Analytical Data
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Gene name
SAR1A
- Application
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Alternative Names
COPII-associated small GTPase
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NR31
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Expression Region
1-198aa
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Molecular Weight
49.4 kDa
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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
SAR1A, a member of the Sar1 protein family, plays a crucial role in the early stages of the secretory pathway by mediating the budding of transport vesicles from the endoplasmic reticulum (ER). It functions as a small GTPase, cycling between an inactive GDP-bound state and an active GTP-bound form, which is essential for driving the assembly of coat protein complexes necessary for vesicle formation. Research on SAR1A has garnered significant attention due to its implications in various biological processes, including protein trafficking, maintaining ER structure, and cell signaling. Mutations or dysregulation of SAR1A have been associated with several diseases, including lipid metabolism disorders and certain types of cancer, highlighting its potential as a therapeutic target. Advancements in recombinant protein technology have enabled the production of SAR1A in large quantities, facilitating detailed studies of its structure and function. Understanding the precise mechanisms by which SAR1A regulates vesicle budding could provide valuable insights into broader cellular dynamics and disease mechanisms, positioning SAR1A as a vital subject in molecular and cell biology research.
