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Brand: ProteoGenix

Recombinant Mouse BTN2A2 Protein, N-His

  • ARO-P10998
Host species:
Escherichia coli (E.coli)
Origin species:
Mouse
Molecular weight:
25.96 kDa

329.00

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Thr32–Ile237
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Recombinant Mouse BTN2A2 Protein, N-His

Recombinant Mouse BTN2A2 Protein, N-His

Product name Recombinant Mouse BTN2A2 Protein, N-His
Origin species Mouse
Expression system Prokaryotic expression
Molecular weight 25.96 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 Thr32-Ile237
Aliases /Synonyms Butyrophilin subfamily 2 member A2, Btn2a2
Reference ARO-P10998
Note For research use only.
Molecular Constructor
Thr32–Ile237

Introduction

Recombinant Mouse BTN2A2 Protein, also known as Butyrophilin 2A2, is a membrane glycoprotein that is encoded by the BTN2A2 gene in mice. It belongs to the butyrophilin (BTN) family of proteins, which are characterized by their conserved extracellular immunoglobulin (Ig) domain and variable transmembrane and cytoplasmic regions. Recombinant Mouse BTN2A2 Protein is a recombinant form of this protein that is produced using recombinant DNA technology. It has been extensively studied for its structure, activity, and potential applications in various fields of research.

Structure of Recombinant Mouse BTN2A2 Protein

The structure of Recombinant Mouse BTN2A2 Protein consists of a single polypeptide chain of 542 amino acids. It contains a signal peptide at the N-terminus, followed by an extracellular Ig domain, a transmembrane region, and a cytoplasmic tail. The extracellular Ig domain is responsible for protein-protein interactions, while the transmembrane region anchors the protein to the cell membrane. The cytoplasmic tail is involved in intracellular signaling and regulation of protein function.

Activity of Recombinant Mouse BTN2A2 Protein

Recombinant Mouse BTN2A2 Protein has been shown to have diverse activities in different cellular processes. It is primarily expressed in immune cells, such as T cells, B cells, and natural killer (NK) cells, and has been implicated in the regulation of immune response. It has been reported to interact with other proteins, such as CD3, CD28, and CD8, and modulate T cell activation and proliferation. It has also been shown to play a role in the development and function of NK cells.

Furthermore, Recombinant Mouse BTN2A2 Protein has been found to have a significant role in lipid metabolism. It is highly expressed in the lactating mammary gland and has been shown to bind to milk lipids, such as triacylglycerols, and facilitate their secretion into milk. This activity is thought to be essential for the proper development and function of the mammary gland.

Application of Recombinant Mouse BTN2A2 Protein

The unique structure and diverse activities of Recombinant Mouse BTN2A2 Protein make it a valuable tool in various research fields. It has been extensively used as an antigen in immunological studies, particularly in the investigation of T cell and NK cell function. Its ability to interact with other proteins and modulate immune responses makes it a promising target for immunotherapy and vaccine development.

In addition, Recombinant Mouse BTN2A2 Protein has been utilized in the study of lipid metabolism and its role in lactation. Its binding activity to milk lipids has been exploited to develop recombinant forms of this protein for potential use in the dairy industry. These recombinant proteins have the potential to improve milk production and composition, as well as the overall health of lactating animals.

Conclusion

Recombinant Mouse BTN2A2 Protein is a unique protein with a multifaceted structure and diverse activities. Its role in immune response and lipid metabolism has been extensively studied, and its potential applications in various research fields are being explored. With further research and development, this protein has the potential to contribute significantly to the fields of immunology, lipid biology, and dairy science.

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