Analytical Data
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Gene name
CYTH1
- Application
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Alternative Names
CYT1; B2-1; SEC7; PSCD1; Pleckstrin Homology,Sec7 And Coiled-Coil Domains 1
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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
Q15438
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Expression Region
Met1~His398
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Molecular Weight
50kDa
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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
Cyth1, or cytohesin-1, is a member of the cytohesin family of guanine nucleotide exchange factors (GEFs) that play crucial roles in intracellular signaling and membrane trafficking. It is primarily involved in the regulation of small GTPases, particularly the Arf (ADP-ribosylation factor) family, which are essential for endocytosis and vesicle transport. Cyth1 has garnered significant attention due to its implications in various cellular processes, including cell adhesion, migration, and tumorigenesis. Abnormal expression or dysfunction of Cyth1 has been linked to several diseases, including cancer and metabolic disorders, highlighting its potential as a therapeutic target. Research into the structure and function of Cyth1 recombinant protein is essential for understanding its mechanistic role in cellular signaling pathways. By producing and characterizing this protein, scientists aim to elucidate how Cyth1 interacts with its GTPase targets and other molecular partners, which will provide insights into its biological functions. Additionally, the development of specific inhibitors or modulators targeting Cyth1 could lead to novel therapeutic strategies for diseases associated with its dysregulation. Studies are therefore focusing on the purification and functional analysis of Cyth1, with the goal of establishing its role in health and disease, ultimately paving the way for innovative treatment modalities.
