Prkag1 ELISA Kit for Rat(Rattus norvegicus) | EIAab.comPrkag1 ELISA Kit for Rat(Rattus norvegicus)

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Prkag1 (Gene name),

5'-AMP-activated protein kinase subunit gamma-1 (Protein name ), AAKG1_RAT from NCBI database.

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General Annotation

Antigen Annotation

Predicted Eptitope

Vaild Sequence

Related Databases

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Gene name:

Prkag1;

Protein name:

5'-AMP-activated protein kinase subunit gamma-1(AMPK gamma1;AMPK subunit gamma-1;AMPKg);

Alternative:

Organism:

Rat (Rattus norvegicus).

General Annotation

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.

Function:

AMP/ATP-binding 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. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive.

Subcellular Location:

N/A

Protein Attributes:

Sequence length:

330

Sequence:

50:

100:

150:

200:

250:

300:

330:

VVDEHDVVKG | IVSLSDILQA | LVLTGGEKKP |

3D Structure:

N/A

Predicted Eptitope:

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Vaild Sequence:

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Related Databases

UniGene:

Rn.11089

SMR:

P80385

String:

P80385

KEGG:

rno:25520

Pfam:

PF00571

STRING:

10116.ENSRNOP00000020093

Uniprot:

P80385

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ELISA Kit for Rat AMPK gamma1

Cat.:

E10187p

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96T

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ELISA Kit for Rat AMPK gamma1

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ELISA Kit for Rat AMPK gamma1

Cat.:

E10187m

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96T

ELISA Kit for Rat AMPK gamma1

Cat.:

E10187b

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96T

ELISA Kit for Rat AMPK gamma1

Cat.:

E10187r

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96T

CLIA Kit for Rat AMPK gamma1

Cat.:

U10187p

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Packing:

96T

CLIA Kit for Rat AMPK gamma1

Cat.:

U10187m

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Packing:

96T

CLIA Kit for Rat AMPK gamma1

Cat.:

U10187b

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96T

CLIA Kit for Rat AMPK gamma1

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CLIA Kit for Rat AMPK gamma1

Cat.:

U10187r

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96T

Polyclonal Antibody for Rat AMPK gamma1

Cat.:

P10187Rb-r

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40ug/0.2ml

Polyclonal Antibody for Rat AMPK gamma1

Cat.:

P10187Rb-h

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40ug/0.2ml

Polyclonal Antibody for Rat AMPK gamma1

Cat.:

P10187Rb-m

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Packing:

40ug/0.2ml

Polyclonal Antibody for Rat AMPK gamma1

Monoclonal Antibody for Rat AMPK gamma1

Protein for Rat AMPK gamma1

R&D Technical Data

For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.

Precision

For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.

Recovery

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Linearity

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References

1.

"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.
2.

"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: Testis.
3.

"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] OF 8-330
strain: Sprague-Dawley.
tissue: Liver.
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 48-330;PARTIAL PROTEIN SEQUENCE
strain: Sprague-Dawley.
tissue: Liver.
5.

"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 AND ULK2;PHOSPHORYLATION AT SER-260; THR-262 AND SER-269
6.

"Structural basis for AMP binding to mammalian AMP-activated protein kinase."
Xiao B. , Heath R. , Saiu P. , Leiper F.C. , Leone P. , Jing C. , Walker P.A. , Haire L. , Eccleston J.F. , Davis C.T. , Martin S.R. , Carling D. , Gamblin S.J.
Nature449:496-500(2007) [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 (2.1 ANGSTROMS) IN COMPLEX WITH PRKAA1 AND PRKAB2;FUNCTION;DOMAIN CBS;AMP-BINDING;ATP-BINDING
7.

"Structure of mammalian AMPK and its regulation by ADP."
Xiao B. , Sanders M.J. , Underwood E. , Heath R. , Mayer F.V. , Carmena D. , Jing C. , Walker P.A. , Eccleston J.F. , Haire L.F. , Saiu P. , Howell S.A. , Aasland R. , Martin S.R. , Carling D. , Gamblin S.J.
Nature472:230-233(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: X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) IN COMPLEX WITH PRKAA1 AND PRKAB2;FUNCTION;DOMAIN CBS;ADP-BINDING

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