A8076
Anti-Phosphoserine−Agarose antibody, Mouse monoclonal
clone PSR-45, purified from hybridoma cell culture
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
biological source
mouse
Quality Level
conjugate
agarose conjugate
antibody form
purified from hybridoma cell culture
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.
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
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.
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
Regulatory Information
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Gayatri R Iyer et al.
The Journal of biological chemistry, 293(25), 9736-9746 (2018-05-03)
The human malaria parasite Plasmodium falciparum proliferates in red blood cells following repeated cycles of invasion, multiplication, and egress. P. falciparum serine repeat antigen 5 (PfSERA5), a putative serine protease, plays an important role in merozoite egress. However, regulation of
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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
Lin Liu et al.
Developmental cell, 52(2), 196-209 (2019-12-24)
Saturated fatty acids (SFAs) (the "bad" fat), especially palmitate (PA), in the human diet are blamed for potential health risks such as obesity and cancer because of SFA-induced lipotoxicity. However, epidemiological results demonstrate a latent benefit of SFAs, and it
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
Articles
Protein modifications are crucial for disease study. Analysis methods are key.
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