SAB1404237
Monoclonal Anti-PRKAB1 antibody produced in mouse
clone 3H12-1A10, purified immunoglobulin, buffered aqueous solution
别名:
AMPK, HAMPKb, MGC17785
产品名称
Monoclonal Anti-PRKAB1 antibody produced in mouse, clone 3H12-1A10, purified immunoglobulin, buffered aqueous solution
form
buffered aqueous solution
biological source
mouse
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
3H12-1A10, monoclonal
mol wt
antigen ~55.81 kDa
species reactivity
human
technique(s)
capture ELISA: suitable
indirect ELISA: suitable
western blot: 1-5 μg/mL
isotype
IgG1κ
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... PRKAB1(5564)
Application
Monoclonal Anti-PRKAB1 antibody produced in mouse is suitable for indirect ELISA, capture ELISA and western blot applications.
Biochem/physiol Actions
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.
General description
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)
Immunogen
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
Sequence
MGNTSSERAALERHGGHKTPRRDSSGGTKDGDRPKILMDSPEDADLFHSEEIKAPEKEEFLAWQHDLEVNDKAPAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRSHNNFVAILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVKKTDFEVFDALMVDSQKCSDVSELSSSPPGPYHQEPYVCKPEERFRAPPILPPHLLQVILNKDTGISCDPALLPEPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKPI
Physical form
Solution in phosphate buffered saline, pH 7.4
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存储类别
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
此项目有
Jonathan S Oakhill et al.
Science (New York, N.Y.), 332(6036), 1433-1435 (2011-06-18)
The adenosine monophosphate (AMP)-activated protein kinase (AMPK) regulates whole-body and cellular energy balance in response to energy demand and supply. AMPK is an αβγ heterotrimer activated by decreasing concentrations of adenosine triphosphate (ATP) and increasing AMP concentrations. AMPK activation depends
Cuilan Li et al.
Molecular cancer, 13, 49-49 (2014-03-08)
AMP-activated protein kinase (AMPK) is a key energy sensor that is involved in regulating cell metabolism. Our previous study revealed that the subunits of the heterotimeric AMPK enzyme are diversely expressed during ovarian cancer progression. However, the impact of the
Shi-Bei Wu et al.
Biochimica et biophysica acta, 1822(2), 233-247 (2011-10-18)
We report that the energy metabolism shifts to anaerobic glycolysis as an adaptive response to oxidative stress in the primary cultures of skin fibroblasts from patients with MERRF syndrome. In order to unravel the molecular mechanism involved in the alteration
D Stapleton et al.
FEBS letters, 409(3), 452-456 (1997-06-16)
The AMP-activated protein kinase (AMPK) consists of catalytic alpha and non-catalytic, beta and gamma (38 kDa) subunits and is responsible for acting as a metabolic sensor for AMP levels. There are multiple genes for each subunit and we find that
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