PKA inhibitor fragment (6-22) amide
In vitro transcription of capped mRNA with modified nucleotides and Poly(A) tail
Tyramide Signal Amplification (TSA)
TSA (Tyramide Signal Amplification), used for signal amplification of ISH, IHC and IC etc.
Phos Binding Reagent Acrylamide
Separation of phosphorylated and non-phosphorylated proteins without phospho-specific antibody
Cell Counting Kit-8 (CCK-8)
A convenient and sensitive way for cell proliferation assay and cytotoxicity assay
SYBR Safe DNA Gel Stain
Safe and sensitive stain for visualization of DNA or RNA in agarose or acrylamide gels.
Protect the integrity of proteins from multiple proteases and phosphatases for different applications.
Ki: 1.6 nM
PKA inhibitor fragment (6-22) amide is a PKA inhibitor.
In cell biology, protein kinase A (PKA) is a family of enzymes whose activity is dependent on cellular levels of cyclic AMP (cAMP). PKA is also regarded as a cAMP-dependent protein kinase. PKA has various functions in the cell, such as regulation of sugar, glycogen, and lipid metabolism.
In vitro: Compared with (Ala)Kemptide, PKA inhibitor fragment (6-22) amide was found to have significant difference in inhibitory potency, likely due to the critical role of several of the nonarginine residues to this difference in potency. The minimal length analog of PKA inhibitor fragment (6-22) that inhibited CAMP-dependent protein kinase with high potency was the 17-residue PKI-(6-22)-amide. PKA inhibitor fragment (6-22) interacted at the peptide/protein binding portion of the active site in a competitive manner with a low nanomolar Ki value. To inhibit CAMP-dependent protein kinase, PKA inhibitor fragment (6-22) required both the pseudosubstrate site (residues 14-22) and additional NH2-terminal determinants within residues 6-13. PKA inhibitor fragment (6-22) could clear mimic protein and peptide substrates in interacting with the binding region of the active site particularly in the COOH-terminal pseudosubstrate basic domain. Undoubtedly, the overall affinity of PKA inhibitor fragment (6-22) was due to the number of hydrogen bonds as well as other bonding interactions with the active site of the CAMP-dependent protein kinase [1, 2].
In vivo: N/A
Clinical trial: N/A
 Glass et al (1989) Primary structural determinants essential for potent inhibition of cAMP-dependent protein kinase by inhibitory peptides corresponding to the active portion of the heat-stable inhibitor protein. J.Biol.Chem. 264 8802. PMID: 2722799.
 Glass et al (1989) Protein kinase inhibitor-(6-22)-amide peptide analogs with standard and nonstandard amino acid substitutions for phenylalanine 10. J.Biol.Chem. 264 14579. PMID: 2760075.
|Physical Appearance||A solid|
|Storage||Desiccate at -20°C|
|Solubility||≥186.8mg/mL in DMSO|
|Shipping Condition||Evaluation sample solution: ship with blue ice. All other available sizes: ship with RT, or blue ice upon request.|
|General tips||For obtaining a higher solubility, please warm the tube at 37°C and shake it in the ultrasonic bath for a while. Stock solution can be stored below -20°C for several months.|