C flip

Manufactured by Santa Cruz Biotechnology

Sourced in United States

C-FLIP is a laboratory equipment product offered by Santa Cruz Biotechnology. It is a device used for the detection and analysis of cellular proteins. The core function of C-FLIP is to facilitate the identification and quantification of specific proteins within cellular samples.

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Lab products found in correlation

Caspase 8, by Cell Signaling Technology (3 mentions) Cleaved caspase 3, by Cell Signaling Technology (3 mentions) Caspase 3, by Cell Signaling Technology (2 mentions) Caspase 9, by Cell Signaling Technology (2 mentions) P jnk, by Cell Signaling Technology (2 mentions) Cleaved caspase 9, by Cell Signaling Technology (2 mentions) β actin, by Santa Cruz Biotechnology (2 mentions) C flip, by R&D Systems (1 mentions) Peroxidase labelled goat anti rabbit and goat anti mouse, by Agilent Technologies (1 mentions) Gapdh, by Santa Cruz Biotechnology (1 mentions) Control sirna, by Santa Cruz Biotechnology (1 mentions) Lipofectamine 2000, by Thermo Fisher Scientific (1 mentions) Pcdna3.1 plasmid, by Thermo Fisher Scientific (1 mentions) Control sirna, by Thermo Fisher Scientific (1 mentions) Mir nc, by Genechem (1 mentions) P akt ser473, by Cell Signaling Technology (1 mentions) C flip, by Cell Signaling Technology (1 mentions) Ciap2, by Abcam (1 mentions) Mcl 1, by Cell Signaling Technology (1 mentions) β actin, by Cell Signaling Technology (1 mentions)

Spelling variants of this product

Anti-c-FLIP (2 citations)

7 protocols using c flip

Investigating FasL-Induced Apoptosis in hDPSCs

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In order to investigate the effects triggered by human FasL rc on hDPSCs at different concentrations, hDPSCs were processed for Western Blot analysis, as detailed above. The expression of FasL, Fas, Caspase 8 (Cell Signaling Technology, Trask Lane Danvers, MA, United States), c-FLIP (R&D systems, McKinley Place NE, Minneapolis, MN, United States), FADD (mouse anti-FADD ab; Santa Cruz Biotechnology, Dallas, TX, United States) was evaluated in hDPSCs after exposure to 0.1 ng/ml, 0.5 ng/ml FasL rc and to 0.5 ng/ml FasL rc + 500 ng/ml FasL inb for 24 h. To this regard, hDPSCs exposed to 1 μM Staurosporine were used as positive control of apoptosis. Densitometry analysis was performed as described earlier.
Furthermore, the expression of c-FLIP was also evaluated in hDPSCs after exposure to FasL rc 0.5 ng/ml and to FasL rc 0.5 ng/ml + FasL inb 500 ng/ml, respectively, by immunofluorescence analysis with rabbit anti-c-FLIP ab (Santa Cruz Biotechnology, Dallas, TX, United States). Immunolabeling intensity of c-FLIP expression in both experimental groups was evaluated by pseudocolor analysis: blue to white arrays the colors in a spectrum with blue assigned to a lower value than white (Carnevale et al., 2017 (link)).

Pisciotta A., Bertani G., Bertoni L., Di Tinco R., De Biasi S., Vallarola A., Pignatti E., Tupler R., Salvarani C., de Pol A, & Carnevale G. (2020). Modulation of Cell Death and Promotion of Chondrogenic Differentiation by Fas/FasL in Human Dental Pulp Stem Cells (hDPSCs). Frontiers in Cell and Developmental Biology, 8, 279.

