Analytical Data
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Gene name
DOCK1
- Application
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Alternative Names
DOCK1；Dedicator of cytokinesis Protein 1
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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
Q14185
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Expression Region
全长
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AA Sequence
full
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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
DOCK1 (Dedicator of Cytokinesis 1) is a member of the DOCK family of guanine nucleotide exchange factors (GEFs) that play crucial roles in cellular signaling processes, particularly in the regulation of the actin cytoskeleton and cell motility. DOCK1 is known to activate Rac GTPases, which are pivotal in various biological processes, including cell migration, proliferation, and differentiation. Dysregulation of DOCK1 has been implicated in several diseases, including cancer, where it may contribute to tumor progression and metastasis. Given its significant role in disease pathogenesis, understanding the functional mechanisms of DOCK1 has garnered attention in biomedical research. The recombinant production of DOCK1 protein is essential for studying its structural and functional properties in vitro. The purification and characterization of this protein enable researchers to investigate its interactions with other cellular components and explore its potential as a therapeutic target. Advances in techniques such as protein expression systems and purification methods have facilitated the study of DOCK1, helping to elucidate its role in cellular dynamics and disease mechanisms.
