Recombinant Human CHMP6 Protein, N-His

Reference: YHK79601
Product nameRecombinant Human CHMP6 Protein, N-His
Origin speciesHuman
Expression systemProkaryotic expression
Molecular weight20.83 kDa
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°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)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypeThr14-Glu169
Aliases /SynonymshVps20, Charged multivesicular body protein 6, Vps20, Chromatin-modifying protein 6, Vacuolar protein sorting-associated protein 20, CHMP6, VPS20
ReferenceYHK79601
NoteFor research use only.

Description of Recombinant Human CHMP6 Protein, N-His

Introduction

Recombinant Human CHMP6 Protein, also known as Charged Multivesicular Body Protein 6, is a protein that plays a crucial role in the formation of multivesicular bodies (MVBs) in eukaryotic cells. MVBs are important for the sorting and degradation of cellular components, and CHMP6 is a key component of the ESCRT-III complex that is involved in this process. In this article, we will discuss the structure, activity, and applications of Recombinant Human CHMP6 Protein.

Structure of Recombinant Human CHMP6 Protein

The CHMP6 gene, located on chromosome 17, encodes for a protein consisting of 220 amino acids. The recombinant form of this protein is produced by cloning the CHMP6 gene into a suitable expression vector and expressing it in a host cell, typically Escherichia coli or Saccharomyces cerevisiae. The resulting protein has a molecular weight of approximately 25 kDa.

The CHMP6 protein contains three domains: an N-terminal helical domain, a central coiled-coil domain, and a C-terminal charged domain. The N-terminal helical domain is responsible for the interaction with other ESCRT-III proteins, while the coiled-coil domain is involved in the formation of the ESCRT-III complex. The C-terminal charged domain is thought to play a role in membrane binding and recognition.

Activity of Recombinant Human CHMP6 Protein

Recombinant Human CHMP6 Protein is involved in the formation of MVBs, which are specialized organelles responsible for the degradation of cellular components. This process, known as endosomal sorting, is crucial for maintaining cellular homeostasis and is also involved in various cellular processes such as cell signaling, receptor downregulation, and viral budding.

CHMP6 is a member of the ESCRT-III complex, which is composed of multiple proteins that work together to form a spiral-shaped filament on the surface of the endosomal membrane. This filament is thought to constrict the membrane, leading to the formation of intraluminal vesicles (ILVs) within the MVB. These ILVs are then released into the lumen of the MVB, where they are eventually degraded by lysosomal enzymes.

Applications of Recombinant Human CHMP6 Protein

Recombinant Human CHMP6 Protein has various applications in both basic research and biotechnology. In basic research, CHMP6 is used as a tool to study the mechanisms of endosomal sorting and the formation of MVBs. It can also be used in studies investigating the role of MVBs in various cellular processes.

In biotechnology, CHMP6 has potential applications in the development of novel drug delivery systems. The ESCRT-III complex, including CHMP6, has been shown to play a role in the release of exosomes, which are small vesicles secreted by cells. Exosomes have been studied as potential vehicles for drug delivery, and CHMP6 could potentially be used to enhance the targeting and release of drugs contained within these vesicles.

Conclusion

In summary, Recombinant Human CHMP6 Protein is a key component of the ESCRT-III complex involved in the formation of MVBs. Its structure, activity, and applications make it an important protein for both basic research and biotechnology. Further studies on CHMP6 and the ESCRT-III complex may lead to a better understanding of endosomal sorting and the development of novel drug delivery systems.

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