Analytical Data
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Gene name
RALB
- Application
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Alternative Names
5730472O18Rik; dRalb; GTP binding protein; Ralb; RALB_HUMAN; RAS like protein B; RAS like proto oncogene B; Ras related GTP binding protein B; Ras-related protein Ral-B; v ral simian leukemia viral oncogene homolog B (ras related GTP binding protein); v ral simian leukemia viral oncogene homolog B (ras related); V ral simian leukemia viral oncogene homolog B
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P11234
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Expression Region
1-206aa
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Molecular Weight
50.1 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
RALB, a member of the Ral family of small GTPases, plays a critical role in various cellular processes, including cell proliferation, survival, and differentiation. As a key regulator of signaling pathways, RALB is implicated in cancer biology, particularly in promoting oncogenic signals that contribute to tumorigenesis and metastasis. Its activation is often associated with several malignancies, making it a potential biomarker for cancer diagnosis and a promising target for therapeutic intervention. Recent research has also highlighted RALB's involvement in modulating the immune response and its potential role in chronic inflammatory conditions. The study of RALB recombinant proteins has emerged as a significant area of interest for scientists seeking to better understand the molecular mechanisms underlying its activity and interactions within the cell. By creating RALB recombinant proteins, researchers can investigate the structural and functional aspects of this GTPase, providing insights into its role in health and disease. Additionally, these proteins serve as valuable tools for screening potential small molecule inhibitors that may disrupt RALB signaling pathways, offering hope for novel cancer therapies. Overall, the ongoing research on RALB recombinant proteins is crucial for advancing our knowledge of its biological functions and therapeutic potential, paving the way for innovative strategies in cancer treatment and other diseases related to aberrant RALB activity.
