Overview
Product name
Description
Specificity
Tested applications
Species reactivity
Immunogen
Positive control
Anti-TOB (phospho S164) antibody
Rabbit polyclonal to TOB (phospho S164) ab78915 detects endogenous levels of TOB only when phosphorylated at serine 164.
ELISA, WB, IHC-P
Reacts with: Human
Predicted to work with: Mouse, Rat
Synthetic phosphopeptide derived from human TOB around the phosphorylation site of serine
Human brain tissue; HT-29 cell extracts, treated with serum (20%, 15mins).
Properties
Form
Storage instructions
Storage buffer
Purity
Purification notes
Liquid
Shipped at 4°C. Store at -20°C. Stable for 12 months at -20°C.
Preservative: 0.02% Sodium Azide
Immunogen affinity purified ab78915 was affinity-purified from rabbit antiserum by affinity-chromatography using epitopespecific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.
Polyclonal
IgG
Clonality
Isotype
Applications
Our Abpromise guarantee covers the use of ab78915 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Application Abreviews Notes
ELISA 1/5000.
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Application
WB
IHC-P
Abreviews Notes
1/500 - 1/1000. Detects a band of approximately 38 kDa (predicted molecular weight: 38 kDa).
1/50 - 1/100.
Target
Relevance The Tob/Btg family of proteins consists of a large number of members. These proteins have a common domain in their amino terminal end and may have anti-proliferative activity in various cell types. The Tob protein was identified in a search for molecules that interact with the receptor tyrosine kinase ErbB2. Active ErbB2 has a negative effect on the anti-proliferative activity of
Tob. However, Tob is phosphorylated on serine and threonine residues but not on tyrosine, suggesting that active ErbB2 activates a Ser/Thr kinase that phosphorylates Tob.
Unphosphorylated Tob suppresses expression of cyclin D1. It was shown that active p90Rsk1 kinase (known to be activated by protein-tyrosine kinase receptor) phosphorylates Tob on serine and threonine residues in vitro. In addition, Erk1/Erk2 MAP kinases phosphorylate Tob in vivo and in vitro, resulting in suppression of the anti-proliferative activity of Tob. Homozygous Tob knockout mice develop greater bone mass resulting from increased numbers of osteoblasts.
Furthermore, it has been shown in osteoblasts, that upon BMP2 (bone morphogenetic protein) activation, Tob associates with receptor regulated Smads (Smad 1, 5, and 8). Thus, osteoblast proliferation and differentiation is negatively regulated by Tob protein through the Smad proteins.
Anti-TOB (phospho S164) antibody images ab78915 at 1/50 dilution staining TOB in human brain by Immunohistochemistry using paraffin-embedded tissue, in the absence or presence of the immunising phosphopeptide.
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - TOB (phospho
S164) antibody (ab78915)
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All lanes : Anti-TOB (phospho S164) antibody (ab78915) at 1/500 dilution
Lane 1 : HT-29 cell extracts, treated with serum (20%, 15mins)
Lane 2 : HT-29 cell extracts, treated with serum (20%, 15mins) with immunising phosphopeptide at 10 µg
Lysates/proteins at 30 µg per lane.
Western blot - TOB (phospho S164) antibody
(ab78915)
Predicted band size : 38 kDa
Observed band size : 38 kDa
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