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Safety Information

MAB5490

Sigma-Aldrich

Anti-Huntingtin Antibody, a.a. 115-129

ascites fluid, Chemicon®

Synonym(s):

Anti-HD

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About This Item

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

biological source

mouse

antibody form

ascites fluid

antibody product type

primary antibodies

clone

monoclonal

species reactivity

human

manufacturer/tradename

Chemicon®

technique(s)

ELISA: suitable
immunocytochemistry: suitable
immunohistochemistry: suitable
western blot: suitable

isotype

IgG1κ

NCBI accession no.

NM_002111.6

UniProt accession no.

P42858

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

human ... HTT(3064) , SLC6A4(6532)

Specificity

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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Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

MAB5490:

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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Ellen Sapp et al.
The Journal of biological chemistry, 287(16), 13487-13499 (2012-03-01)
Huntington disease (HD) is caused by polyglutamine expansion in the N terminus of huntingtin (htt). Analysis of human postmortem brain lysates by SDS-PAGE and Western blot reveals htt as full-length and fragmented. Here we used Blue Native PAGE (BNP) and
N-terminal proteolysis of full-length mutant huntingtin in an inducible PC12 cell model of Huntington's disease.
Tamara Ratovitski,Masayuki Nakamura,James D'Ambola,Ekaterine Chighladze,Yideng Liang et al.
Cell Cycle null
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
Astrid Lunkes et al.
Molecular cell, 10(2), 259-269 (2002-08-23)
Proteolytic processing of mutant huntingtin (mhtt) is regarded as a key event in the pathogenesis of Huntington's disease (HD). Mhtt fragments containing a polyglutamine expansion form intracellular inclusions and are more cytotoxic than full-length mhtt. Here, we report that two
Jacqueline Gire O'Rourke et al.
Cell reports, 4(2), 362-375 (2013-07-23)
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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