PRKAB2 Human

Protein Kinase, AMP-Activated, Beta 2 non-Catalytic Subunit Human Recombinant
Cat. No.
BT14122
Source
E.coli.
Synonyms
5'-AMP-activated protein kinase subunit beta-2, AMPK subunit beta-2.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

PRKAB2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (1-272) and having a molecular mass of 32.8kDa. PRKAB2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
PRKAB2, a regulatory subunit of AMP-activated protein kinase (AMPK), plays a crucial role in cellular energy regulation. AMPK, a heterotrimeric complex, consists of an alpha catalytic subunit and non-catalytic beta and gamma subunits. As an energy sensor, AMPK responds to metabolic stress by phosphorylating and inactivating key enzymes like acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), which are involved in fatty acid and cholesterol synthesis. PRKAB2, highly expressed in skeletal muscle, positively regulates AMPK activity.
Description
Recombinant human PRKAB2, expressed in E. coli, is a non-glycosylated polypeptide chain containing 296 amino acids (residues 1-272). This 32.8 kDa protein is fused to a 24 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
The PRKAB2 solution is supplied at a concentration of 1 mg/ml in a buffer containing 20 mM Tris-HCl (pH 8.0), 10% glycerol, and 2 M urea.
Stability
For short-term storage (2-4 weeks), the product should be stored at 4°C. For long-term storage, it is recommended to store the product frozen at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for extended storage. Avoid repeated freeze-thaw cycles.
Purity
The purity of the protein is greater than 90% as determined by SDS-PAGE analysis.
Synonyms
5'-AMP-activated protein kinase subunit beta-2, AMPK subunit beta-2.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMGNTTS DRVSGERHGA KAARSEGAGG HAPGKEHKIM VGSTDDPSVF SLPDSKLPGD KEFVSWQQDL EDSVKPTQQA RPTVIRWSEG GKEVFISGSF NNWSTKIPLI KSHNDFVAIL DLPEGEHQYK FFVDGQWVHD PSEPVVTSQL GTINNLIHVK KSDFEVFDAL KLDSMESSET SCRDLSSSPP GPYGQEMYAF RSEERFKSPP ILPPHLLQVI LNKDTNISCD PALLPEPNHV MLNHLYALSI KDSVMVLSAT HRYKKKYVTT LLYKPI.

Product Science Overview

Introduction

Protein Kinase, AMP-Activated, Beta 2 Non-Catalytic Subunit, also known as PRKAB2, is a regulatory subunit of the AMP-activated protein kinase (AMPK) complex. AMPK is a crucial energy-sensing enzyme that plays a significant role in maintaining cellular energy homeostasis. It is a heterotrimeric complex composed of an alpha catalytic subunit and non-catalytic beta and gamma subunits .

Structure and Function

The PRKAB2 subunit is integral to the AMPK complex’s function. It acts as a scaffold, facilitating the assembly of the alpha and gamma subunits. This subunit is involved in the regulation of AMPK activity through its myristoylation and phosphorylation, which affect the enzyme’s activity and cellular localization .

AMPK is activated in response to metabolic stresses that deplete cellular ATP levels, such as exercise, hypoxia, and glucose deprivation. Upon activation, AMPK phosphorylates and inactivates key enzymes involved in anabolic processes, thereby conserving ATP. It also promotes catabolic processes that generate ATP, thus restoring energy balance within the cell .

Biological Significance

The AMPK complex, including the PRKAB2 subunit, is essential for cellular energy regulation. It inhibits energy-consuming processes like protein, carbohydrate, and lipid biosynthesis, while promoting energy-producing pathways. This regulation is vital for cellular adaptation to metabolic stress and maintaining overall energy homeostasis .

Clinical Relevance

Mutations or dysregulation of the PRKAB2 subunit and the AMPK complex have been associated with various metabolic disorders and diseases. For instance, alterations in AMPK activity are linked to conditions such as obesity, type 2 diabetes, and cancer. Understanding the role of PRKAB2 in these processes can provide insights into potential therapeutic targets for these diseases .

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Source
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