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Brand: ProteoGenix

Recombinant Human ATP6V1D Protein, N-His

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

329.00

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Met1–Glu247
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Recombinant Human ATP6V1D Protein, N-His

Recombinant Human ATP6V1D Protein, N-His

Product name Recombinant Human ATP6V1D Protein, N-His
Origin species Human
Expression system Prokaryotic expression
Molecular weight 30.43 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 Met1-Glu247
Aliases /Synonyms ATP6M, V-ATPase subunit D, Vacuolar proton pump subunit D, VATD, ATP6V1D, V-type proton ATPase subunit D, V-ATPase 28 kDa accessory protein
Reference ARO-P11784
Note For research use only.
Molecular Constructor
Met1–Glu247

Introduction

Recombinant proteins have become essential tools in scientific research and biotechnology due to their ability to mimic naturally occurring proteins and perform specific functions in various biological processes. One such protein is the Recombinant Human ATP6V1D Protein, which has gained significant attention in recent years due to its diverse roles in cellular physiology and potential therapeutic applications.

Structure of Recombinant Human ATP6V1D Protein

The Recombinant Human ATP6V1D Protein, also known as V-type proton ATPase subunit D, is a subunit of the vacuolar ATPase (V-ATPase) complex. This protein is composed of 365 amino acids and has a molecular weight of approximately 41 kDa. The primary structure of this protein is highly conserved among different species, indicating its essential role in cellular function.

The ATP6V1D protein consists of three main domains: an N-terminal cytoplasmic domain, a transmembrane domain, and a C-terminal domain. The N-terminal domain is responsible for the binding of ATP, while the transmembrane domain forms the proton channel and is essential for the proton pumping activity of the V-ATPase complex. The C-terminal domain is involved in protein-protein interactions and plays a crucial role in the assembly and stability of the V-ATPase complex.

Activity of Recombinant Human ATP6V1D Protein

The primary function of the Recombinant Human ATP6V1D Protein is to regulate the acidification of cellular compartments by pumping protons from the cytoplasm into the lumen of various organelles. This process is crucial for maintaining the proper pH balance and creating an acidic environment necessary for the functioning of enzymes and other cellular processes. Additionally, the ATP6V1D protein is involved in the transport of various molecules, such as neurotransmitters, metabolites, and ions, across cellular membranes.

Moreover, recent studies have shown that the ATP6V1D protein plays a significant role in cellular signaling and gene expression. It has been found to interact with various signaling molecules and transcription factors, thereby modulating their activity and affecting cellular processes, such as cell proliferation, differentiation, and apoptosis.

Application of Recombinant Human ATP6V1D Protein

The diverse functions of the Recombinant Human ATP6V1D Protein make it a valuable tool in various research areas, such as cell biology, biochemistry, and pharmacology. Its ability to regulate pH and transport molecules across cellular membranes makes it an essential component in studying cellular processes and identifying potential drug targets.

Furthermore, the ATP6V1D protein has been implicated in several diseases, including cancer, osteoporosis, and neurological disorders. Therefore, it has potential therapeutic applications, and recombinant forms of this protein are being studied for their efficacy in treating these conditions. For instance, the ATP6V1D protein has been found to be overexpressed in various cancer cells, and targeting its activity has shown promising results in inhibiting cancer cell growth.

Conclusion

The Recombinant Human ATP6V1D Protein is a crucial component of the V-ATPase complex and plays diverse roles in cellular physiology. Its structure, activity, and potential applications make it an essential tool for scientific research and a potential therapeutic target for various diseases. Further studies on this protein will provide valuable insights into its functions and potential therapeutic applications.

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