Analytical Data
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Gene name
CHMP2A
- Application
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Alternative Names
CHMP2A；BC2；CHMP2；Charged multivesicular body Protein 2a
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O43633
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Expression Region
1-222aa
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AA Sequence
MDLLFGRRKTPEELLRQNQRALNRAMRELDRERQKLETQEKKIIADIKKMAKQGQMDAVRIMAKDLVRTRRYVRKFVLMRANIQAVSLKIQTLKSNNSMAQAMKGVTKAMGTMNRQLKLPQIQKIMMEFERQAEIMDMKEEMMNDAIDDAMGDEEDEEESDAVVSQVLDELGLSLTDELSNLPSTGGSLSVAAGGKKAEAAASALADADADLEERLKNLRRD
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Molecular Weight
52.1kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
CHMP2A (charged multivesicular body protein 2A) is an essential component of the endosomal sorting complexes required for transport (ESCRT) machinery, which plays a critical role in intracellular membrane trafficking, particularly in the formation and budding of multivesicular bodies (MVBs). The study of CHMP2A recombinantly expressed proteins has gained significant attention due to its implications in various cellular processes, including receptor downregulation, autophagy, and the inward budding of membrane proteins. Mutations or dysregulation in CHMP2A have been associated with several pathological conditions, including neurodegenerative diseases and certain cancers, indicating its potential as a therapeutic target. Recent advancements in recombinant protein technology have enabled the production of CHMP2A proteins, allowing researchers to investigate their structural properties, functional dynamics, and interactions with other ESCRT components. Understanding CHMP2A's role in cellular mechanisms not only enhances our knowledge of fundamental biological processes but also opens avenues for developing innovative strategies for disease intervention. As the field evolves, the characterization of CHMP2A reconstituted in vitro systems alongside advanced imaging techniques will further elucidate its contributions to cellular homeostasis and pathology, making it a focal point for future research in cell biology and therapeutic development.
