monoclonal; cat. no. 7074; Cell Signaling Technology, Inc.) or rabbit anti-mouse (polyclonal; cat. no. P0260; Dako; Agilent Technologies, Inc.) secondary antibodies. Visualization of the protein bands was performed with the SuperSignal^™ West Pico PLUS Chemiluminescent Substrate (cat. no. 34580; Thermo Fisher Scientific) or SuperSignal^™ West Femto Maximum Sensitivity Substrate (cat. no. 34096; Thermo Fisher Scientific, Inc.). Quantification of the bands was carried out by densitometry using ImageJ version 1.53k software (National Institutes of Health).

Keeratichamroen S., Sornprachum T., Ngiwsara L., Ornnork N, & Svasti J. (2023). p‑STAT3 influences doxorubicin and etoposide resistance of A549 cells grown in an in vitro 3D culture model. Oncology Reports, 49(4), 71.

Publication 2023

A549 Cells Antibodies Biological Assay Buffers CDK2 protein, human Cyclin D1 Cyclin D3 Densitometry GAPDH protein, human Goat Hypersensitivity Immobilon P Mice, House Mitogen-Activated Protein Kinase 3 MYLK protein, human Phosphoric Monoester Hydrolases Protease Inhibitors Proteins Puma Rabbits SDS-PAGE Staphylococcal Protein A STAT3 Protein Survivin Technique, Dilution Tissue, Membrane Tween 20

Signaling Pathways in Chronic Myelogenous Leukemia

K562 CD34⁺ cells and primary CML CD34⁺ cells(2.5 × 10⁵ cells/well in 6-well plates) were exposed to various stimulating conditions for the indicated times. The lysated preparations were carried out by Western blot as previously mentioned. Antibodies for Western blot were used in our research: p-JAK2^Tyr1007/1008, p-STAT5^Tyr694, JAK2, STAT5, BCR-ABL, CrkL, Survivin, Bcl-2, Mcl-1, XIAP, cleaved-caspase 3, bax, caspase 3, GAPDH, DNMT1 were obtained from Cell Signaling Technology (Danvers, MA, USA). SHP-1 and cyclin D2 were ordered from Abcam(Cambridge, MA, USA).

Xu X., Ji S., Chen Y., Xia S., Li Y., Chen L., Li Y., Zhang F., Zhang Z, & Zheng S. (2023). Induction of DNMT1-dependent demethylation of SHP-1 by the natural flavonoid compound Baicalein overcame Imatinib-resistance in CML CD34+ cells. Cell Communication and Signaling : CCS, 21, 47.

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Publication 2023

Antibodies BCL2 protein, human Caspase 3 CCND2 protein, human Cells CRKL protein DNMT1 protein, human GAPDH protein, human Janus Kinase 2 K562 Cells STAT5A protein, human Survivin Western Blot

Western Blot Analysis of Cell Signaling

Western blot analysis was performed as previously described 20 (link). Antibodies against FoxM1, survivin, XIAP, Cyclin B1, phospho-Cdc25c, Bax, Bcl-2, cleaved PARP, and cleaved caspase 3 were purchased from Cell Signaling Technology (Danvers, MA, USA), and antibodies against Ki67 and GAPDH were purchased from Santa Cruz Biotechnology (Dallas, TX, USA). The antibody against phospho-histone H2AX, Ser139 (γ-H2AX) was purchased from EMD Millipore (MA, USA).

Qin Q., Chen H., Xu H., Zhang X., Chen J., Zhang C., Liu J., Xu L, & Sun X. (2023). FoxM1 knockdown enhanced radiosensitivity of esophageal cancer by inducing apoptosis. Journal of Cancer, 14(3), 454-463.

