MOUSE ANTI AMPK ALPHA 1/2

GWB-E5FB3C

IgG2aSpecies Cross Reactivity: Based on sequence similarity is expected to react with:Vertebrates Human Mouse RatN. B. Antibody reactivity and working conditions may vary between species.

Phosphate buffered saline pH7. 4

29 amino acid peptide within the N-terminal catalytic domain of Drosophila AMPK alpha.

Responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase. It also regulates cholesterol synthesis via phosphorylation and inactivation of hormone-sensitive lipase and hydroxymethylglutaryl-CoA reductase. Appears to act as a metabolic stress-sensing protein kinase switching off biosynthetic pathways when cellular ATP levels are depleted and when 5\' -AMP rises in response to fuel limitation and/or hypoxia. This is a catalytic subunit. Ref. 8Ref. 9Catalytic activityATP + a protein = ADP + a phosphoprotein. Cofactor: Magnesium. Enzyme regulationBinding of AMP results in allosteric activation inducing phosphorylation on Thr-183 by STK11 in complex with STE20-related adapter-alpha (STRAD alpha) pseudo kinase and CAB39. Also activated by phosphorylation by CAMKK2 triggered by a rise in intracellular calcium ions without detectable changes in the AMP/ATP ratio. Ref. 8Ref. 9Subunit structureHeterotrimer of an alpha catalytic subunit a beta and a gamma non-catalytic subunits. Interacts with FNIP1 and FNIP2. Ref. 14Ref. 15Sequence similaritiesBelongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily. Contains 1 protein kinase domain. Sequence cautionThe sequence AAA64850. 1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAD43027. 1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAH37303. 1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAA36547. 1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAG35788. 1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. [1] \" Isolation mapping and functional analysis of a novel human cDNA (BNIP3L) encoding a protein homologous to human NIP3. \" Matsushima M. Fujiwara T. Takahashi E. Minaguchi T. Eguchi Y. Tsujimoto Y. Suzumori K. Nakamura Y. Genes Chromosomes Cancer 21:230-235(1998) [PubMed: 9523198] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA]. [2] \" BNIP3a a human homolog of pro-apoptotic protein BNIP3 promotes apoptosis and interacts with viral and cellular anti-apoptosis proteins. \" Yasuda M. Han J. -W. Dionne C. A. Boyd J. M. Chinnadurai G. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databasesCited for: NUCLEOTIDE SEQUENCE [MRNA]. [3] \" Nix and Nip3 form a subfamily of pro-apoptotic mitochondrial proteins. \" Chen G. Cizeau J. Vande Velde C. Park J. H. Bozek G. Bolton J. Shi L. Dubik D. Greenberg A. J. Biol. Chem. 274:7-10(1999) [PubMed: 9867803] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal liver. [4] \" A novel adenovirus E1B19K-binding protein B5 inhibits apoptosis induced by Nip3 by forming a heterodimer through the C-terminal hydrophobic region. \" Ohi N. Tokunaga A. Tsunoda H. Nakano K. Haraguchi K. Oda K. Motoyama N. Nakajima T. Cell Death Differ. 6:314-325(1999) [PubMed: 10381623] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] FUNCTION SUBCELLULAR LOCATION SELF-ASSOCIATION INTERACTION WITH BNIP3 AND HUMAN ADENOVIRUS-2 E1B 19 KDA PROTEIN. [5] \" The proapoptotic factor Nix is coexpressed with Bcl-xL during terminal erythroid differentiation. \" Aerbajinai W. Giattina M. Lee Y. T. Raffeld M. Miller J. L. Blood 102:712-717(2003) [PubMed: 12663450] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA]. [6] \" A catalog of genes in the human dermal papilla cells as identified by expressed sequence tags. \" Farooq M. Kim M. K. Kim Y. H. Seo J. M. Lee H. M. Sohn M. Y. Hwang S. Y. Chung H. J. Im S. U. Jung E. J. Kim J. C. Submitted (APR-2000) to the EMBL/GenBank/DDBJ databasesCited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Hair follicle dermal papilla. [7] \" Cloning of human full-length CDSs in BD Creator(TM) system donor vector. \" Kalnine N. Chen X. Rolfs A. Halleck A. Hines L. Eisenstein S. Koundinya M. Raphael J. Moreira D. Kelley T. LaBaer J. Lin Y. Phelan M. Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databasesCited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. [8] \" The full-ORF clone resource of the German cDNA consortium. \" Bechtel S. Rosenfelder H. Duda A. Schmidt C. P. Ernst U. Wellenreuther R. Mehrle A. Schuster C. Bahr A. Bloecker H. Heubner D. Hoerlein A. Michel G. Wedler H. Koehrer K. Ottenwaelder B. Poustka A. Wiemann S. Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney. [9] \" The status quality and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). \" The MGC Project TeamGenome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone marrow and Cervix. [10] \" The p53-inducible TSAP6 gene product regulates apoptosis and the cell cycle and interacts with Nix and the Myt1 kinase. \" Passer B. J. Nancy-Portebois V. Amzallag N. Prieur S. Cans C. Roborel de Climens A. Fiucci G. Bouvard V. Tuynder M. Susini L. Morchoisne S. Crible V. Lespagnol A. Dausset J. Oren M. Amson R. Telerman A. Proc. Natl. Acad. Sci. U. S. A. 100:2284-2289(2003) [PubMed: 12606722] [Abstract]Cited for: INTERACTION WITH STEAP3.