Analytical Data
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Gene name
CRKL
- Application
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Alternative Names
V-Crk Sarcoma Virus CT10 Oncogene Homolog(avian)-Like
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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 95% as determined by SDS-PAGE.
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Uniprot
P46109
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Expression Region
Met1~Glu303
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Molecular Weight
42kDa
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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
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Protein Description
Vps29, a key component of the retromer complex, plays a critical role in intracellular trafficking and endosomal sorting, particularly in the retrieval of proteins from endosomes to the trans-Golgi network. The retromer complex is essential for maintaining cellular homeostasis by regulating the recycling of transmembrane proteins, thereby influencing various cellular processes including signaling pathways, nutrient transport, and membrane protein composition. Dysfunction of Vps29 has been implicated in several neurodegenerative diseases, such as Alzheimer’s, where impaired endosomal trafficking contributes to the accumulation of misfolded proteins. Research on Vps29 recombinant protein involves elucidating its structural properties and understanding its functional mechanisms within the retromer complex. These studies aim to uncover how Vps29 interacts with other retromer components and its role in protein sorting. Such insights can facilitate the development of targeted therapeutic strategies for diseases associated with retromer dysfunction and may provide a framework for drug discovery aimed at enhancing protein recycling mechanisms within the cell. By generating and characterizing Vps29 in a recombinant form, researchers can further investigate its biochemical properties, interactions, and potential as a therapeutic target to correct trafficking defects in various pathological conditions.
