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48-602MAG
Buffer Detection Kit for Magnetic Beads
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Anti-Aldh1L1, clone N103/39 is an antibody targeting the Aldh1L1 protein, validated for use in Immunofluorescence, Immunohistochemistry, and Western Blotting.
More>>Anti-Aldh1L1, clone N103/39 is an antibody targeting the Aldh1L1 protein, validated for use in Immunofluorescence, Immunohistochemistry, and Western Blotting. Less<<
Anti-Aldh1L1 Antibody, clone N103/39: SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
Aldh1L1, also known as 10-formyltetrahydrofolate dehydrogenase (10-FTHFDH), is a multidomain protein that is found in liver cytosol and also serves as a CNS astrocyte marker. Aldh1L1 is comprised of two functionally unrelated domains, an aldehyde dehydrogenase-homologous domain and a folate-binding hydrolase domain. These two domains are thought to be connected by a 100-residue linker. It is known to induce phosphorylation of p53 at Ser6, which is a critical step in stimulating apoptosis.
References
Product Information
Format
Purified
HS Code
3002 15 90
Control
Mouse brain tissue lysate
Presentation
Purified mouse IgG1κ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Anti-Aldh1L1, clone N103/39 is an antibody targeting the Aldh1L1 protein, validated for use in Immunofluorescence, Immunohistochemistry, and Western Blotting.
Key Applications
Immunofluorescence
Immunohistochemistry
Western Blotting
Application Notes
Western Blot Analysis: 0.5 µg/mL from a representative lot detected Aldh1L1 in 10 µg of human brain tissue lysate.
Immunohistochemistry Analysis: A 1:2,000 dilution from a representative lot detected Aldh1L1 rat cerebral cortex tissue and human pons/midbrain tissue.
Immunofluorescence Analysis: A representative lot detected Aldh1L1 in rat cortex and cerebellum tissue.
Biological Information
Immunogen
Recombinant full-length rat Aldh1L1.
Clone
N103/39
Concentration
Please refer to the Certificate of Analysis for the lot-specific concentration.
Host
Mouse
Specificity
This Aldh1L1 monoclonal antibody does not exhibit cross-reactivity toward Aldh1L2.
Evaluated by Western Blot in mouse brain tissue lysate.
Western Blot Analysis: 0.5 µg/mL of this antibody detected Aldh1L1 in 10 µg of mouse brain tissue lysate.
Usage Statement
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.
New α- and γ-synuclein immunopathological lesions in human brain. Surgucheva, I; Newell, KL; Burns, J; Surguchov, A Acta neuropathologica communications
2
132
2014
Several neurodegenerative diseases are classified as proteopathies as they are associated with the aggregation of misfolded proteins. Synucleinopathies are a group of neurodegenerative disorders associated with abnormal deposition of synucleins. α-Synucleinopathies include Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy. Recently accumulation of another member of the synuclein family- γ-synuclein in neurodegenerative diseases compelled the introduction of the term γ-synucleinopathy. The formation of aggregates and deposits of γ-synuclein is facilitated after its oxidation at methionine 38 (Met38).Several types of intracytoplasmic inclusions containing post-translationally modified α- and γ-synucleins are detected. Oxidized Met38-γ-synuclein forms aberrant inclusions in amygdala and substantia nigra. Double staining revealed colocalization of oxidized-γ-synuclein with α-synuclein in the cytoplasm of neurons. Another type of synuclein positive inclusions in the amygdala of dementia with Lewy bodies patients has the appearance of Lewy bodies. These inclusions are immunoreactive when analyzed with antibodies to α-synuclein phosphorylated on serine 129, as well as with antibodies to oxidized-γ-synuclein. Some of these Lewy bodies have doughnut-like shape with round or elongated shape. The separate immunofluorescent images obtained with individual antibodies specific to oxidized-γ-synuclein and phospho-α-synuclein clearly shows the colocalization of these synuclein isoforms in substantia nigra inclusions. Phospho-α-synuclein is present almost exclusively at the periphery of these structures, whereas oxidized-γ-syn immunoreactivity is also located in the internal parts forming dot-like pattern of staining.These results reveal new γ-synuclein positive lesions in human brain. Oxidized-γ-synuclein is colocalized with phospho-α-synuclein in doughnut-like inclusions. Several types of astrocytes with different morphology are immunopositive for oxidized-γ-synuclein.
