Analytical Data
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Gene name
DOCK4
- Application
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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
Q8N1I0
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Expression Region
Met1~Pro300
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Molecular Weight
39kDa
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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
DOCK4 (Dedicator of Cytokinesis 4) is a member of the DOCK family of proteins, known as guanine nucleotide exchange factors (GEFs) that activate small GTPases, particularly Rac1, which play a crucial role in regulating various cellular processes, including cytoskeletal dynamics, migration, and cell division. Researchers have increasingly focused on DOCK4 due to its potential involvement in cancer progression and metastasis, as well as its role in immune response modulation. Aberrant expression of DOCK4 has been associated with various malignancies, highlighting its significance in cancer biology. Moreover, studies suggest that DOCK4 may participate in the inflammatory response and immune cell signaling, making it a potential therapeutic target for inflammatory diseases. Understanding the structural and functional characteristics of DOCK4, including its protein-protein interactions and regulatory mechanisms, is essential for elucidating its biological roles and therapeutic potentials. Recent advancements in recombinant protein technology have enabled researchers to produce and characterize DOCK4 at a molecular level, providing insights into its function in both healthy and diseased states. As such, the study of DOCK4 recombinant proteins is crucial for deciphering the intricacies of cellular signaling pathways and developing novel strategies for cancer and immune-related therapies.
