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MABE50

Sigma-Aldrich

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

100

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).
Research Category
Epigenetics & Nuclear Function
Research Sub Category
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.

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.

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

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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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’.

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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
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)
Tom Haltenhof et al.
Molecular cell, 78(1), 57-69 (2020-02-16)
Homeothermic organisms maintain their core body temperature in a narrow, tightly controlled range. Whether and how subtle circadian oscillations or disease-associated changes in core body temperature are sensed and integrated in gene expression programs remain elusive. Furthermore, a thermo-sensor capable
Amita Vaidya et al.
Cells, 9(8) (2020-08-07)
Breast tumor heterogeneity is a major impediment to oncotherapy. Cancer cells undergo rapid clonal evolution, thereby acquiring significant growth and invasive advantages. The absence of specific markers of these high-risk populations precludes efficient therapeutic and diagnostic management of the disease.
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