The protein encoded by this gene is a regulatory subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. This subunit may be a positive regulator of AMPK activity. The myristoylation and phosphorylation of this subunit have been shown to affect the enzyme activity and cellular localization of AMPK. This subunit may also serve as an adaptor molecule mediating the association of the AMPK complex. (provided by RefSeq)

PRKAB1 (AAH01007, 1 a.a. ~ 270 a.a) full-length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.

Sequence
MGNTSSERAALERHGGHKTPRRDSSGGTKDGDRPKILMDSPEDADLFHSEEIKAPEKEEFLAWQHDLEVNDKAPAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRSHNNFVAILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVKKTDFEVFDALMVDSQKCSDVSELSSSPPGPYHQEPYVCKPEERFRAPPILPPHLLQVILNKDTGISCDPALLPEPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKPI

Monoclonal Anti-PRKAB1 antibody produced in mouse is suitable for indirect ELISA, capture ELISA and western blot applications.

PRKAB1 (protein kinase, AMP-activated, β 1 non-catalytic subunit) is a non-catalytic, β subunit of AMP-activated protein kinase (AMPK). It acts as a metabolic sensor for AMP levels. It plays a key role in energy sensor during the response to energy demand and supply. It regulates cell metabolism. It increases the glycolytic flux by H₂0₂ which increase intracellular NADPH content. The activity of PRKAB1 is controlled by decreasing concentrations of adenosine triphosphate (ATP) and increasing AMP concentrations.

Solution in phosphate buffered saline, pH 7.4