Product Datasheet  
PKA C (Phospho-Thr198) Antibody  
Catalog Number: 13330  
Technical:tech@swbio.com  
Information:info@swbio.com  
Description  
  • host_species：  
  • Rabbit
  • Amount：  
  • 100μgμg
  • Swiss-Prot No.：  
  • Swiss-Prot#:P17612
  • Form of Antibody：  
  • 1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.
  • Storage：  
  • Store at -20˚C
  • Immunogen：  
  • A short amino acid sequence containing Thr 198 phosphorylated PKAα cat of human origin.
  • reactivity：  
  • Hu, Ms, Rt
  • appl_detail：  
  • WB: 1:100-1:1,000


    IP: 1-2 μg per 100-500 μg of total protein (1 ml of cell lysate)
  • other_names：  
  • cAMP dependent protein kinase catalytic subunit alpha antibody
    cAMP dependent protein kinase catalytic subunit beta antibody
    cAMP dependent protein kinase catalytic subunit gamma antibody
    PKA C alpha antibody
    PKA C beta antibody
    P
  • Purification：  
  • Immunogen affinity purified
  • Specificity：  
  • Applications：  
  • WB, IP, IF
  • Background：  
  • The second messenger cyclic AMP (cAMP) mediates diverse cellular responses to external signals such as proliferation, ion transport, regulation of metabolism and gene transcription by activation of the cAMP-dependent protein kinase (cAPK or PKA). Activation of PKA occurs when cAMP binds to the two regulatory subunits of the tetrameric PKA holoenzyme resulting in release of active catalytic subunits. Three catalytic (C) subunits have been identified, designated Cα, Cβ and Cγ, that each represent specific gene products. Cα and Cβ are closely related (93% amino acid sequence similarity), whereas Cγ displays 83% and 79% similarity to Cα and Cβ, respectively. Activation of transcription upon elevation of cAMP levels results from translocation of PKA to the nucleus where it phosphorylates the transcription factor cAMP response element binding protein (CREB) on Serine 133, which in turn leads to TFIIB binding to TATA-box-binding protein TBP1, thus linking phospho-CREB to the Pol II transcription initiation complex. The phosphorylation at Threonine 198 is cAMP dependent.



 
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