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Anti-14-3-3 phospho Serine58 Antibody detects level of 14-3-3 phospho Serine58 & has been published & validated for use in WB.
More>>Anti-14-3-3 phospho Serine58 Antibody detects level of 14-3-3 phospho Serine58 & has been published & validated for use in WB. Less<<
Anti-14-3-3 phospho Serine58 Antibody: SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
Anti-14-3-3 phospho Serine58 Antibody detects level of 14-3-3 phospho Serine58 & has been published & validated for use in WB.
Key Applications
Western Blotting
Application Notes
Western blot: 1:1,000
Biological Information
Immunogen
Synthetic peptide of amino acids surrounding the phosphoSerine 58 site of rat 14-3-3 Protein.
Host
Rabbit
Specificity
14-3-3 Protein, phosphoSerine58. The antibody recognizes a protein of ~29 kDa corresponding to 14-3-3 Protein, phosphoSerine58 in lysates from rat brainstem. Immunolabeling is blocked by the phosphopeptide used as the immunogen but not the corresponding non-phosphopeptide.
Species Reactivity
Human
Rat
Species Reactivity Note
The immunogen sequence has 100% conservation with mouse and Xenopus.
This gene product belongs to the 14-3-3 family of proteins which mediate signal transduction by binding to phosphoserine-containing proteins. This highly conserved protein family is found in both plants and mammals, and this protein is 100% identical to the mouse ortholog. It interacts with CDC25 phosphatases, RAF1 and IRS1 proteins, suggesting its role in diverse biochemical activities related to signal transduction, such as cell division and regulation of insulin sensitivity. It has also been implicated in the pathogenesis of small cell lung cancer.
FUNCTION: SwissProt: P62258 # Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathway. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. SIZE: 255 amino acids; 29174 Da SUBUNIT: Homodimer. Interacts with NDEL1 (By similarity). Interacts with HCV core protein. SUBCELLULAR LOCATION: Cytoplasm (By similarity). Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. SIMILARITY: SwissProt: P62258 ## Belongs to the 14-3-3 family.
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Usage Statement
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.
Storage and Shipping Information
Storage Conditions
Maintain at -20°C in undiluted for up to 6 months after date of receipt. Avoid repeated freeze/thaw cycles. Do not store in a self defrosting freezer.
One of the most striking 'rags to riches' stories in the protein world is that of 14-3-3, originally identified in 1967 as merely an abundant brain protein. The first clues that 14-3-3 would play an important role in cell biology came almost 25 years later when it was found to interact with various proto-oncogene proteins and signaling proteins. The subsequent identification of 14-3-3 as a phosphoserine/phosphothreonine-binding protein firmly established its importance in cell signaling. 14-3-3 family members are found in all eukaryotes - from plants to mammals - and more than 100 binding partners have been identified to date. The targets of 14-3-3 are found in all subcellular compartments and their functional diversity is overwhelming - they include transcription factors, biosynthetic enzymes, cytoskeletal proteins, signaling molecules, apoptosis factors and tumor suppressors. 14-3-3 binding can alter the localization, stability, phosphorylation state, activity and/or molecular interactions of a target protein. Recent studies now indicate that the serine/threonine protein phosphatases PP1 and PP2A are important regulators of 14-3-3 binding interactions, and demonstrate a role for 14-3-3 in controlling the translocation of certain proteins from the cytoplasmic and endoplasmic reticulum to the plasma membrane. New reports also link 14-3-3 to several neoplastic and neurological disorders, where it might contribute to the pathogenesis and progression of these diseases.
14-3-3 protein C-terminal stretch occupies ligand binding groove and is displaced by phosphopeptide binding Silhan, J., et al. J. Biol. Chem., 279:49113-49119 (2004)
2004
The dimeric versus monomeric status of 14-3-3zeta is controlled by phosphorylation of Ser58 at the dimer interface Woodcock, J. M., et al. J. Biol. Chem., 278:36323-36327 (2003)
2003
