Analytical Data
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Gene name
MPP5
- Application
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Alternative Names
PALS1; Stardust; MAGUK P55 Subfamily Member 5
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8N3R9
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Expression Region
Asn455~Arg675
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Molecular Weight
33kDa
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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
The study of MPP5 (Membrane Protein, Palmitoylated 5) recombinant protein is grounded in its critical role in cellular processes, particularly in maintaining epithelial cell structure and function. MPP5 is a member of the MAGUK (Membrane-Associated Guanylate Kinase) protein family and is known to be involved in the organization of protein complexes at the cell membrane, facilitating interactions between various signaling molecules and maintaining tight junction integrity. Research has revealed that MPP5 is implicated in numerous physiological processes, including cell proliferation, differentiation, and signaling pathways vital for cellular homeostasis. Additionally, its dysregulation has been linked to various pathological conditions, such as cancer and neurodegenerative diseases, highlighting its potential as a therapeutic target. Investigating MPP5's structure-function relationships through recombinant protein techniques allows for a deeper understanding of its molecular mechanisms and interactions with other proteins. This knowledge is essential for the development of novel therapeutic approaches aimed at correcting MPP5-related dysfunctions or enhancing its normal functions, thereby contributing to advancements in disease management and treatment strategies. The innovative application of recombinant protein technology in this context not only provides insights into fundamental biological processes but also paves the way for future biomedical applications.
