HDAC6 is a histone deacetylase that associates with polyubiquitinated protein and also functions as a tubulin deacetylase. Additionally, HDAC6 is known to rescue neurodegeneration. It can also function as a mechanistic link between autophagy and ubiquitin-proteasome system during protein degradation. Rabbit Anti-HDAC6 antibody recognizes canine, human, rat, bovine, and mouse HDAC6.
Immunogen
Synthetic peptide directed towards the N terminal region of human HDAC6
Application
Rabbit Anti-HDAC6 antibody can be used for western blot applications at 1.0μg/ml.
Biochem/physiol Actions
Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein belongs to class II of the histone deacetylase/acuc/apha family. It contains an internal duplication of two catalytic domains which appear to function independently of each other. This protein possesses histone deacetylase activity and represses transcription.
Sequence
Synthetic peptide located within the following region: VGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQ
Physical form
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
A prominent feature of late-onset neurodegenerative diseases is accumulation of misfolded protein in vulnerable neurons. When levels of misfolded protein overwhelm degradative pathways, the result is cellular toxicity and neurodegeneration. Cellular mechanisms for degrading misfolded protein include the ubiquitin-proteasome system
Reversible acetylation of alpha-tubulin has been implicated in regulating microtubule stability and function. The distribution of acetylated alpha-tubulin is tightly controlled and stereotypic. Acetylated alpha-tubulin is most abundant in stable microtubules but is absent from dynamic cellular structures such as
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