Recombinant Proteins

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ATP1B1 Human

ATPase Transporting Beta 1 Human Recombinant

Recombinant Human ATP1B1, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 264 amino acids (residues 63-303) and has a molecular weight of 30.4 kDa. The protein includes a 23 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21868
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

ATP1B1 Human, Sf9

ATPase Transporting Beta 1 Human Recombinant, Sf9

Recombinant Human ATP1B1, produced in Sf9 Baculovirus cells, is a single glycosylated polypeptide chain comprising 250 amino acids (residues 63-303). With a molecular weight of 29 kDa, it appears as a band at approximately 28-40 kDa on SDS-PAGE analysis. The protein is expressed with a C-terminal 6-amino acid His tag and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21957
Source
Sf9, Baculovirus cells.
Appearance
A clear, colorless solution that has been sterilized by filtration.

ATP1B2 Human

ATPaseTransporting Beta 2 Human Recombinant

Recombinant ATP1B2, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 246 amino acids (68-246). It has a molecular weight of 27.8 kDa. This protein is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22017
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized through filtration.

ATP1B2 Human, Sf9

ATPase Transporting Beta 2 Human Recombinant, Sf9

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.
Shipped with Ice Packs
Cat. No.
BT22110
Source
Sf9, Baculovirus cells.
Appearance
The product is a sterile, colorless, and clear solution.

ATP1B3 Human

ATPaseTransporting Beta 3 Human Recombinant

Recombinantly produced in E.coli, ATP1B3 Human is a single, non-glycosylated polypeptide chain comprising 246 amino acids (57-279) with a molecular mass of 27.4 kDa. This protein is fused to a 23 amino acid His-tag at the N-terminus and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22181
Source
Escherichia Coli.
Appearance
The solution is colorless, sterile, and has been filtered.

ATP6AP2 Human

ATPase Transporting Lysosomal Accessory Protein 2 Human Recombinant

Recombinant human ATP6AP2, expressed in E. coli, is available as a single, non-glycosylated polypeptide chain. This protein consists of 296 amino acids, including a 10 amino acid N-terminal His-tag, resulting in a calculated molecular mass of 33 kDa.
Shipped with Ice Packs
Cat. No.
BT22244
Source
Escherichia Coli.
Appearance
White, lyophilized powder after filtration.

ATP6V1F Human

ATPase Transporting, Lysosomal V1 Subunit F Human Recombinant

Recombinant ATP6V1F Human, produced in E.Coli, is a single, non-glycosylated polypeptide chain comprising 142 amino acids (specifically, amino acids 1 to 119). With a molecular mass of 15.8 kDa, this protein features a 23 amino acid His-tag at its N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22313
Source
Escherichia Coli.
Appearance
A clear solution that has undergone sterile filtration.

ATPIF1 Human

ATPase Inhibitory Factor 1 Human Recombinant

This product is a recombinant human ATPIF1 protein produced in E. coli. It is a single, non-glycosylated polypeptide chain consisting of 106 amino acids (residues 26-106) with a molecular weight of 12.2 kDa. The protein includes a 25 amino acid His-tag at the N-terminus to facilitate purification. This recombinant ATPIF1 protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22378
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.
Definition and Classification

ATPases (Adenosine Triphosphatases) are a class of enzymes that catalyze the decomposition of ATP into ADP and a free phosphate ion. This reaction releases energy, which the enzyme harnesses to drive other chemical reactions that would not otherwise occur . ATPases are classified into several types based on their structure and function, including F-type, V-type, A-type, and P-type ATPases .

Biological Properties

ATPases are integral membrane proteins that play crucial roles in various biological processes. They are expressed in almost all tissues and are essential for maintaining cellular homeostasis . The expression patterns and tissue distribution of ATPases vary depending on the specific type of ATPase. For example, Na+/K±ATPase is predominantly found in the plasma membrane of animal cells, while V-ATPases are located in the membranes of intracellular organelles such as lysosomes and endosomes .

Biological Functions

ATPases are involved in a wide range of biological functions. They are essential for active transport, muscle contraction, protein folding, and cellular signaling . Na+/K±ATPase, for instance, helps maintain the resting potential of cells, regulates cellular volume, and functions as a signal transducer . ATPases also play roles in immune responses and pathogen recognition by regulating the activity of immune cells and facilitating the transport of antigens .

Modes of Action

ATPases function by binding to ATP and hydrolyzing it to ADP and inorganic phosphate. This hydrolysis reaction releases energy, which is used to drive conformational changes in the ATPase enzyme, allowing it to transport ions or other molecules across membranes . ATPases interact with various binding partners and are involved in downstream signaling cascades that regulate cellular processes .

Regulatory Mechanisms

The expression and activity of ATPases are tightly regulated by various mechanisms. Transcriptional regulation involves the control of ATPase gene expression by transcription factors and other regulatory proteins . Post-translational modifications, such as phosphorylation and ubiquitination, also play crucial roles in modulating ATPase activity and stability . Additionally, ATPase activity can be regulated by reversible disassembly and reassembly of the enzyme complex .

Applications

ATPases have numerous applications in biomedical research, diagnostics, and therapeutics. They are used as targets for drug discovery, with ATPase inhibitors being developed for the treatment of various diseases, including cancer and cardiovascular disorders . ATPase activity assays are employed to screen chemical compound libraries for potential enzyme inhibitors and to measure inhibitor potency . ATPases also serve as diagnostic markers for certain diseases and are used in the development of therapeutic strategies .

Role in the Life Cycle

ATPases play vital roles throughout the life cycle, from development to aging and disease. During development, ATPases are involved in cell differentiation, tissue formation, and organ development . In adulthood, they maintain cellular homeostasis and support various physiological functions. As organisms age, changes in ATPase activity can contribute to the development of age-related diseases and conditions . Dysregulation of ATPase activity is also associated with various pathological conditions, including neurodegenerative diseases and cancer .

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