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Rabbit Anti-PRKAA2 Polyclonal Antibody#abs133035

Please note that the price mentioned above is for your reference only. For detailed pricing, we kindly request you to contact our seller, Vecent. Western blot analysis of PRKAA2 expression in ; HepG2 cell lysate,The lane on the left is treated with the antigen-specific peptide. This product is...

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Description

Catalog-specification	Delivery time	USD price
abs133035-50ug	1-2 Weeks	201.0
abs133035-100ug	1-2 Weeks	301.0

Please note that the price mentioned above is for your reference only. For detailed pricing, we kindly request you to contact our seller, Vecent.

Overview
catalog	abs133035
Other names	AMP-activated protein kinase catalytic subunit alpha-2, also known as AAPK2_HUMAN or ACACA kinase, is an enzyme responsible for phosphorylating and regulating various metabolic pathways. It plays a crucial role in cellular energy homeostasis by sensing and responding to fluctuations in AMP and ADP levels. This kinase, commonly referred to as Acetyl-CoA carboxylase kinase, is involved in the regulation of lipid metabolism. It phosphorylates and inhibits Acetyl-CoA carboxylase, thereby reducing the synthesis of fatty acids and cholesterol. Another important role of AMPK catalytic subunit alpha-2, also called AMPK alpha 2 chain, is its involvement in the control of HMGCR activity. HMGCR kinase phosphorylates and inactivates hydroxymethylglutaryl-CoA reductase, which is a key enzyme in the cholesterol synthesis pathway. AMPK alpha-2 is part of the AMPK heterotrimeric complex, which consists of an alpha subunit (including alpha 1 and alpha 2 isoforms), a beta subunit, and a gamma subunit. This complex senses the AMP:ATP ratio in the cell and regulates various metabolic processes accordingly. The PRKAA and PRKAA2 genes encode the protein kinase AMP activated alpha 2 catalytic subunit. These genes are highly conserved among different species, highlighting the importance of this kinase in cellular metabolism. In summary, the AMP-activated protein kinase catalytic subunit alpha-2 is a crucial enzyme involved in the regulation of lipid metabolism and energy homeostasis. It phosphorylates and modulates the activity of key enzymes, such as Acetyl-CoA carboxylase and HMGCR, to maintain cellular energy balance.
Source	Rabbit
Specificity	The PRKAA2 antibody is capable of detecting the overall levels of endogenous PRKAA2 protein present in a sample. This means that it can identify the total amount of PRKAA2 present in the given biological sample.
Species Reactivity	Human;Mouse;Rat
Predictive reaction species	Zebrafish;Chicken;Rabbit;Pig;Dog;Sheep;
Antigen	PRKAA2
Application	WB 1:500-1:2000, ELISA(peptide) 1:20000-1:40000
Immunogen	A synthesized peptide.
MW	60 kDa;Exposure time : 2 hours
Properties
Concentration	1mg/ml
purification	Using SulfoLink™ Coupling Resin, the antiserum was subjected to peptide affinity chromatography, resulting in its purification.
Clonality	Polyclonal Antibody
Stability & Storage	To preserve its quality, keep the item at a constant temperature of -20 °C for a duration of one year. It is important to prevent the item from undergoing frequent cycles of freezing and thawing.
Storage buffer	Rabbit IgG in phosphate buffered saline, pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Target
Background	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. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. Involved in insulin receptor/INSR internalization (PubMed:25687571). AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1. AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1. Plays an important role in the differential regulation of pro-autophagy (composed of PIK3C3, BECN1, PIK3R4 and UVRAG or ATG14) and non-autophagy (composed of PIK3C3, BECN1 and PIK3R4) complexes, in response to glucose starvation. Can inhibit the non-autophagy complex by phosphorylating PIK3C3 and can activate the pro-autophagy complex by phosphorylating BECN1 (By similarity).
Posttranslational modification	Ubiquitinated.Phosphorylated at Thr-172 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Also phosphorylated at Thr-172 by CAMKK2; triggered by a rise in intracellular calcium ions, without detectable changes in the AMP/ATP ratio. CAMKK1 can also phosphorylate Thr-172, but at much lower level. Dephosphorylated by protein phosphatase 2A and 2C (PP2A and PP2C). Phosphorylated by ULK1; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1 and AMPK. Dephosphorylated by PPM1A and PPM1B at Thr-172 (mediated by STK11/LKB1).
Celluar localization	Cytosol;Golgi apparatus;Nucleus;
UniPort	P54646