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Comprehensive Western Blotting for Apoptosis Signaling

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For Western blotting, total protein extracts were obtained in cell lysis buffer containing 150 mM NaCl, 1 mM EDTA, 1% NP-40, 50 mM Tris (pH 8.0), as well as phosphatase and protease inhibitors. Following SDS polyacrylamide gel electrophoresis, proteins were blotted on nitrocellulose membranes.
Primary antibodies of Cell Signaling (Danvers, MA, USA): caspase-3 (9662, rabbit, 1:1000), cleaved caspase-3 (9664, rabbit, 1:1000), caspase-8 (9746, mouse, 1:1000), caspase-9 (9502, rabbit, 1:1000), XIAP (2042, rabbit, 1:1000). Primary antibodies of Santa Cruz Biotech (Dallas, TX, USA): c-FLIP (sc-5276, mouse, 1:500), p21 (sc-6246, mouse, 1:500), p53 (sc-126, mouse, 1:500), GAPDH (sc-32233, mouse, 1:1000). The antibody for PKCδ (PA587443, rabbit polyclonal, 1:1000) was from Thermo Fisher Scientific (Hennigsdorf, Germany). As secondary antibodies, peroxidase-labelled goat anti-rabbit and goat anti-mouse (Dako, Hamburg, Germany; 1:5000) were used.

Sumarni U., Reidel U, & Eberle J. (2021). Targeting Cutaneous T-Cell Lymphoma Cells by Ingenol Mebutate (PEP005) Correlates with PKCδ Activation, ROS Induction as Well as Downregulation of XIAP and c-FLIP. Cells, 10(5), 987.

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Overexpression and Silencing of c-FLIP

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The open reading frame of c-FLIP was amplified and ligated into pcDNA3.1 plasmid (Thermo Fisher Scientific). c-FLIP and control siRNA were purchased from Santa Cruz Biotechnology (Dallas, TX, USA). For transfection, c-FLIP plasmid (2 μg/mL), miR-382 (5′-AAUCAUUCACGGACAACACUU-3′, 50 pmol/mL, GeneChem), negative control oligonucleotide (miR-NC, 5′-CGACAACAUGAUAUAACUCUC-3′, 50 pmol/mL, GeneChem), c-FLIP, and control siRNA (50 pmol/mL) were transfected into the HCC cell lines by using lipofectamine 2000 (Thermo Fisher Scientific), according to the manufacturer’s protocol.

Chen Z., Zheng Z., Feng L., Huo Z., Huang L., Fu M., Chen Q., Ke Y., Yang J, & Hou B. (2020). Overexpression of miR-382 Sensitizes Hepatocellular Carcinoma Cells to γδ T Cells by Inhibiting the Expression of c-FLIP. Molecular Therapy Oncolytics, 18, 467-475.

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Apoptosis Pathway Protein Analysis

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Western blot analyses were performed as described previously [25 ] using the following antibodies: caspase-8, cFLIP, caspase-9, XIAP, Bim, caspase-3, PTEN, p-PTEN (Ser380/Thr382/383), PARP, p-AKT (Ser-473), AKT, β-actin, MCL-1 (all from Cell Signaling, Beverly, MA), cIAP-2 (Epitomics, Burlingame, CA, USA), cIAP-1, survivin (both from R&D Systems), Noxa, and cFLIP (Santa Cruz Biotechnology).

Wang H., Yang S., Zhou H., Sun M., Du L., Wei M., Luo M., Huang J., Deng H., Feng Y., Huang J, & Zhou Y. (2015). Aloperine executes antitumor effects against multiple myeloma through dual apoptotic mechanisms. Journal of Hematology & Oncology, 8, 26.

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Medicarpin Synthesis and Cell Assays

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Medicarpin (Med), a naturally occurring phytoalexin was synthesized in gram scale at the medicinal process chemistry division of the CSIR-Central Drug Research Institute, India as per a standardized procedure.^{45 (link)} The Med stock (20 mM in DMSO, stored at −20°C) solution was diluted in cell culture media for experimental use. The Super killer TRAIL/Apo2L and the antagonistic antibodies against DR4 (HS101) and DR5 (HS201) were purchased from Alexis Biosciences (San Diego, CA, USA). The primary antibodies against DR4, c-FLIP, Bid, tBid, Cytochrome C, Smac/Diablo, and β-actin were purchased from Santa Cruz Biotechnology, Inc. (Santa Cruz, CA, USA), while the antibodies against DR5, Survivin, CHOP, XIAP, JNK, p-JNK, Bip, eIF2α, p-eIF2α, cleaved caspase-8, cleaved caspase-9, cleaved caspase-3, and cleaved caspase-7 were purchased from Cell Signaling Technology (Boston, MA, USA). Primary antibodies against Bcl-2 and Bax and the 7AAD/Annexin-based cell death assay kit were purchased from BD Biosciences (San Jose, CA, USA). All the other biochemicals were from Sigma (St Louis, MO, USA) unless otherwise stated.

