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Home / Assay Kits / ELISA Kits

ELISA Kit for Rat 5'-AMP-activated protein kinase subunit beta-1

SKU : BHE13800275

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EIAAB SCIENCE INC, WUHAN

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Mfr.No.	E1671r
Alternative Names	5'-AMP-activated protein kinase 40 kDa subunit
Categories	Elisa
Function	Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).
Specificity	Natural and recombinant Rat 5'-AMP-activated protein kinase subunit beta-1
Detection Range	0.156-10ng/mL
Entryname	AAKB1_RAT
Method Type	Sandwich
Platform	PF04739
Protein Name	5'-AMP-activated protein kinase subunit beta-1
Sensitivity	0.081ng/mL
Sequence	50: MGNTSSERAA ; LERQAGHKTP ; RRDSSGGTKD ; GDRPKILMDS ; PEDADIFHTE ; 100: EMKAPEKEEF ; LAWQHDLEVN ; EKAPAQARPT ; VFRWTGGGKE ; VYLSGSFNNW ; 150: SKLPLTRSQN ; NFVAILDLPE ; GEHQYKFFVD ; GQWTHDPSEP ; IVTSQLGTVN ; 200: NIIQVKKTDF ; EVFDALMVDS ; QKCSDVSELS ; SSPPGPYHQE ; PYISKPEERF ; 250: KAPPILPPHL ; LQVILNKDTG ; ISCDPALLPE ; PNHVMLNHLY ; ALSIKDGVMV ; 270: LSATHRYKKK ; YVTTLLYKPI ;
Sequence Length	270
String	P80386
Sub Unit	AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with FNIP1 and FNIP2.

Uniprot	P80386
Gene Name	Prkab1
Immunogen Species	Rattus norvegicus (Rat)
Kegg	rno:83803
Unigene	Rn.3619

Reference	1. "Non-catalytic beta- and gamma-subunit isoforms of the 5'-AMP-activated protein kinase." Gao G., Fernandez C.S., Stapleton D., Auster A.S., Widmer J., Dyck J.R.B., Kemp B.E., Witters L.A. J. Biol. Chem.271:8675-8681(1996) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA];PARTIAL PROTEIN SEQUENCE strain: Sprague-Dawley. tissue: Liver. 2. "Characterization of AMP-activated protein kinase beta and gamma subunits. Assembly of the heterotrimeric complex in vitro." Woods A., Cheung P.C.F., Smith F.C., Davison M.D., Scott J., Beri R.K., Carling D. J. Biol. Chem.271:10282-10290(1996) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA] strain: Wistar. 3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res.14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] tissue: Prostate. 4. "Mammalian 5'-AMP-activated protein kinase non-catalytic subunits are homologs of proteins that interact with yeast Snf1 protein kinase." Stapleton D., Gao G., Michell B.J., Widmer J., Mitchelhill K.I., Teh T., House C.M., Witters L.A., Kemp B.E. J. Biol. Chem.269:29343-29346(1994) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 36-159;PROTEIN SEQUENCE OF 36-72; 79-83 AND 90-159 strain: Sprague-Dawley. tissue: Liver. 5. "Posttranslational modifications of the 5'-AMP-activated protein kinase beta1 subunit." Mitchelhill K.I., Michell B.J., House C.M., Stapleton D., Dyck J., Gamble J., Ullrich C., Witters L.A., Kemp B.E. J. Biol. Chem.272:24475-24479(1997) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PARTIAL PROTEIN SEQUENCE;MYRISTOYLATION AT GLY-2;PHOSPHORYLATION AT SER-24; SER-25; SER-108 AND SER-182 6. "Post-translational modifications of the beta-1 subunit of AMP-activated protein kinase affect enzyme activity and cellular localization." Warden S.M., Richardson C., O'Donnell J. Jr., Stapleton D., Kemp B.E., Witters L.A. Biochem. J.354:275-283(2001) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: MUTAGENESIS;MYRISTOYLATION AT GLY-2;PHOSPHORYLATION AT SER-24; SER-25; SER-108 AND SER-182 7. "Identification of phosphorylation sites in AMP-activated protein kinase (AMPK) for upstream AMPK kinases and study of their roles by site-directed mutagenesis." Woods A., Vertommen D., Neumann D., Turk R., Bayliss J., Schlattner U., Wallimann T., Carling D., Rider M.H. J. Biol. Chem.278:28434-28442(2003) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION AT SER-96; SER-101 AND SER-108 8. "Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory feedback loop." Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M., Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B. Autophagy7:696-706(2011) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION BY ULK1 9. "Structural basis for glycogen recognition by AMP-activated protein kinase." Polekhina G., Gupta A., van Denderen B.J., Feil S.C., Kemp B.E., Stapleton D., Parker M.W. Structure13:1453-1462(2005) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 68-162 IN COMPLEX WITH BETA-CYCLODEXTRIN;DOMAIN GLYCOGEN-BINDING;MUTAGENESIS OF TRP-100; LYS-126; LEU-146 AND ASN-150

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