MABN1773
Anti-oxDJ-1 Antibody (Cys106), clone M149
clone M149, from mouse
Synonym(s):
Protein DJ-1, Oncogene DJ1, Parkinson disease protein 7, oxDJ-1 (Cys106)
Select a Size
About This Item
biological source
mouse
Quality Level
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
M149, monoclonal
species reactivity
mouse, human
technique(s)
immunohistochemistry: suitable
western blot: suitable
isotype
IgG2aκ
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human  ...  PARK7(11315)   
General description
Immunogen
Application
Western Blotting Analysis: A reporesentative lot detected basal DJ-1 oxidation (oxDJ-1) in human neuroblastoma SH-SY5Y cells and murine fibroblasts from wild-type, but not DJ-1 knockout, mice, as well as enhanced oxDJ-1 in H2O2-treated SH-SY5Y cells (Saito, Y., et al. (2014). J Neuropathol Exp Neurol. 73(7):714-728.).
Neuroscience
Developmental Signaling
Biochem/physiol Actions
Physical form
Preparation Note
Analysis Note
Western Blotting Analysis: 0.1 µg/mL of this antibody detected enhanced DJ-1 oxidation in 10 µg cell lysate from H2O2-treated human neuroblastoma SH-SY5Y cells.
Other Notes
Disclaimer
Not finding the right product?
Try our Product Selector Tool.
Storage Class Code
12 - Non 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’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Related Content
A major focus of breast cancer research is to understand the mechanisms responsible for disease progression and drug resistance. Toward that end, it has been found that approximately two thirds of all human breast carcinomas overexpress the Estrogen Receptor α (ERα) protein and it remains the primary pharmacological target for endocrine therapy1,2. The normal cellular function of ERα is as a transcription factor that mediates a wide variety of physiological processes, many of which are dependent upon phosphorylation of the receptor at specific amino acid residues3,4. Indeed, ERα is known to be phosphorylated at a multitude of different sites, yet how these all correlate to disease remains unclear5. Here, we interrogated multiple sites of ERα for phosphorylation status by screening an extensive panel of different breast cancer patient samples and other non-breast cancer tissue microarray (TMA) slide samples to determine their relevance to disease.
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service