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Brand: ProteoGenix

Recombinant Human ATP6V1B2 Protein, N-His

Host species:
Escherichia coli (E.coli)
Origin species:
Human
Molecular weight:
53.56 kDa

$392.00

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Ser51–His511
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Recombinant Human ATP6V1B2 Protein, N-His

Recombinant Human ATP6V1B2 Protein, N-His

Product name Recombinant Human ATP6V1B2 Protein, N-His
Origin species Human
Expression system Prokaryotic expression
Molecular weight 53.56 kDa
Buffer Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Delivery condition Dry Ice
Delivery lead time in business days 3-5 days if in stock; 3-5 weeks if production needed
Storage condition 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
Brand ProteoGenix
Host species Escherichia coli (E.coli)
Fragment Type Ser51-His511
Aliases /Synonyms Endomembrane proton pump 58 kDa subunit, ATP6B2, V-type proton ATPase subunit B, brain isoform, HO57, VPP3, Vacuolar proton pump subunit B 2, ATP6V1B2, V-ATPase subunit B 2
Reference ARO-P12252
Note For research use only.
Molecular Constructor
Ser51–His511

Introduction

Recombinant Human ATP6V1B2 Protein, also known as ATPase H+ transporting V1 subunit B2, is a protein that plays a crucial role in the cellular process of acidification. This protein is encoded by the ATP6V1B2 gene and is a subunit of the vacuolar ATPase (V-ATPase) complex. In this article, we will discuss the structure, activity, and applications of this important protein.

Structure of Recombinant Human ATP6V1B2 Protein

The human ATP6V1B2 protein is composed of 347 amino acids with a molecular weight of approximately 38 kDa. It belongs to the V-ATPase B subfamily and contains a conserved ATPase domain. The protein has a transmembrane domain that allows it to be embedded in the membrane of acidic organelles such as lysosomes and endosomes. It also has a cytoplasmic domain that interacts with other subunits of the V-ATPase complex.

Activity of Recombinant Human ATP6V1B2 Protein

The main function of the ATP6V1B2 protein is to act as a subunit of the V-ATPase complex, which is responsible for acidifying the interior of various cellular compartments. This acidification is crucial for a variety of cellular processes, including protein degradation, receptor-mediated endocytosis, and neurotransmitter release. The ATP6V1B2 protein plays a key role in regulating the activity of the V-ATPase complex, which is essential for maintaining the proper pH balance within the cell.

In addition to its role in acidification, the ATP6V1B2 protein has been found to have other functions as well. Studies have shown that it is involved in the regulation of cell migration and invasion, as well as in the formation of lysosomal exocytosis. It has also been linked to the regulation of autophagy, a process that helps to maintain cellular homeostasis by degrading damaged organelles and proteins.

Application of Recombinant Human ATP6V1B2 Protein

The recombinant form of the ATP6V1B2 protein has been widely used in various research applications. It is commonly used as an antigen in antibody production, as it is highly immunogenic and can elicit a strong immune response. This makes it a valuable tool for studying the structure and function of the V-ATPase complex.

Furthermore, the ATP6V1B2 protein has been studied for its potential as a therapeutic target. Dysregulation of the V-ATPase complex has been linked to various diseases, including cancer and neurodegenerative disorders. As the ATP6V1B2 protein plays a crucial role in the activity of this complex, targeting it could potentially lead to the development of new treatments for these diseases.

In addition, the ATP6V1B2 protein has been used in drug discovery studies. By understanding its structure and function, researchers can identify potential inhibitors or activators of the V-ATPase complex, which could lead to the development of new drugs for various conditions.

Conclusion

Recombinant Human ATP6V1B2 Protein is an important protein that plays a crucial role in the cellular process of acidification. Its structure, activity, and applications have been extensively studied, and it has been found to have multiple functions in addition to its role in acidification. With its potential as a therapeutic target and its use in research and drug discovery, this protein continues to be a subject of interest for scientists in various fields.

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