14-3-3 (phospho Ser58) antibody
- Host / ClonalityRabbit Polyclonal
- Species reactivityHuman
14-3-3 (phospho Ser58) antibody validated data
14-3-3 (phospho Ser58) antibody
|Full Name||tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, beta polypeptide|
|Synonyms||14-3-3 (phospho S58), 14-3-3 (phospho Ser58), 14-3-3 (pS58), 14-3-3 (pSer58), 14-3-3 phospho S58, 14-3-3 phospho Ser58, Phospho 14-3-3 (S58), Phospho 14-3-3 (Ser58), Phospho 14-3-3 (pS58), Phospho 14-3-3 (pSer58)|
|Product Description||Rabbit Polyclonal antibody to 14-3-3 (Phospho S58)|
|Specificity||GTX42911 specifically recognises the 29kDa 14-3-3 protein, when phosphorylated at Ser58. |
The family of 14-3-3 proteins are highly conserved proteins expressed abundantly in the brain, which have been identified as crucial regulators of many cellular processes including multiple signalling pathways, cell growth, apoptosis, intracellular trafficking and malignant transformation. The interaction of 14-3-3 with target proteins is typically dependant upon phosphorylation, occurring through phosphoserine and phosphothreonine binding, with 14-3-3 protein activity itself being regulated by kinases such as kinase A and C, Akt, and CaMK1 and equally by phosphatases such as protein phosphatase 1 (PP1) and 2A (PP2A).
The ability of 14-3-3 protein to facilitate the phosphorylation of Tau present in neurofibrillary tangles (NFTs) and the co-localisation of 14-3-3 protein with alpha-synuclein found in Lewy bodies, suggests a role for 14-3-3 protein in the pathogenesis of both Alzheimer’s disease and Parkinson’s disease (1).
|Target||14-3-3 (Phospho S58)|
|Immunogen||Synthetic phosphopeptide corresponding to an amino acid sequence within 14-3-3 protein which includes phosphorylated Ser58.|
|Application Note||Recommended Starting Dilutions:|
For WB: Use at 1/1000
Optimal dilutions should be determined experimentally by the researcher.
|Storage Buffer||10mM HEPES pH7.5, 0.09%Sodium Azide0.01%Bovine Serum Albumin50%Glycerol|
|Storage Instruction||Keep as concentrated solution. Aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.|
|Notes||For In vitro laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption. |
Why is the observed Western Blot band size different from predicted size?
The predicted M.W. is based on protein sequence analysis; however, some factors might lead to an observed band size that is different from the predicted size. The reasons might include:
1.Post-translational modification (PTM):
a. Some post-translational modifications might lead to increased protein size, including
phosphorylation, acetylation, methylation, glycosylation, sumoylation, ubiquitination,
b. Some post-translational modifications might lead to decreased protein size including
phosphatidylethanolamine conjunction (e.g. LC3-II)
c. Some proteins may be cleaved to form an active or mature form; this process will
lead to a decreased protein size (e.g. Notch activation, Caspase activation, etc.)
d. Some websites provide useful PTM information
iv.CBS data sets http://www.cbs.dtu.dk/databases/
v.CBS prediction Servers http://www.cbs.dtu.dk/services/
2.mRNA splice variants (Isoforms):
Through alternative splicing, one gene can generate different proteins with different M.W. Regulation of alternative splicing depends upon cell type, conditions, etc.
Some proteins could form dimers or multimers, increasing the M.W. This phenomenon usually can be found in reducing gel condition; however, strong interactions may still be seen with higher molecular weight proteins even in denaturing gel.
The observed size could also potentially be influenced by the protein charge
Different species likely have different protein sequence and PTM, which can lead to a different protein M.W.
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