A8076
Monoclonal Anti-Phosphoserine−Agarose antibody produced in mouse
clone PSR-45, purified immunoglobulin, buffered aqueous solution
Synonym(s):
Monoclonal Anti-Phosphoserine, Phospho Ser, Phospho serine, Phospho−Ser, Phospho−serine
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.44
Recommended Products
biological source
mouse
Quality Level
conjugate
agarose conjugate
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
PSR-45, monoclonal
form
buffered aqueous solution
technique(s)
immunoprecipitation (IP): suitable
isotype
IgG1
shipped in
wet ice
storage temp.
2-8°C
target post-translational modification
unmodified
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General description
Monoclonal Anti-Phosphoserine (mouse IgG1 isotype) is derived from the hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse.
Specificity
By ELISA and dot blot, the antibody reacts specifically with phosphorylated serine, both as free amino acid or conjugated to carriers such as BSA or KLH. No cross-reactivity is observed with non-phosphorylated serine, phosphothreonine, phosphotyrosine, AMP or ATP. This antibody has been used in immunoblotting for the localization of some phosphoserine-containing proteins. Certain proteins known to contain phosphorylated serine may not be recognized by this antibody due to steric hindrance of the recognition site.
Immunogen
phosphoserine conjugated to Keyhole Limpet Hemocyanin (KLH).
Application
Monoclonal Anti-Phosphoserine - Agarose may be used for the immunoprecipitation or immuno-affinity purification of serine phosphoproteins.The antibody may be used for the localization of some phosphoserine containing proteins using the immunoblotting method.
Biochem/physiol Actions
Reversible phosphorylation of proteins is an important post-translational modification that plays a regulatory role in the expression of most proteins in the cells. Reversible phosphorylation at multiple serine, tyrosine and threonine residues mediate numerous signalling pathways in both prokaryotic and Eukaryotic cells. Cellular proteins with phosphorylated serine increase many fold by the activation of serine kinases. Most mitogenic receptor systems such as EGF, PDGF, insulin receptors contain serine/threonine/tyrosine kinase domains that undergo autophosphorylation when receptors bind to the respective ligands. T cell antigen receptor complex or the receptors for some hemopoietic growth factors may stimulate these phosphorylation associated kinases,3 and cells transformed by viral oncogenes contain elevated levels of phosphorylated tyr/ser/thr.
Monoclonal Anti-Phosphoserine may be used for the identification of proteins containing phosphorylated serine both as the free amino acid or when conjugated to carriers such as BSA or KLH. It does not react with non-phosphorylated serine, phosphorylated tyrosine or threonine, AMP or ATP.
Monoclonal Anti-Phosphoserine may be used for the identification of proteins containing phosphorylated serine both as the free amino acid or when conjugated to carriers such as BSA or KLH. It does not react with non-phosphorylated serine, phosphorylated tyrosine or threonine, AMP or ATP.
Physical form
Suspension in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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 3
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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Claire E Fletcher et al.
Nucleic acids research (2016-12-03)
Regulation of microRNA (miR) biogenesis is complex and stringently controlled. Here, we identify the kinase GSK3β as an important modulator of miR biogenesis at Microprocessor level. Repression of GSK3β activity reduces Drosha activity toward pri-miRs, leading to accumulation of unprocessed
G Sármay et al.
Proceedings of the National Academy of Sciences of the United States of America, 91(10), 4140-4144 (1994-05-10)
Stimulation of B cells by clustering their surface immunoglobulins (sIg) leads to enhanced phosphorylation of several cellular proteins on Ser and Tyr residues. The type II Fc gamma receptor (Fc gamma RII) is one of those proteins that undergo Ser
A Dvir et al.
The Journal of cell biology, 113(4), 857-865 (1991-05-01)
Protein tyrosine kinase blockers of the tyrphostin family inhibited the EGF-dependent proliferation of human and guinea pig keratinocytes grown in culture and induced their growth arrest. These blockers also significantly inhibited the growth of epidermal keratinocytes, but not of dermal
Joanna Cieśla et al.
Acta biochimica Polonica, 58(2), 137-148 (2011-05-31)
Reversible phosphorylation is the most widespread posttranslational protein modification, playing regulatory role in almost every aspect of cell life. The majority of protein phosphorylation research has been focused on serine, threonine and tyrosine that form acid-stable phosphomonoesters. However, protein histidine
Wiljan J A J Hendriks et al.
The FEBS journal, 275(5), 816-830 (2008-02-27)
Some 40-odd genes in mammals encode phosphotyrosine-specific, 'classical' protein tyrosine phosphatases. The generation of animal model systems and the study of various human disease states have begun to elucidate the important and diverse roles of protein tyrosine phosphatases in cellular
Articles
Post-translational modifications such as glycosylation, phosphorylation, and sulfation, to name a few, serve many functions. As a result, the analysis of proteins and their post-translational modifications is particularly important for the study of diseases where multiple genes are known to be involved, such as heart disease, cancer and diabetes.
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