MAB1574
Anti-Polyglutamine-Expansion Diseases Marker Antibody, clone 5TF1-1C2
ascites fluid, clone 5TF1-1C2, Chemicon®
Synonym(s):
Poly-Glu, PolyQ
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
mouse
Quality Level
antibody form
ascites fluid
antibody product type
primary antibodies
clone
5TF1-1C2, monoclonal
species reactivity
human
manufacturer/tradename
Chemicon®
technique(s)
ELISA: suitable
immunocytochemistry: suitable
immunohistochemistry: suitable (paraffin)
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG1κ
shipped in
dry ice
target post-translational modification
unmodified
General description
Huntington’s disease (HD) belongs to a family of polyglutamine diseases, which includes dentatorubralpallidoluysian atrophy (DRPLA), spinobulbar muscular atrophy (SBMA) and spinocerebellar ataxia (SCA) types 1–3, 6, 7 and 17. In these diseases, the non-pathogenic alleles contain fewer than approximately 35 consecutive glutamine repeats and encode a normal polyglutamine domain. In contrast, the pathogenic alleles usually contain 39 or more consecutive glutamine repeats. Higher repeat numbers lead to lower ages of onset. Patients with 40-60 glutamine repeats normally develop disease as adults, whereas patients with more than 60 repeats develop a juvenile onset disease. Each polyglutamine expansion disorder displays characteristic pathology, with neuronal loss evident in specific regions of the brain. HD results from expansions of a glutamine tract in a large cystolic protein known as huntingtin.
Specificity
The epitope of MAB1574 was found to be a homopolymeric glutamine stretch. The original immunogen was the general transcription factor TATA Box-binding protein (TBP) which contains a 38-glns stretch (Lescure et al). Other polyglutamine-containing proteins are recognized by the MAB1574, notably those involved in several human neurodegenerative diseases caused by a CAG repeat expansion, like Huntington′s disease and spinocerebellar ataxia type 2, 3 and 7 (Trottier et al., 1995). Importantly, for proteins involved in these neurodegenerative disorders, MAB1574 showed remarkable property of detecting much better the pathological proteins that contain a polyglutamine expansion (37 glns) than the wild type proteins (Trottier et al., 1995). MAB1574 has been used to identify new neurodegenerative diseases caused by polyglutamine expansion and to help for cloning of the corresponding affected genes (Trottier 1995-1998; Imbert 1996; Stevanin 1996). MAB1574 is also able to detect intracellular inclusions, which is a hallmark of such diseases (Paulson, 1997).
Immunogen
N-terminal part of the human TATA Box Binding Protein (TBP).
Application
Anti-Polyglutamine-Expansion Diseases Marker Antibody, clone 5TF1-1C2 is an antibody against Polyglutamine-Expansion Diseases Marker for use in ELISA, IC, IH(P), IP & WB.
ELISA: 1:1,000-1:20,000
Western Blot: 1:1,000-1:20,000
Immunohistochemistry on frozen and paraffin sections (human tissue): 1:1,000-1:20,000
Immunocytochemistry on transfected cells: 1:1,000-1:20,000 Immunoprecipitation: 1:1,000-1:20,000
Optimal working dilutions must be determined by end user.
Western Blot: 1:1,000-1:20,000
Immunohistochemistry on frozen and paraffin sections (human tissue): 1:1,000-1:20,000
Immunocytochemistry on transfected cells: 1:1,000-1:20,000 Immunoprecipitation: 1:1,000-1:20,000
Optimal working dilutions must be determined by end user.
Research Category
Neuroscience
Neuroscience
Research Sub Category
Neurodegenerative Diseases
Neurodegenerative Diseases
Physical form
Ascites fluid containing no preservatives.
Unpurified
Storage and Stability
Maintain for 1 year at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Analysis Note
Control
Huntigton′s Disease brain
Huntigton′s Disease brain
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
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
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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Find documentation for the products that you have recently purchased in the Document Library.
Changes in key hypothalamic neuropeptide populations in Huntington disease revealed by neuropathological analyses.
Gabery S, Murphy K, Schultz K, Loy CT, McCusker E, Kirik D, Halliday G, Petersen A
Acta neuropathologica null
Muscleblind participates in RNA toxicity of expanded CAG and CUG repeats in Caenorhabditis elegans.
Wang LC, Chen KY, Pan H, Wu CC, Chen PH, Liao YT, Li C, Huang ML, Hsiao KM
Cellular and Molecular Life Sciences null
Testosterone reduction prevents phenotypic expression in a transgenic mouse model of spinal and bulbar muscular atrophy
Katsuno, M. et al.
Neuron, 35, 843-854 (2002)
J Takahashi et al.
Journal of neuropathology and experimental neurology, 60(4), 369-376 (2001-04-18)
Recruitment of polyglutamine-containing proteins into nuclear inclusions (NIs) was investigated in neuronal intranuclear hyaline inclusion disease (NIHID). Some polyglutamine-containing proteins, ataxin-2, ataxin-3, and TATA box binding protein (TBP), as well as unidentified proteins with expanded polyglutamine tracts were recruited into
Neuronal intranuclear inclusions in a new cerebellar tremor/ataxia syndrome among fragile X carriers.
C M Greco, R J Hagerman, F Tassone, A E Chudley, M R Del Bigio, S Jacquemont, M Leehey, P J Hagerman
Brain null
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