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Anti-Phosphoserine Antibody, clone 4A4

clone 4A4, Upstate®, from mouse

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

purified antibody

antibody product type

primary antibodies

clone

4A4, monoclonal

species reactivity

vertebrates

manufacturer/tradename

Upstate®

technique(s)

ELISA: suitable
flow cytometry: suitable
immunofluorescence: suitable
immunohistochemistry: suitable (paraffin)
western blot: suitable

isotype

IgG1

shipped in

wet ice

target post-translational modification

phosphorylation (pSer)

General description

The identification of protein phosphorylation as a regulatory mechanism originated from studies by Fischer and Krebs in the mid 1950s that later earned them the 1992 Nobel prize. It is the major mechanism for the regulation of diverse cellular processes including cell division, protein synthesis, transcriptional regulation and neurotransmission. The steady state phosphorylation of any given substrate is governed by the opposing activities of kinases and phosphatases. It is now believed that a third of all eukaryotic cellular proteins are phosphorylated and that the majority of all phosphorylation events occur on serine and threonine residues (greater than 95%).

Specificity

Serine-phosphorylated proteins from all species

Immunogen

Phosphoserine coupled to KLH

Application

Anti-Phosphoserine Antibody, clone 4A4 is an antibody against Phosphoserine for use in WB, IF, FC, IH(P), ELISA.
Research Category
Signaling
Research Sub Category
General Post-translation Modification

Quality

Routinely evaluated by immunoblot analysis on lysate from Calyculin A/Okadaic-treated human A431 carcinoma cells.

Target description

Dependent upon the molecular weight of the serine phosphorylated protein being detected.

Physical form

50 µL of PBS with 0.05% sodium azide with 30% glycerol.
Format: Purified
Protein G-Sepharose Chromatography

Storage and Stability

2 years at -20°C from date of shipment.
For maximum recovery of the product, centrifuge the original vial prior to removing the cap. If the product has accidentally been frozen and thawed, spin it at 13,000 x g for 10 minutes at 2-8°C.

Legal Information

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

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

10 - Combustible liquids

wgk_germany

WGK 2


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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Avital Mendelson et al.
JCI insight, 4(16) (2019-08-23)
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Zou, C; Chen, Y; Smith, RM; Snavely, C; Li, J; Coon, TA; Chen, BB; Zhao, Y; Mallampalli, RK
The Journal of Biological Chemistry null
Ying Yang et al.
Chemistry & biodiversity, 19(11), e202200333-e202200333 (2022-09-24)
N6-Methyladenosine (m6A), one of the post-transcriptional modifications of RNA, is important in hepatocellular carcinoma (HCC). However, the mechanism of its regulation remains elusive. We here show that exposure of HCC cells to sulfatide significantly reduced the total mRNA m6A modification.
Vic Hart et al.
Journal of cancer research and clinical oncology, 147(10), 2893-2912 (2021-06-18)
In this study, two novel alternative splice variants of HER2, named HER2-PI9 and HER2-I12, were identified in breast cancer cell lines and breast tumour tissues. Whilst HER2-P19 arises from the inclusion of an 117 bp cassette-exon of intron 9 of HER2
Mario A Acuña et al.
The Journal of clinical investigation, 126(7), 2547-2560 (2016-06-09)
Diminished inhibitory neurotransmission in the superficial dorsal horn of the spinal cord is thought to contribute to chronic pain. In inflammatory pain, reductions in synaptic inhibition occur partially through prostaglandin E2- (PGE2-) and PKA-dependent phosphorylation of a specific subtype of

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