Analytical Data
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Gene name
ARL6IP5
- Application
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Alternative Names
ARL6IP5; DERP11; JWA; PRA2; PRAF3; HSPC127; PRA1 family Protein 3
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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
O75915
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Expression Region
1-64aa
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AA Sequence
MDVNIAPLRAWDDFFPGSDRFARPDFRDISKWNNRVVSNLLYYQTNYLVVAAMMISIVGFLSPF
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Molecular Weight
32.78 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
ARL6IP5, also known as ADP-ribosylation factor-like 6 interacting protein 5, is a protein of significant interest due to its potential role in cellular processes such as intracellular trafficking and cytoskeletal dynamics. Recent studies have suggested that ARL6IP5 may be involved in regulating mitochondrial function and apoptosis, making it a candidate for exploration in various disease contexts, including neurodegenerative disorders and cancer. Understanding the structure and function of ARL6IP5 through recombinant protein studies can provide insights into its biological mechanisms. Additionally, the ability to produce ARL6IP5 in a recombinant form allows researchers to study its interactions with other cellular proteins and its role in signaling pathways. These investigations may pave the way for novel therapeutic strategies targeting ARL6IP5-related pathways, highlighting the importance of this protein in health and disease. The exploration includes assessing its functional domains, interaction networks, and post-translational modifications, which contribute to its activity and regulatory mechanisms within the cell. Overall, ARL6IP5 is poised to be a valuable subject of research, with implications that extend to diverse areas of molecular and cellular biology.











