Anti-S6K1 (phospho T229) antibody (ab5231)
Key features and details
- Rabbit polyclonal to S6K1 (phospho T229)
- Suitable for: WB
- Reacts with: Human
- Isotype: IgG
Overview
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Product name
Anti-S6K1 (phospho T229) antibody
See all S6K1 primary antibodies -
Description
Rabbit polyclonal to S6K1 (phospho T229) -
Host species
Rabbit -
Tested Applications & Species
See all applications and species dataApplication Species WB Human
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Immunogen
Other Immunogen Type corresponding to Human S6K1. The antiserum was produced against a chemically synthesized phosphopeptide derived from the region of human p70-S6K that contains threonine 229. The sequence is conserved in rat.
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Positive control
- Hek293 cells +/- EGF; truncated p70S6K protein, an N-terminus His-tagged fusion protein corresponding to amino acids 1-421 of human p70S6K containing a T412E mutation to become constitutively active.
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General notes
70 kDa ribosomal protein S6 kinase (p70S6K or p70S6K beta 1) is a member of a serine/threonine kinase family that phosphorylates the 40S ribosomal protein S6, thereby modulating the translation of ribosomal proteins and translation elongation factors. p70S6K is activated in response to the phosphatidylinositol 3-kinase (PI3K) and mitogen-activated protein kinase (MAPK) pathways, and is required for progression through the cell cycle and for cell growth. Activation of p70S6K is regulated by phosphorylation of seven different residues distributed throughout the protein, with the critical sites being threonines 229, 389, 421 and serine 424. Threonine 229 is located within the activation loop.
Properties
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Form
Liquid -
Storage instructions
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles. -
Storage buffer
pH: 7.30
Preservative: 0.05% Sodium azide
Constituents: PBS, 0.1% BSA
BSA is IgG and protease free -
Concentration information loading... -
Purity
Immunogen affinity purified -
Purification notes
Purified from rabbit serum by sequential epitope-specific chromatography. The antibody has been negatively preadsorbed using a non-phosphopeptide corresponding to the site of phosphorylation to remove antibody that is reactive with non-phosphorylated p70S6K. The final product is generated by affinity chromatography using a p70S6K derived peptide that is phosphorylated at threonine 229. -
Primary antibody notes
70 kDa ribosomal protein S6 kinase (p70S6K or p70S6K beta 1) is a member of a serine/threonine kinase family that phosphorylates the 40S ribosomal protein S6, thereby modulating the translation of ribosomal proteins and translation elongation factors. p70S6K is activated in response to the phosphatidylinositol 3-kinase (PI3K) and mitogen-activated protein kinase (MAPK) pathways, and is required for progression through the cell cycle and for cell growth. Activation of p70S6K is regulated by phosphorylation of seven different residues distributed throughout the protein, with the critical sites being threonines 229, 389, 421 and serine 424. Threonine 229 is located within the activation loop. -
Clonality
Polyclonal -
Isotype
IgG -
Research areas
Images
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Western blot - Anti-S6K1 (phospho T229) antibody (ab5231)Extracts prepared from Hek293 cells (1-4) or activated p70 S6 kinase protein (5, 6) were resolved on a 10% polyacrylamide gel and transferred to PVDF. Membranes were either untreated (1-5), or treated with lambda (ë) phosphatase (6), blocked with a 5% BSA-TBST buffer overnight at 4°C, then incubated with 0.50
µ g/mL ab5231 for two hours at room temperature in a 3% BSA-TBST buffer, following its prior incubation with: nopeptide (1, 5, 6), the non-phosphorylated peptide corresponding to the phosphopeptide (2), a generic phosphothreonine-containing peptide (3), or, the phosphopeptide immunogen (4).After washing, membranes were incubated with goat F(ab')2 anti-rabbit IgG alkaline phosphatase and the signal was detected using the Tropix WesternStar method.The data show that only the phosphopeptide corresponding to p70S6K [pT229] blocks the antibody signal, demonstrating the specificity of the antibody. The data also show that phosphatase stripping eliminates the si
