ATP1B2 Human, Sf9

ATPase Transporting Beta 2 Human Recombinant, Sf9
Cat. No.
BT22110
Source
Sf9, Baculovirus cells.
Synonyms
ATP1B2, AMOG, Sodium/Potassium-Transporting ATPase Beta-2 Chain, Sodium/Potassium-Dependent ATPase Beta-2 Subunit, Na, K-ATPase Beta-2 Polypeptide, Adhesion Molecule On Glia, ATPase Na+/K+ Transporting Subunit Beta 2, Sodium-Potassium ATPase Subunit Beta 2 (Non-Catalytic), Sodium/Potassium-Transporting ATPase Subunit Beta-2, Sodium/Potassium-Dependent ATPase Subunit Beta-2, ATPase, Na+/K+ Transporting, Beta 2 Polypeptide, Sodium Pump Subunit Beta-2, Adhesion Molecule In Glia.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% 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.
Shipped with Ice Packs
In Stock

Description

ATP1B2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 232 amino acids (68-290a.a.) and having a molecular mass of 26.4kDa (Molecular size on SDS-PAGE will appear at approximately 28-40 kDa). ATP1B2 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
ATPase Transporting Beta 2, also known as ATP1B2, is a protein that in humans is encoded by the ATP1B2 gene. This protein constitutes the non-catalytic component of the active sodium-potassium pump enzyme, which plays a crucial role in maintaining electrochemical gradients across the plasma membrane by exchanging sodium (Na+) and potassium (K+) ions. While the precise function of the beta-2 subunit remains unclear, it is essential for the enzyme's activity. The ATP1B2 protein comprises three subunits: alpha (catalytic), beta, and gamma.
Description
Recombinant human ATP1B2 protein was expressed in Sf9 insect cells using a baculovirus expression system. This protein is a single, glycosylated polypeptide chain that contains 232 amino acids (residues 68-290) and has a molecular mass of 26.4 kDa. On SDS-PAGE, the apparent molecular size is approximately 28-40 kDa due to glycosylation. The protein includes a 9 amino acid His tag at the C-terminus to facilitate purification, which was performed using proprietary chromatographic techniques.
Physical Appearance
The product is a sterile, colorless, and clear solution.
Formulation
The ATP1B2 protein solution is provided at a concentration of 0.5 mg/ml in Phosphate Buffered Saline (pH 7.4) containing 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For long-term storage, it is recommended to store the protein at -20°C. To further enhance stability during long-term storage, adding a carrier protein such as 0.1% HSA or BSA is advised. Avoid repeated freeze-thaw cycles to maintain protein integrity.
Purity
The purity of the ATP1B2 protein is greater than 90% as determined by SDS-PAGE analysis.
Synonyms
ATP1B2, AMOG, Sodium/Potassium-Transporting ATPase Beta-2 Chain, Sodium/Potassium-Dependent ATPase Beta-2 Subunit, Na, K-ATPase Beta-2 Polypeptide, Adhesion Molecule On Glia, ATPase Na+/K+ Transporting Subunit Beta 2, Sodium-Potassium ATPase Subunit Beta 2 (Non-Catalytic), Sodium/Potassium-Transporting ATPase Subunit Beta-2, Sodium/Potassium-Dependent ATPase Subunit Beta-2, ATPase, Na+/K+ Transporting, Beta 2 Polypeptide, Sodium Pump Subunit Beta-2, Adhesion Molecule In Glia.
Source
Sf9, Baculovirus cells.
Amino Acid Sequence
ADPDHTPKYQ DRLATPGLMI RPKTENLDVI VNVSDTESWD QHVQKLNKFL EPYNDSIQAQ KNDVCRPGRY YEQPDNGVLN YPKRACQFNR TQLGNCSGIG DSTHYGYSTG QPCVFIKMNR VINFYAGANQ SMNVTCAGKR DEDAENLGNF VMFPANGNID LMYFPYYGKK FHVNYTQPLV AVKFLNVTPN VEVNVECRIN AANIATDDER DKFAGRVAFK LRINKTHHHH HH.

Product Science Overview

Introduction

ATPase Transporting Beta 2, also known as ATP1B2, is a non-catalytic component of the Na+/K+ ATPase enzyme. This enzyme is crucial for maintaining the electrochemical gradients of sodium and potassium ions across the plasma membrane, which is essential for various cellular processes .

Structure

The Na+/K+ ATPase enzyme is composed of two main subunits: a large catalytic alpha subunit and a smaller glycoprotein beta subunit. The beta subunit, including ATP1B2, plays a regulatory role by assembling alpha/beta heterodimers, which determine the number of sodium pumps transported to the plasma membrane . The beta-2 subunit specifically mediates cell adhesion of neurons and astrocytes and promotes neurite outgrowth .

Function

The primary function of ATP1B2 is to catalyze the hydrolysis of ATP, coupled with the exchange of Na+ and K+ ions across the plasma membrane. This process is vital for maintaining the resting potential, affecting transport, and regulating cellular volume . Although the exact function of the beta-2 subunit is not fully understood, it is known to play a role in cell adhesion and neurite outgrowth .

Role in the Human Body

ATP1B2 is involved in various physiological processes. It helps maintain the sodium and potassium gradients across the plasma membrane, which are used by animal cells for numerous processes, including secondary transport of molecules and rapid signaling . The sodium gradient is particularly crucial in organs like the kidneys, where it is utilized for filtering blood, reabsorbing glucose and amino acids, and regulating electrolytes and pH .

Recombinant Production in Sf9 Cells

Recombinant ATPase Transporting Beta 2 is often produced in Sf9 cells, a type of insect cell line derived from the fall armyworm. This system is widely used for the production of recombinant proteins due to its high expression levels and ability to perform post-translational modifications similar to those in mammalian cells .

Applications

Recombinant ATP1B2 has various applications in research and medicine. It is used to study the structure and function of the Na+/K+ ATPase enzyme, investigate its role in different physiological processes, and develop potential therapeutic interventions for diseases related to ion transport dysfunction .

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