Analytical Data
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Gene name
PLEKHF1
- Application
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Alternative Names
Lysosome-associated apoptosis-inducing protein containing PH and FYVE domains (Apoptosis-inducing protein) (PH and FYVE domain-containing protein 1) (Phafin-1) (Zinc finger FYVE domain-containing protein 15) (APPD) (LAPF) (ZFYVE15)
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Species
Human
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Source
Baculovirus
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96S99
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Expression Region
1-279aa
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Molecular Weight
35.2 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
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Protein Description
PLEKHF1, a member of the pleckstrin homology domain-containing protein family, plays a significant role in cellular signaling and cytoskeletal dynamics. Recent studies have highlighted its involvement in various biological processes, including cell migration, proliferation, and differentiation, which are critical in both normal physiological functions and pathological conditions such as cancer. Despite its importance, the precise mechanisms by which PLEKHF1 exerts its effects remain poorly understood. The investigation of PLEKHF1 recombinant protein is essential for elucidating its structural and functional properties, as well as its interactions with other cellular molecules. By producing PLEKHF1 as a recombinant protein, researchers can facilitate detailed biochemical studies and structural analyses, which may reveal key insights into its role within signaling pathways. Furthermore, understanding the function of PLEKHF1 at the molecular level could provide potential therapeutic targets for diseases associated with its dysregulation. As such, the study of PLEKHF1 recombinant protein is poised to offer valuable contributions to the broader field of cell biology and pathology.
