Reacts huntingtin protein, amino acids 115-129. The antibody recognizes wild type and mutant huntingtin.
Immunogen
Epitope: a.a. 115-129
Recombinant human huntingtin, amino acids 115-129.
Application
Anti-Huntingtin Antibody, a.a. 115-129 detects level of Huntingtin & has been published & validated for use in ELISA, WB, IC, IH.
Research Category Neuroscience
Research Sub Category Neurodegenerative Diseases
Western blot: 1:500-1:5,000
Immunocytochemistry (1): 1:500-1:5,000
Immunohistochemistry (1,2): 1:500-1:5,000
ELISA: 1:500-1:5,000
Optimal working dilutions must be determined by end user.
Physical form
Ascites fluid. Liquid. Contains no preservative.
Storage and Stability
Maintain at -20°C in undiluted aliquots for up to 6 months after date of receipt. Avoid repeated freeze/thaw cycles.
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
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.
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Quantitative analysis of proteins secreted from the cells poses a challenge due to their low abundance and the interfering presence of a large amount of bovine serum albumin (BSA) in the cell culture media. We established assays for detection of
Cdk5 is a post-mitotic kinase with complex roles in maintaining neuronal health. The various mechanisms by which Cdk5 inhibits and promotes neurodegeneration are still poorly understood. Here, we show that in Drosophila melanogaster Cdk5 regulates basal autophagy, a key mechanism
Ser46 phosphorylation and prolyl-isomerase Pin1-mediated isomerization of p53 are key events in p53-dependent apoptosis induced by mutant huntingtin.
Grison, A; Mantovani, F; Comel, A; Agostoni, E; Gustincich, S; Persichetti, F; Del Sal, G
Proceedings of the National Academy of Sciences of the USA null
Abnormal protein interactions of mutant huntingtin (Htt) triggered by polyglutamine expansion are thought to mediate Huntington's disease (HD) pathogenesis. Here, we explored a functional interaction of Htt with protein arginine methyltransferase 5 (PRMT5), an enzyme mediating symmetrical dimethylation of arginine
A key feature in Huntington disease (HD) is the accumulation of mutant Huntingtin (HTT) protein, which may be regulated by posttranslational modifications. Here, we define the primary sites of SUMO modification in the amino-terminal domain of HTT, show modification downstream of
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