MABE50
Anti-Phosphoepitope SR proteins Antibody, clone 1H4
clone 1H4, from mouse
Synonym(s):
Ser-Arg-rich proteins
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
biological source
mouse
Quality Level
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
1H4, monoclonal
species reactivity
rat
species reactivity (predicted by homology)
human (based on 100% sequence homology), mouse (based on 100% sequence homology)
technique(s)
immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG1κ
shipped in
wet ice
target post-translational modification
unmodified
General description
Ser-Arg-rich (SR) proteins make up a family of functionally and structurally conserved phosphoproteins, and are required components of alternative and constitutive pre-mRNA splicing. SR proteins are characterized by their modular composition consisting of two domains of interest: an N-terminal RNA recognition motif (RRM) which serves in the determination of DNA-binding specificity, and the RS domain, an arginine and serine rich, C-terminal domain that serves as a shuttling and localization director of SR proteins and as a splicing activation domain. They are involved in various aspects of pre-mRNA splicing and in spliceosome assembly including; the identification and appropriation of splice-sites, and the manipulation of alternative splicing regulation.
Immunogen
Purified oocyte nuclei containing xenopus SR proteins.
Application
Immunocytochemistry Analysis: A representative lot was used by an independent laboratory in IC (Fukuhara, T., et al. (2006).
Immunoprecipitation Analysis: A representative lot was used by an independent laboratory in IP (Buratti, E., et al. (2007).
Immunoprecipitation Analysis: A representative lot was used by an independent laboratory in IP (Buratti, E., et al. (2007).
Research Category
Epigenetics & Nuclear Function
Epigenetics & Nuclear Function
Research Sub Category
RNA Metabolism & Binding Proteins
RNA Metabolism & Binding Proteins
Use Anti-Phosphoepitope SR proteins Antibody, clone 1H4 (Mouse Monoclonal Antibody) validated in WB, ICC, IP to detect Phosphoepitope SR proteins also known as Ser-Arg-rich proteins.
Quality
Evaluated by Western Blot in L6 plus insulin cell lysate.
Western Blot Analysis: 0.025 µg/mL of this antibody detected SR proteins in 10 µg of L6 plus insulin cell lysate.
Western Blot Analysis: 0.025 µg/mL of this antibody detected SR proteins in 10 µg of L6 plus insulin cell lysate.
Target description
~ 75, 55, 40, 30, and 20 kDa observed.
This antibody recognizes the family of SR proteins which consist of 75, 55, 40, 30, 20 kDa proteins.
This antibody recognizes the family of SR proteins which consist of 75, 55, 40, 30, 20 kDa proteins.
Physical form
Format: Purified
Protein G Purified
Purified mouse monoclonal IgG1κ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Storage and Stability
Stable for 1 year at 2-8°C from date of receipt.
Analysis Note
Control
L6 plus insulin cell lysate
L6 plus insulin cell lysate
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
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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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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Anil Aktas Samur et al.
Blood cancer journal, 12(12), 171-171 (2022-12-20)
Splicing changes are common in cancer and are associated with dysregulated splicing factors. Here, we analyzed RNA-seq data from 323 newly diagnosed multiple myeloma (MM) patients and described the alternative splicing (AS) landscape. We observed a large number of splicing
A global analysis on the differential regulation of RNA binding proteins (RBPs) by TNF-I? as potential modulators of metabolic syndromes.
Louis, et al.
BBA advances, 2, 100037-100037 (2023)
Yihui Shi et al.
PloS one, 15(5), e0233672-e0233672 (2020-05-30)
Agents that modulate pre-mRNA splicing are of interest in multiple therapeutic areas, including cancer. We report our recent screening results with the application of a cell-based Triple Exon Skipping Luciferase Reporter (TESLR) using a library that is composed of FDA
Miriam Pacetti et al.
Disease models & mechanisms, 15(4) (2022-03-05)
The cellular level of TDP-43 (also known as TARDBP) is tightly regulated; increases or decreases in TDP-43 have deleterious effects in cells. The predominant mechanism responsible for the regulation of the level of TDP-43 is an autoregulatory negative feedback loop.
Mousumi Khatun et al.
Hepatology (Baltimore, Md.), 74(1), 41-54 (2020-11-26)
HCV often causes chronic infection in liver, cirrhosis, and, in some instances, HCC. HCV encodes several factors' those impair host genes for establishment of chronic infection. The long noncoding RNAs (lncRNAs) display diverse effects on biological regulations. However, their role
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