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Key Documents

P5747

Sigma-Aldrich

Monoclonal Anti-Phosphoserine 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.41

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

PSR-45, monoclonal

form

buffered aqueous solution

packaging

antibody small pack of 25 μL

concentration

~2 mg/mL

technique(s)

dot blot: suitable
indirect ELISA: 0.3-0.6 μg/mL using phosphoserine conjugated to BSA
microarray: suitable
western blot: 2.5-5.0 μg/mL using total rat brain extract.

isotype

IgG1

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

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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

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)
The antibody has been used for the detection of some phosphoserine containing proteins using immunoblotting and dot blotting.

Biochem/physiol Actions

Protein phosphorylation and dephosphorylation are basic signaling mechanisms that modify protein function in eukaryotic cells. Phosphorylation is a rare posttranslational event in normal tissues, however, the abundance of phosphorylated cellular proteins increases several folds following various activation processes. The main amino acids that are phosphorylated are tyrosine, serine, or threonine (pTyr/pSer/pThr), each having specific kinases that phosphorylate them and specific phosphatases that dephosphorylate them. Mono and polyclonal antibodies directed against phosphorylated residues were generated and found useful as analytical and preparative tools by enabling the identification, quantification, and immunoaffinity isolation of phosphorylated cellular proteins.

Physical form

Solution 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

nwg

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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Mechanisms of specificity in protein phosphorylation
Ubersax JA and Ferrell Jr JE
Nature Reviews in Molecular and Cell Biology, 8(7), 530-530 (2007)
Matteo Fornai et al.
The Journal of pharmacology and experimental therapeutics, 356(2), 434-444 (2015-11-20)
Parkinson's disease is frequently associated with gastrointestinal symptoms, mostly represented by constipation and defecatory dysfunctions. This study examined the impact of central dopaminergic denervation, induced by injection of 6-hydroxydopamine (6-OHDA) into the medial forebrain bundle, on distal colonic excitatory cholinergic
An integrated assessment of histopathological changes of the enteric neuromuscular compartment in experimental colitis
Ippolito C, et al.
Journal of Cellular and Molecular Medicine, 19(2), 485-500 (2015)
Ling Lai et al.
Journal of pineal research, 45(4), 476-488 (2008-08-19)
Melatonin, via its MT1 receptor, but not the MT2 receptor, can modulate the transcriptional activity of various nuclear receptors - estrogen receptor alpha (ERalpha) and retinoic acid receptor alpha (RARalpha), but not ERbeta- in MCF-7, T47D, and ZR-75-1 human breast
Changes in expression of VE-cadherin and MMPs in endothelial cells: Implications for angiogenesis
Kiran MS, et al.
Vascular Cell, 3(1), 6-6 (2011)

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