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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

319.00

100ug + 319 loyalty points
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

Introduction

Recombinant Human VAPB Protein, also known as VAMP-associated protein B (VAPB), is a highly conserved protein that plays a crucial role in various cellular processes. This protein is encoded by the VAPB gene and is found in both humans and animals. Recombinant Human VAPB Protein is produced through recombinant DNA technology and has gained significant attention in the scientific community due to its unique structure, diverse activities, and potential applications.

Structure of Recombinant Human VAPB Protein

Recombinant Human VAPB Protein is a transmembrane protein that consists of 243 amino acids and has a molecular weight of approximately 33 kDa. It contains a conserved 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. The protein also has a hydrophobic transmembrane domain that anchors it to the endoplasmic reticulum (ER) membrane.

Activity of Recombinant Human VAPB Protein

Recombinant Human VAPB Protein is primarily involved in the regulation of ER-mitochondria contact sites, which are critical for various cellular functions such as calcium signaling, lipid metabolism, and apoptosis. It interacts with multiple proteins, including the ER-resident protein, VAP-A, and the mitochondria-associated protein, PTPIP51, to form the VAPB-PTPIP51 complex. This complex plays a crucial role in maintaining the structural and functional integrity of the ER-mitochondria contact sites.

Moreover, Recombinant Human VAPB Protein has been shown to regulate the transport of lipids and proteins between the ER and the Golgi apparatus. It also plays a role in the formation of autophagosomes, which are involved in the degradation of damaged organelles and proteins. Additionally, this protein has been linked to the regulation of synaptic function and neuronal survival, making it a potential therapeutic target for neurodegenerative diseases.

Application of Recombinant Human VAPB Protein

Recombinant Human VAPB Protein has a wide range of applications in both basic research and biotechnology. In basic research, this protein is used to study the structure and function of ER-mitochondria contact sites and their role in various cellular processes. It is also used to investigate the mechanisms of neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS) and spinal muscular atrophy (SMA), which have been linked to mutations in the VAPB gene.

In biotechnology, Recombinant Human VAPB Protein is used for protein-protein interaction studies and drug discovery. Its ability to interact with multiple proteins makes it a valuable tool for identifying potential drug targets and developing new therapies for various diseases. Moreover, this protein can be used as an antigen in the production of antibodies for research and diagnostic purposes.

Conclusion

In conclusion, Recombinant Human VAPB Protein is a highly conserved transmembrane protein that plays a crucial role in regulating ER-mitochondria contact sites and various cellular processes. Its unique structure and diverse activities make it a valuable tool for basic research and biotechnology applications. Further studies on this protein could lead to a better understanding of its role in disease pathogenesis and the development of novel therapeutics.

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