Log In Sign up
The largest database of trusted experimental protocols

Antibodies against c myc

Manufactured by Santa Cruz Biotechnology
Visit Supplier
Sourced in United States

Antibodies against c-myc are a type of laboratory reagent used in various research applications. These antibodies are designed to specifically bind to and detect the c-myc protein, which is a transcription factor involved in the regulation of gene expression. The core function of these antibodies is to provide a tool for the identification, quantification, and analysis of the c-myc protein in biological samples.

Automatically generated - may contain errors

Lab products found in correlation

Rac1 activation assay kit, by Merck Group (2 mentions) β actin, by Merck Group (2 mentions) Protein a g magnetic beads, by Merck Group (1 mentions)

Spelling variants of this product

C-Myc (386 citations) Primary antibodies against c‐Myc (2 citations)

4 protocols using antibodies against c myc

1

Quantifying Active Rac1 Levels

Check if the same lab product or an alternative is used in the 5 most similar protocols
Transfected hEK293 cells were harvested when they reached ∼95% confluency. Active Rac1 levels were assessed using a Rac1 Activation Assay Kit (Millipore, Billerica, Massachusetts) following the manufacturers' protocol with normalization to total Rac1 as described previously17 (link). Antibodies against c-myc (1:500, Santa Cruz Biotechnology, Dallas, Texas) and β-actin (1:4000, Sigma-Aldrich) were used to control for levels of exogenously expressed protein. Blots were then analyzed with ImageJ68 (link).
Russell T.A., Blizinsky K.D., Cobia D.J., Cahill M., Xie Z., Sweet R.A., Duan J., Gejman P.V., Wang L., Csernansky J.G, & Penzes P. (2014). A sequence variant in human KALRN impairs protein function and coincides with reduced cortical thickness. Nature communications, 5, 4858.
+ Open protocol
+ Expand
2

Yeast Iron Metabolism Assays

Check if the same lab product or an alternative is used in the 5 most similar protocols
Details on yeast strains, media, cloning procedures and vectors21 22 (link) as well as on generation of mutant allele and construction of mutant strains23–25 (link) are reported in the online supplementary dataComplex II (succinate dehydrogenase (SDH)) and complex IV (cytochrome c oxidase (COX)) specific activities were measured on a mitochondrial-enriched fraction prepared as previously described.26 27 (link) Aconitase activity was measured in whole-cell extracts.28 (link) In vivo radiolabelling of yeast cells with 55FeCl3 (ICN) and measurement of 55Fe-incorporation into Fe-S proteins by immunoprecipitation and scintillation counting were performed as described.29 (link) Antibodies against c-Myc were obtained from Santa-Cruz. The green fluorescent protein (GFP) based reporter assay for determination of FET3 promoter strength was described previously.29 (link) The iron content was determined by a colorimetric assay, essentially as described before.30 31 (link)
Legati A., Reyes A., Ceccatelli Berti C., Stehling O., Marchet S., Lamperti C., Ferrari A., Robinson A.J., Mühlenhoff U., Lill R., Zeviani M., Goffrini P, & Ghezzi D. (2017). A novel de novo dominant mutation in ISCU associated with mitochondrial myopathy. Journal of Medical Genetics, 54(12), 815-824.
+ Open protocol
+ Expand
3

Quantifying Active Rac1 Levels

Check if the same lab product or an alternative is used in the 5 most similar protocols
Transfected hEK293 cells were harvested when they reached ∼95% confluency. Active Rac1 levels were assessed using a Rac1 Activation Assay Kit (Millipore, Billerica, Massachusetts) following the manufacturers' protocol with normalization to total Rac1 as described previously17 (link). Antibodies against c-myc (1:500, Santa Cruz Biotechnology, Dallas, Texas) and β-actin (1:4000, Sigma-Aldrich) were used to control for levels of exogenously expressed protein. Blots were then analyzed with ImageJ68 (link).
Russell T.A., Blizinsky K.D., Cobia D.J., Cahill M., Xie Z., Sweet R.A., Duan J., Gejman P.V., Wang L., Csernansky J.G, & Penzes P. (2014). A sequence variant in human KALRN impairs protein function and coincides with reduced cortical thickness. Nature communications, 5, 4858.
+ Open protocol
+ Expand
4

ChIP Assay for c-Myc Binding to PDAP1

Cited 1 time
Check if the same lab product or an alternative is used in the 5 most similar protocols
The binding of c‐Myc to the PDAP1 promoter was measured using a ChIP assay as previously described [19 (link)]. HCT‐8 cells were fixed with 1% formaldehyde and treated with 1 mol/L glycine. After washing with ice‐cold PBS, cells were scraped off and lysed with 1% SDS lysis buffer supplemented with a protease inhibitor cocktail on ice. The lysed cells were sonicated to shear the chromatin DNA to an optimal size of approximately 200 bp‐1000 bp. Sheared chromatin DNA was immunoprecipitated using antibodies against c‐Myc (Santa Cruz Biotechnology, Dallas, TX, USA). Equal amounts of IgG (Santa Cruz Biotechnology) served as negative controls. The immunoprecipitate was then incubated with protein A/G magnetic beads (Millipore, Boston, MA, USA) and pulled down on a magnetic stand. After washing, reverse crosslinking was performed in 5 mol/L NaCl at 65°C overnight. Contaminating RNA was cleaned with ribonuclease A, and the protein was digested with proteinase K. Finally, the sheared DNA recovered from reverse crosslinking was extracted using a DNA extraction kit for further analysis with quantitative polymerase chain reaction (qPCR). The same amount of sheared DNA without antibody precipitation after reverse crosslinking was used as the input control.
Cui H., Wei W., Qian M., Tian R., Fu X., Li H., Nan G., Yang T., Lin P., Chen X., Zhu Y., Wang B., Sun X., Dou J., Jiang J., Li L., Wang S, & Chen Z. (2022). PDGFA‐associated protein 1 is a novel target of c‐Myc and contributes to colorectal cancer initiation and progression. Cancer Communications, 42(8), 750-767.
+ 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!