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MAB2170

Sigma-Aldrich

Anti-Huntingtin Protein Antibody, a.a. 1247-1646, clone HU-4E6

ascites fluid, clone HU-4E6, Chemicon®

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

ascites fluid

antibody product type

primary antibodies

clone

HU-4E6, monoclonal

species reactivity

mouse, human

manufacturer/tradename

Chemicon®

technique(s)

ELISA: suitable
immunocytochemistry: suitable
immunohistochemistry: suitable (paraffin)
immunoprecipitation (IP): suitable
western blot: suitable

isotype

IgG2b

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

Specificity

Huntingtin Protein. No detectable cross reactivity with other proteins by Western blot.

Immunogen

Epitope: a.a. 1247-1646
Huntingtin fragment from aa 1247 to 1646 as a fusion protein

Application

Detect Huntingtin Protein using this Anti-Huntingtin Protein Antibody, a.a. 1247-1646, clone HU-4E6 validated for use in ELISA, IP, WB, IC, IH(P).
ELISA: 1:500-1:5,000

Western blot (recombinant protein, not suitable for the natural Huntingtin) : 1:500-1:5,000

Immunohistochemistry on frozen and microwave oven treated paraffin sections (human): 1:500-1:5,000

Immunocytochemistry on transfected cells: 1:500-1:5,000

Immunoprecipitation: 1:500-1:5,000

Optimal working dilutions must be determined by the end user.
Research Category
Neuroscience
Research Sub Category
Neurodegenerative Diseases

Physical form

Ascites fluid. Liquid, does not contain any preservative.

Storage and Stability

Maintain at -20°C in undiluted aliquots up to 12 months after date of receipt. Avoid repeated freeze/thaw cycles.

During shipment, small volumes of antibody will occasionally become entrapped in the seal of the product vial. For antibodies with volumes of 200 μl or less, we recommend gently tapping the vial on a hard surface or briefly centrifuging the vial in a tabletop centrifuge to dislodge any liquid in the container′s cap.

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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Storage Class Code

10 - Combustible liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Anjalika Chongtham et al.
Human molecular genetics, 29(4), 674-688 (2020-01-17)
Huntington's disease (HD) is caused by an expansion of a poly glutamine (polyQ) stretch in the huntingtin protein (HTT) that is necessary to cause pathology and formation of HTT aggregates. Here we ask whether expanded polyQ is sufficient to cause
Wei Li et al.
The Journal of biological chemistry, 281(23), 15916-15922 (2006-04-06)
Huntington disease is an inherited neurodegenerative disorder that is caused by expanded CAG trinucleotide repeats, resulting in a polyglutamine stretch of >37 on the N terminus of the protein huntingtin (htt). htt is a large (347 kDa), ubiquitously expressed protein.
Baehyun Shin et al.
Molecular therapy. Nucleic acids, 11, 416-428 (2018-06-03)
The CAG repeat expansion that elongates the polyglutamine tract in huntingtin is the root genetic cause of Huntington's disease (HD), a debilitating neurodegenerative disorder. This seemingly slight change to the primary amino acid sequence alters the physical structure of the
Melanie Alpaugh et al.
Molecular therapy : the journal of the American Society of Gene Therapy, 30(4), 1500-1522 (2022-01-21)
Huntington's disease is classically described as a neurodegenerative disorder of monogenic aetiology. The disease is characterized by an abnormal polyglutamine expansion in the huntingtin gene, which drives the toxicity of the mutated form of the protein. However, accumulation of the
Maria Masnata et al.
Acta neuropathologica, 137(6), 981-1001 (2019-02-23)
In recent years, evidence has accumulated to suggest that mutant huntingtin protein (mHTT) can spread into healthy tissue in a prion-like fashion. This theory, however, remains controversial. To fully address this concept and to understand the possible consequences of mHTT spreading

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