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Brand: ProteoGenix

Recombinant Human VAPB Protein, N-His

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

$380.00

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Met1–Glu124
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Recombinant Human VAPB Protein, N-His

Recombinant Human VAPB Protein, N-His

Product name Recombinant Human VAPB Protein, N-His
Origin species Human
Expression system Prokaryotic expression
Molecular weight 16.25 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-Glu124
Aliases /Synonyms VAMP-B/VAMP-C, VAPB, VAP-B/VAP-C, Vesicle-associated membrane protein-associated protein B/C, VAMP-associated protein B/C
Reference ARO-P12480
Note For research use only.
Molecular Constructor
Met1–Glu124

Recombinant Human VAPB Protein: Structure, Activity, and Applications

Introduction

Recombinant proteins are proteins that are produced through genetic engineering techniques, where the DNA sequence of a desired protein is inserted into a host organism for production. Recombinant human VAPB protein is a type of recombinant protein that has gained significant attention in the scientific community due to its potential therapeutic applications. In this article, we will discuss the structure, activity, and applications of recombinant human VAPB protein.

Structure of Recombinant Human VAPB Protein

The human VAPB (vesicle-associated membrane protein-associated protein B) gene encodes a type II integral membrane protein that is composed of 243 amino acids. The recombinant human VAPB protein is a homodimer, with each monomer consisting of an N-terminal major sperm protein (MSP) domain and a C-terminal coiled-coil domain. The MSP domain is responsible for protein-protein interactions, while the coiled-coil domain is involved in membrane binding and vesicle trafficking.

Activity of Recombinant Human VAPB Protein

The main function of VAPB protein is to regulate intracellular membrane trafficking and lipid metabolism. It is also involved in the formation of endoplasmic reticulum (ER)-mitochondria contact sites, which play a crucial role in cellular processes such as calcium signaling, lipid transfer, and apoptosis. Recombinant human VAPB protein has been shown to interact with various proteins, including amyotrophic lateral sclerosis 8 (ALS8) protein, which is linked to the development of ALS, a progressive neurodegenerative disease.

Applications of Recombinant Human VAPB Protein

Due to its role in regulating cellular processes, recombinant human VAPB protein has potential applications in various fields, including medicine, biotechnology, and research. Some of the key applications of this protein are:

  • Therapeutic Applications: Studies have shown that mutations in the VAPB gene are linked to the development of ALS and other neurodegenerative diseases. Recombinant human VAPB protein can be used as a potential therapeutic agent for these diseases by modulating its activity and interactions with other proteins.
  • Biotechnology: Recombinant human VAPB protein can be used in the production of liposomes, which are lipid-based vesicles that can be loaded with drugs or genetic material for targeted delivery. VAPB protein’s role in membrane trafficking and lipid metabolism makes it a valuable tool for the development of liposomal drug delivery systems.
  • Research: The study of recombinant human VAPB protein has provided valuable insights into the mechanisms of ER-mitochondria contact sites and their role in cellular processes. This protein can also be used as a tool in various research studies to investigate its interactions with other proteins and their effects on cellular functions.

Conclusion

In summary, recombinant human VAPB protein is a homodimeric protein with a unique structure and diverse functions. Its role in regulating cellular processes and its potential therapeutic applications make it a

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