PKAr-1a Recombinant Protein
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| Amount : | 3 µg |
| Purification : | Greater than 95% as determined by SDS-PAGE. |
| Content : | PKA regulatory subunit-II alpha is supplied at a concentration of 0.37mg/ml in 20mM MES, 150mM NaCl, 2mM EDTA, 2mM EGTA, 1mM BME and 50% glycerol. |
| Storage condition : | PKA should be stored at 4°C if entire vial will be used within 1 week. For long term storage below -20°C.Avoid multiple freeze-thaw cycles. |
| AA sequence : | MSHIQIPPGL TELLQGYTVE VLRQQPPDLV EFAVEYFTRL REARAPASVL PAATPRQSLG HPPPEPGPDR VADAKGDSES EEDEDLEVPV PSRFNRRVSV CAETYNPDEE EEDTDPRVIH PKTDEQRCRL QEACKDILLF KNLDQEQLSQ VLDAMFERIV KADEHVIDQG DDGDNFYVIE RGTYDILVTK DNQTRSVGQY DNRGSFGELA LMYNTPRAAT IVATSEGSLW GLDRVTFRRI IVKNNAKKRK MFESFIESVP LLKSLEVSER MKIVDVIGEK IYKDGERIIT QGEKADSFYI IESGEVSILI RSRTKSNKDG GNQEVEIARC HKGQYFGELA LVTNKPRAAS AYAVGDVKCL VMDVQAFERL LGPCMDIMKR NISHYEEQLV KMFGSSVDLG NLGQ. |
| Alternative Name : | cAMP-Dependent Protein Kinase A regulatory subunit-II A, PKA-RII alpha. |
Source : Escherichia Coli.
The recombinant PKA regulatory subunit II-a is a dimeric 90 kDa protein. Protein Kinase A is purified by proprietary chromatographic techniques.
cAMP-dependent PKA is a ubiquitous serine/theonine protein kinase present in a variety of tissues (e.g. brain, skeletal muscle, heart). The intracellular cAMP level regulates cellular responses by altering the interaction between the catatytic C and regulatory R subunits of PKA. The inactive tetrameric PKA holoenzyme R2C2 is activated when cAMP binds to R2, which dissociates the tetramer to R2 cAMP 4 and two active catalytic subunits. Free Catalytic subunits of PKA can phosphorylate a wide variety of intracellular target proteins. In response to hormone- induced high cAMP levels, PKA phosphorylates glycogen synthetase (inhibition of the enzyme activity) and phosphorylase kinase to block glycogen synthesis. Different isoforms of catalytic and regulatory subunits suggest specific functions.
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
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