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Publication 2023

Antibodies BCL2 protein, human Caspase 3 CDC25C protein, human Cyclin B1 GAPDH protein, human H2AX protein, human Immunoglobulins Survivin Western Blot

Quantification of Survivin mRNA Levels

Total RNA from control or PPRH-transfected cells for 24 h and 48 h was extracted using Trizol Reagent (Life Technologies, Madrid, Spain), following the instructions of the manufacturer. Complementary DNA was synthesized in a 20 µL reaction mixture from 1 µg of total RNA, 0.5 mM of each deoxyribonucleotide triphosphate (dNTP, Epicentre, Madison, USA), 250 ng of random hexamers (Roche, Barcelona, Spain), 10 mM dithiothreitol, 200 units of a Moloney murine leukemia virus reverse transcriptase (RT), 20 units of RNase inhibitor, and 4 µL of buffer (5×) (all three from Lucigen, Middleton, WI, USA). The reaction was incubated at 42 °C for 1 h.
The BIRC5 mRNA TaqMan probe (Hs04194392_s1; ThermoFisher Scientific, Madrid, Spain) was used to determine survivin mRNA levels and the Cyclophilin (PP1A) mRNA TaqMan probe (Hs04194521_s1, ThermoFisher Scientific, Madrid, Spain) was used as the endogenous control. The reaction was conducted in 20 μL containing 1xTaqMan Universal PCR Mastermix (Applied Biosystems, Madrid, Spain), 0.5xTaqMan probe, and 3 μL of cDNA. PCR cycling conditions were 10 min denaturation at 95 °C, followed by 40 cycles of 15 s at 95 °C, and 1 min at 60 °C using a QuantStudio 3 Real-Time PCR System (Applied Biosystems, Barcelona, Spain). The quantification was performed using the ΔΔCt method, where Ct is the threshold cycle that corresponds to the cycle when the amount of amplified mRNA reaches the fluorescence threshold.

Delgado A., Griera R., Llor N., López-Aguilar E., Busquets M.A., Noé V, & Ciudad C.J. (2023). Trioleyl Pyridinium, a Cationic Transfection Agent for the Lipofection of Therapeutic Oligonucleotides into Mammalian Cells. Pharmaceutics, 15(2), 420.

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Publication 2023

BIRC5 protein, human Buffers Cells Deoxyribonucleotides Dithiothreitol DNA, Complementary Endoribonucleases Fluorescence Moloney Leukemia Virus Peptidylprolyl Isomerase RNA, Messenger RNA-Directed DNA Polymerase Survivin triphosphate trizol

Design and Validation of Polypurine Reverse Hoogsteen Hairpins

The search for polypurine sequences to design PPRHs from was performed with the triplex-forming oligonucleotide target sequence search software (http://utw10685.utweb.utexas.edu/tfo/, accessed on 22 December 2022, MD Anderson cancer center, The University of Texas) [32 (link)]. The PPRH (HpsPr-C) against the survivin gene, which was directed to the promoter sequence, was used for gene silencing experiments and was previously validated in our laboratory [15 (link),19 (link)]. The design of the hairpin consisted of two antiparallel mirror repeats of polypurine sequences bound by intramolecular reverse Hoogsteen bonds and linked by a thymidine loop (4–5 Ts). The same PPRH against survivin was also synthesized with a fluorescence label (FAM-HpsPr-C) in its 5′-end. The negative control was an unspecific scrambled hairpin (HpScr9) that could not form a triplex with the target DNA.
Hairpins used in the study were synthesized as nonmodified oligodeoxynucleotides by Merck (Haverhill, UK). They were resuspended in a sterile Tris–EDTA buffer (1 mM EDTA and 10 mM Tris, pH 8.0) (Merck, Madrid, Spain) and stored at −20 °C. The hairpin sequences are shown in Table 1.
The PPRHs designed using the TFO searching tool are shown in Figure 1. The two sequences run in an antiparallel fashion bound by Hoogsteen bonds and linked by a thymidine loop.

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Publication 2023

Edetic Acid Fluorescence Genes Malignant Neoplasms Oligodeoxyribonucleotides Oligonucleotides Sterility, Reproductive Survivin Thymidine triplex DNA Tromethamine

Top products related to «Survivin»

Survivin by Cell Signaling Technology

Sourced in United States, United Kingdom, China

Survivin is a recombinant protein that functions as a member of the inhibitor of apoptosis (IAP) protein family. It plays a role in the regulation of cell division and programmed cell death (apoptosis).

