Protein extracts were prepared as described previously [4 (link)]. Following Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and electroblotting, membranes were incubated with the following primary antibodies: anti-p21, anti-p27, anti-p16, CDK4, CDK6, cycline D1, cycline E, cycline B1, Light Chain3 (LC)3 AB I/II, Atg4B, p62, Atg3, Atg5, Atg7, Atg12, beclin-1, full length and cleaved caspases 3, 7, 8, 9, (phospho-)p38, (phospho-)p44/42, (phospho-)rb, (phospho-)akt, and anti-tubulin (Cell Signaling, Danvers, MA, USA). Primary antibody application was followed by incubation with horseradish peroxidase-conjugated secondary antibodies (anti-mouse and anti-rabbit IgG, Amersham, Uppsala, Sweden; anti-goat, Dako, Glostrup, Denmark). Blots were developed using an enhanced chemiluminescence detection system (ECL) (Amersham) according to the manufacturer’s instructions.
Anti mouse and anti rabbit igg
Manufactured by Cytiva
Sourced in Sweden
Anti-mouse and anti-rabbit IgG are secondary antibodies used in various immunological techniques. They are designed to bind to the primary antibodies that were raised against mouse or rabbit antigens, allowing for the detection and visualization of target proteins or biomolecules in samples.
Automatically generated - may contain errors
Lab products found in correlation
Phospho akt, by Cell Signaling Technology (2 mentions)
Anti tubulin, by Cell Signaling Technology (2 mentions)
Anti p27, by Cell Signaling Technology (2 mentions)
Anti p21, by Cell Signaling Technology (2 mentions)
Phospho p38, by Cell Signaling Technology (1 mentions)
Anti p16, by Cell Signaling Technology (1 mentions)
Phospho rb, by Cell Signaling Technology (1 mentions)
Anti cleaved caspase 3, by Cell Signaling Technology (1 mentions)
Anti cleaved caspase 9, by Cell Signaling Technology (1 mentions)
Anti cleaved caspase 7, by Cell Signaling Technology (1 mentions)
Anti p53, by Cell Signaling Technology (1 mentions)
Anti cdk6, by Santa Cruz Biotechnology (1 mentions)
Enhanced chemiluminescence detection system, by Cytiva (1 mentions)
Anti ciap1, by Cell Signaling Technology (1 mentions)
Anti ciap2, by Cell Signaling Technology (1 mentions)
Anti cdk4, by Santa Cruz Biotechnology (1 mentions)
Anti cyclin a, by Santa Cruz Biotechnology (1 mentions)
Anti cyclin d1, by Santa Cruz Biotechnology (1 mentions)
Cleaved parp, by Cell Signaling Technology (1 mentions)
Bcl2 associated x (bax), by Cell Signaling Technology (1 mentions)
5 protocols using anti mouse and anti rabbit igg
1
Protein Expression Analysis Protocol
2
Western Blot Analysis of Cell Signaling
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Protein extracts were prepared as described previously [13 (link)]. Following SDS-PAGE and electroblotting, membranes were incubated with the following primary antibodies: anti-p21 (#2947, Cell Signaling, Danvers, MA, USA), anti-p27 (#3686, Cell Signaling, Danvers, MA, USA), anti-p53 (#9282, Cell Signaling, Danvers, MA, USA), anti-cleaved caspase 3 (#9661, Cell Signaling, Danvers, MA, USA), anti-cleaved caspase 7 (#9491, Cell Signaling, Danvers, MA, USA), anti-cleaved caspase 9 (#9501, Cell Signaling, Danvers, MA, USA), anti-cIAP-1 (#4952, Cell Signaling, Danvers, MA, USA), anti-cIAP-2 (#3130, Cell Signaling, Danvers, MA, USA), anti-tubulin (#3873, Cell Signaling, Danvers, MA, USA), anti-cyclin A (sc-271645, Santa Cruz, CA, USA), anti-cyclin D1 (sc-718, Santa Cruz, CA, USA), anti-CDK4 (sc-70831, Santa Cruz, CA, USA) and anti-CDK6 (sc-177, Santa Cruz, CA, USA). Primary antibody application was followed by incubation with horseradish peroxidase-conjugated secondary antibodies (anti-mouse and anti-rabbit IgG, Amersham, Uppsala, Sweden; anti-goat, Dako, Glostrup, Denmark). Blots were developed using an enhanced chemiluminescence detection system (Amersham) according to the manufacturer’s instructions.
3
D2O-Treated Cell Protein Analysis
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Protein extracts of cells treated with D2O for 48 hrs were separated by SDS-polyacrylamide gels and electroblotted as described.12 (link) Membranes were incubated with the following primary antibodies: Bcl-2, Bcl-XL, Bax, AIF, cleaved PARP, surviving (all purchased from Cell Signaling, Frankfurt, Germany) and actin (Heidelberg, Santa Cruz). Primary antibody application was followed by incubation with horseradish peroxidase-conjugated secondary antibodies (anti-mouse and anti-rabbit IgG, Amersham, Uppsala, Sweden). Blots were developed using an enhanced chemiluminescence detection system (ECL) (Amersham) according to the manufacturer’s instructions.
4
Quantitative Western Blot Analysis
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Whole cell protein was prepared as previously described [23 (link)]. Membranes were incubated with the indicated primary antibodies. Antibodies were as follows: anti-ICAM-1 (SC-107; 15.2) from Santa Cruz (Heidelberg, Germany) and anti-Tubulinα Ab-2 (DM1A) from LabVision (Fremont, CA, USA). Primary antibody application was followed by incubation with horseradish peroxidase-conjugated secondary antibodies (anti-mouse and anti-rabbit IgG, Amersham, Uppsala, Sweden; anti-goat, Dako, Glostrup, Denmark). Blots were developed using an enhanced chemiluminescence detection system (ECL) (Amersham, Uppsala, Sweden), according to the manufacturer’s instructions. Densitometry was used to quantify band intensities using ImageJ (v1.29 s). Optical densities of the bands were corrected for loading differences based on corresponding control bands.
5
Quantification of Signaling Protein Levels
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The protein extracts were prepared as described previously [14 (link)]. Following SDS-PAGE and electroblotting, the membranes were incubated with the following primary antibodies: p65, phospho-p65 (Ser536), IκBα p38, p42/44, JNK, pospho-p38, phospho-p42/44, phospho-JNK, Phospho-Akt, Akt and tubulin (Cell Signaling, Danvers, MA, USA); Laminin A/B (Santa Cruz, Dallas, Texas, USA); SP1 (Sigma-Aldrich, St. Louis, MO, USA). Primary antibody application was followed by incubation with horseradish peroxidase-conjugated secondary antibodies (anti-mouse and anti-rabbit IgG, Amersham, Uppsala, Sweden; anti-goat, Dako, Glostrup, Denmark). The blots were visualized using an enhanced chemiluminescence detection system (ECL) (Amersham, Freiburg, Germany) according to the manufacturer’s instructions. Densitometry was used to quantify band intensities using ImageJ (v1.29 s). Optical densities of the bands were corrected for loading differences based on corresponding control bands.
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