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Read our guarantee »Products:Neuroscience >> Neurology process >> Neurodegenerative disease >> Huntington's disease
Anti-Huntingtin antibody
See all Huntingtin products (13) ...
Mouse polyclonal to Huntingtin
Reacts with
Fruit fly (Drosophila melanogaster)
Vector coding for a partial recombinant fusion protein, corresponding to internal sequence amino acids 325-425 of Fruit fly (Drosophila melanogaster) Huntingtin. Target sequence used to make antibody: SDGQCSQSLG QSLRQLLCNQ QLQHNEYLRR RKSLKNQIFQ LKNYEVATSQ HQLEDEDENE DVDELVVGAT AMQMKKNSNA KLQQAKCREQ QQHQHQQQLE.
SDGQCSQSLG QSLRQLLCNQ QLQHNEYLRR RKSLKNQIFQ LKNYEVATSQ HQLEDEDENE DVDELVVGAT AMQMKKNSNA KLQQAKCREQ QQHQHQQQLE
Liquid
Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
Preservative: None
Constituents: 50% Glycerol, Whole serum
Whole antiserum
This antibody was raised by a genetic immunization technique. Genetic immunization can be used to generate antibodies by directly delivering antigen-coding DNA into the animal, rather than injecting a protein or peptide (Tang et al. PubMed: 1545867; Chambers and Johnston PubMed 12910245; Barry and Johnston PubMed: 9234514). The animal's cells produce the protein, which stimulates the animal's immune system to produce antibodies against that particular protein. A vector coding for a partial fusion protein was used for genetic immunisation of a mouse and the resulting serum was tested in Western blot against an E.coli lysate containing that partial fusion protein. Genetic immunization offers enormous advantages over the traditional protein-based immunization method. DNA is faster, cheaper and easier to produce and can be produced by standard techniques readily amenable to automation. Furthermore, the antibodies generated by genetic immunization are usually of superior quality with regard to specificity, affinity and recognizing the native protein.
Polyclonal
IgG
Neuroscience >> Neurology process >> Neurodegenerative disease >> Huntington's disease
Our Abpromise guarantee covers the use of ab43553 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
WB: 1/1000. Predicted molecular weight: 395 kDa.
This antibody has been tested in Western blot against an E.coli lysate containing the partial recombinant fusion protein used as an immunogen. We have no data on detection of endogenous protein.
Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
May play a role in microtubule-mediated transport or vesicle function.
Expressed in the brain cortex (at protein level). Widely expressed with the highest level of expression in the brain (nerve fibers, varicosities, and nerve endings). In the brain, the regions where it can be mainly found are the cerebellar cortex, the neocortex, the striatum, and the hippocampal formation.
Defects in HTT are the cause of Huntington disease (HD) [MIM:143100]. HD is an autosomal dominant neurodegenerative disorder characterized by involuntary movements (chorea), general motor impairment, psychiatric disorders and dementia. Onset of the disease occurs usually in the third or fourth decade of life and symptoms progressively worsen leading to death in 10 to 20 years. Onset and clinical course depend on the degree of poly-Gln repeat expansion, longer expansions resulting in earlier onset and more severe clinical manifestations. HD affects 1 in 10,000 individuals of European origin. Neuropathology of Huntington disease displays a distinctive pattern with loss of neurons, especially in the caudate and putamen (striatum).
Belongs to the huntingtin family.
Contains 10 HEAT repeats.
The N-terminal Gln-rich and Pro-rich domain has great conformational flexibility and is likely to exist in a fluctuating equilibrium of alpha-helical, random coil, and extended conformations.
Cleaved by apopain downstream of the polyglutamine stretch. The resulting N-terminal fragment is cytotoxic and provokes apoptosis.
Forms with expanded polyglutamine expansion are specifically ubiquitinated by SYVN1, which promotes their proteasomal degradation.
Cytoplasm. Nucleus. The mutant Huntingtin protein colocalizes with AKAP8L in the nuclear matrix of Huntington's disease neurons.
Target information above from: UniProt accessionP42858
The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010).
ab43553 has not yet been referenced specifically in any publications.
Publishing research using ab43553? Please let us know so that we can cite the reference in this datasheet
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