Cleaved caspase 3 by Cell Signaling Technology

Sourced in United States, United Kingdom, China, Germany, Canada, Japan, Morocco, Denmark, Switzerland, France, Netherlands, Macao

Cleaved caspase-3 is an antibody that detects the activated form of caspase-3 protein. Caspase-3 is a key enzyme involved in the execution phase of apoptosis, or programmed cell death. The cleaved caspase-3 antibody specifically recognizes the active, cleaved form of the enzyme and can be used to monitor and quantify apoptosis in experimental systems.

Bcl 2 by Cell Signaling Technology

Sourced in United States, China, United Kingdom, Germany, Canada, Japan, Italy, India

Bcl-2 is a protein that plays a key role in regulating apoptosis, or programmed cell death. It functions as an anti-apoptotic protein, helping to prevent cell death by inhibiting the activity of pro-apoptotic proteins.

Survivin by Santa Cruz Biotechnology

Sourced in United States, Germany

Survivin is a protein involved in the regulation of cell division and cell death. It plays a role in preventing apoptosis, or programmed cell death. Survivin is expressed in a variety of cancer cells and is associated with tumor progression and drug resistance.

Bcl xl by Cell Signaling Technology

Sourced in United States, United Kingdom, Germany, China, Japan, Canada

Bcl-xL is a protein that plays a role in the regulation of apoptosis, or programmed cell death. It is a member of the Bcl-2 family of proteins and functions as an anti-apoptotic factor, helping to prevent cell death. Bcl-xL is commonly used in cell biology research to study the mechanisms of apoptosis and cell survival.

β actin by Merck Group

Sourced in United States, United Kingdom, Germany, China, Canada, Japan, Macao, Italy, Sao Tome and Principe, Israel, Spain, Denmark, France, Finland, Australia, Morocco, Ireland, Czechia, Sweden, Uruguay, Switzerland, Netherlands, Senegal

β-actin is a protein that is found in all eukaryotic cells and is involved in the structure and function of the cytoskeleton. It is a key component of the actin filaments that make up the cytoskeleton and plays a critical role in cell motility, cell division, and other cellular processes.

Anti survivin by Cell Signaling Technology

Sourced in United States

Anti-survivin is a laboratory reagent used to detect the expression of the survivin protein. Survivin is a member of the inhibitor of apoptosis (IAP) family of proteins and plays a role in the regulation of cell division and programmed cell death. Anti-survivin can be used in various experimental techniques, such as Western blotting, immunohistochemistry, and flow cytometry, to study the expression and localization of survivin in biological samples.

Trizol reagent by Thermo Fisher Scientific

Sourced in United States, China, Japan, Germany, United Kingdom, Canada, France, Italy, Australia, Spain, Switzerland, Netherlands, Belgium, Lithuania, Denmark, Singapore, New Zealand, India, Brazil, Argentina, Sweden, Norway, Austria, Poland, Finland, Israel, Hong Kong, Cameroon, Sao Tome and Principe, Macao, Taiwan, Province of China, Thailand

TRIzol reagent is a monophasic solution of phenol, guanidine isothiocyanate, and other proprietary components designed for the isolation of total RNA, DNA, and proteins from a variety of biological samples. The reagent maintains the integrity of the RNA while disrupting cells and dissolving cell components.

Mcl 1 by Cell Signaling Technology

Sourced in United States, United Kingdom, Canada, China, Germany

Mcl-1 is a protein that plays a role in the regulation of apoptosis, or programmed cell death. It is a member of the Bcl-2 family of proteins and functions as an anti-apoptotic protein, helping to prevent cell death.

