Abcam, ab135398, Anti-GAL4 antibody [14-7E10G10]

Size: 100µg
Mouse Monoclonal GAL4 antibody. Suitable for WB and reacts with Saccharomyces cerevisiae samples. Cited in 3 publications.
Key facts
Host species:Mouse,
Clonality:Monoclonal,
Clone number:14-7E10G10,
Isotype:IgG2b,
Carrier free:No,
Reacts with:Saccharomyces cerevisiae,
Applications:WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:The exact immunogen used to generate this antibody is proprietary information.

Product details:
The GAL4 Activation Domain monoclonal antibody binds specifically to the AD of the yeast GAL4 protein. This antibody is useful for verifying the expression and correct molecular weight of fusion proteins containing GAL4 AD as the fusion partner in two hybrid studies. The activation domain is typically used in a two-hybrid experiment as the fusion partner for a library of cDNA clones to screen against a protein of interest fused to a DNA-binding domain. Gal4is a positive regulator for the gene expression of the galactose-induced genes such as GAL1, GAL2, GAL7, GAL10, and MEL1 which encode for the enzymes used to convert galactose to glucose. It recognizes a 17 base pair sequence in (5'-CGGRNNRCYNYNCNCCG-3') the upstream activating sequence (UAS-G) of these genes.
Want a custom formulation?
This antibody clone is manufactured by Abcam. If you require a custom buffer formulation or conjugation for your experiments, please contact orders@abcam.com
Compatibility
This product is compatible with the Maxpar
Antibody Labeling Kit from Fluidigm, without the need for antibody preparation. Maxpar
is a trademark of Fluidigm Canada Inc.

Properties and Storage Information:
Form-Liquid, Purification technique-Precipitation Ammonium Sulphate, Storage buffer-pH: 7.5Preservative: 0.02% Sodium azide, Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions-+4°C

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
GAL4 also known as a transcription factor is an important protein in yeast. It plays a critical role in regulating the transcription of genes involved in galactose metabolism. The GAL4 protein has a mass of approximately 881 amino acids and is mainly expressed in the nucleus of yeast cells. Common parts of GAL4 include the GAL4 DBD (DNA-binding domain) and GAL4 AD (activation domain) which are critical for its function. Although similar sounding GAL4 should not be confused with galectin-4 or galectin 4 which are different proteins.
Biological function summary
The GAL4 transcription factor functions as a major regulator of galactose-responsive genes. It acts as part of a complex binding with its DNA target sites to initiate transcription of GAL genes like GAL1 GAL7 and GAL10. GAL4 protein recruits transcriptional machinery through its activation domain working alongside other factors to turn on specific gene expression in response to the presence of galactose. This capacity for gene regulation underlines its essential role in sugar metabolism in yeast.
Pathways
GAL4 is intimately involved in the GAL gene regulatory pathway that manages the cellular response to galactose. In this pathway proteins such as GAL80 inhibit GAL4 function under non-inducing conditions. However in the presence of galactose GAL3 binds and neutralizes GAL80 liberating GAL4 to activate gene expression. This system exemplifies a dynamic interaction in yeast allowing precise gene regulation in accordance with sugar availability.
While GAL4 is specifically a yeast protein and does not directly relate to human diseases its functional analogs and concepts have implications in genetic research and synthetic biology. For example GAL4 system is widely used in Drosophila and other model organisms to study gene expression patterns and related disorders. This system compared with mammalian transcription factors provides a foundational methodology for exploring genetic regulation mechanisms and potential implications in understanding metabolic disorders.