Trivedi R., Maurya R, & Mishra D.P. (2014). Medicarpin, a legume phytoalexin sensitizes myeloid leukemia cells to TRAIL-induced apoptosis through the induction of DR5 and activation of the ROS-JNK-CHOP pathway. Cell Death & Disease, 5(10), e1465-.

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Protein Expression Analysis in Apoptosis

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The cells were washed twice with PBS at 4°C and lysed on ice in RIPA lysis buffer
containing 50 mM tris(hydroxymethyl) aminomethane (Tris)–HCl, pH 7.4, 1% NP-40,
150 mM NaCl, 0.25% Na-deoxycholate, 1 mM Na₃VO₄, and 1 mM NaF and 2
mM phenylmethylsulfonyl fluoride, 2 mM EDTA, 10 µg/mL pepstatin, and 10
µg/mL leupeptin. The lysates were centrifuged at 12,000 rpm for 20 min at
4°C, and then the supernatants were collected for bicinchoninic acid protein
assay. Total proteins (30 µg) were separated by 12% sodium dodecyl
sulfate–polyacrylamide gel electrophoresis and then transferred to polyvinylidene
fluoride membrane. The membranes were incubated with primary antibodies for cleaved PARP,
Bcl-2, Mcl-1, Bcl-xl, c-FLIP, CIAP1, XIAP, p53, NQO1, and β-actin, which were
purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA), at 4°C overnight,
washed, and then incubated with horseradish peroxidase-conjugated secondary antibodies
(Santa Cruz Biotechnology) at 37°C for 1 h. The membranes were washed and detected
using enhanced chemiluminescence detection system according to the manufacturer’s
protocols.

Zhao X.Z, & Wu X.H. (2018). A small compound spindlactone A sensitizes human endometrial cancer cells to TRAIL-induced apoptosis via the inhibition of NAD(P)H dehydrogenase quinone 1. OncoTargets and therapy, 11, 3609-3617.

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Hinokiflavone Induces Apoptosis Signaling

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Hinokiflavone (HF) with purity >98% was purchased from Chengdu Herb purify Co., Ltd., batch number: B‐051‐180730. A stock solution of HF at 200 mmol/L concentration was prepared in DMSO (Sigma) and stored at −20°C. Broad‐spectrum caspase inhibitor (z‐VAD‐FMK), caspase‐3 specific inhibitor (z‐DEVD‐FMK), caspase‐9 specific inhibitor (z‐LEHD‐FMK), JNK inhibitor (SP600125) and p38 inhibitor (SB202190) were procured from MedChemExpress. Dulbecco's modified Eagle's medium (DMEM), foetal bovine serum (FBS), penicillin‐streptomycin, phosphate buffered saline (PBS) and 0.25% trypsin were obtained from Gibco/BRL. The primary antibodies such as CDK4, CDK6, cyclin D1, CDK2, cyclin E, p21^Cip1, p53, p‐p53 Ser15, cleaved caspase‐3, cleaved caspase‐9, cleaved poly (ADP‐ribose) polymerase (c‐PARP), B cell lymphoma 2 (Bcl‐2), Bcl‐2 associated x (Bax), cytochrome c (cyt c), p‐p38, p38, p‐JNK, JNK, c‐Jun, p‐IKBα, IKBα, p‐p65, p65 and glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH) were provided by Cell Signaling Technology. The antibodies IAP1/2, XIAP were provided by Abcam, and c‐FLIP was provided by santa cruz biotechnology.

Mu W., Cheng X., Zhang X., Liu Y., Lv Q., Liu G., Zhang J, & Li X. (2020). Hinokiflavone induces apoptosis via activating mitochondrial ROS/JNK/caspase pathway and inhibiting NF‐κB activity in hepatocellular carcinoma. Journal of Cellular and Molecular Medicine, 24(14), 8151-8165.

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