Bcl2 associated x (bax) by Cell Signaling Technology

Sourced in United States, China, United Kingdom, Germany, Canada, Japan, Morocco

Bax is a protein that plays a key role in the intrinsic apoptosis pathway. It is a member of the Bcl-2 family of proteins and functions as a pro-apoptotic regulator.

What are the common challenges researchers face when working with Survivin?

Researchers often encounter difficulties in reproducibility and accuracy when working with Survivin. The complex nature of this protein, its involvement in various cellular processes, and the diverse experimental conditions used in Survivin research can lead to inconsistent results across studies. This makes it challenging to identify the most effective protocols and products for Survivin-related research and therapeutic development.

How can PubCompare.ai help streamline Survivin research?

PubCompare.ai's AI-driven platform can significantly enhance the reproducibility and accuracy of Survivin research. The tool allows researchers to screen protocol literature more efficiently, leveraging AI to pinpoint critical insights. By comparing protocols from literature, pre-prints, and patents, PubCompare.ai can help identify the most effective methods and products related to Survivin, enabling researchers to choose the best option for their specific research goals. This can streamline the research process and accelerate the development of new Survivin-targeted treatments.

What are the different variations or types of Survivin?

Survivin is a member of the inhibitor of apoptosis (IAP) protein family and exists in several isoforms or splice variants. These include wild-type Survivin, as well as variants such as Survivin-2B, Survivin-ΔEx3, and Survivin-3B. Each of these isoforms can have distinct functional roles and expression patterns, which researchers must consider when studying Survivin in the context of cancer and other diseases.

What are some specific applications of Survivin research?

Survivin research has a wide range of applications, particularly in the field of oncology. Since Survivin is often overexpressed in various types of cancer, it has become a potential target for cancer therapies. Researchers are exploring the use of Survivin as a biomarker for early cancer detection, as well as developing Survivin-targeted treatments, such as vaccines, small-molecule inhibitors, and antisense oligonucleotides. Additionally, Survivin research can provide insights into cell division, apoptosis, and other fundamental cellular processes, with implications for a variety of disease states.

How can PubCompare.ai help identify the optimal Survivin protocols and products?

PubCompare.ai's AI-driven analysis can highlight key differences in protocol effectiveness, enabling researchers to choose the best option for reproducibility and accuracy in Survivin research. By leveraging machine learning algorithms to compare protocols from literature, pre-prints, and patents, the platform can identify the most effective methods and prodcuts related to Survivin. This can save researchers time and effort, while also improving the quality and consistency of their Survivin-focused studies.

More about "Survivin"

Survivin, a crucial protein in cell division and apoptosis, is often overexpressed in various cancers, making it a promising target for cancer therapies.
PubCommpare.ai's AI-driven platform can enhance the reproducibility and accuracy of Survivin research by helping researchers easily locate the best protocols from literature, preprints, and patents, and identify the optimal methods and products through intelligent comparisons.
This powerful tool can streamline Survivin research and accelerate the development of new treatments.
Survivin is a member of the inhibitor of apoptosis (IAP) protein family and plays a pivotal role in regulating cell division and programmed cell death (apoptosis).
It is often overexpressed in a wide range of cancers, including lung, breast, prostate, and colorectal cancer, making it an attractive target for cancer therapies.
The Cleaved caspase-3 protein is a key executioner of apoptosis and is closely linked to Survivin's function.
Bcl-2 and Bcl-xL are anti-apoptotic proteins that can interact with and regulate Survivin's activity. β-actin is commonly used as a housekeeping gene or loading control in Survivin research.
Anti-survivin antibodies are widely used to detect and quantify Survivin expression in various experimental settings.
TRIzol reagent is a popular tool for extracting RNA, which can be used to analyze Survivin gene expression.
Mcl-1 and Bax are other proteins that play important roles in the apoptosis pathway and may be studied in conjunction with Survivin.
PubCommpare.ai's AI-driven platform can streamline Survivin research by helping researchers easily locate the best protocols and identify the optimal methods and products through intelligent comparisons.
This tool can enhance the reproducibility and accuracy of Survivin research, accelerating the development of new cancer therapies.