Analytical Data
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Gene name
RHBDL2
- Application
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Alternative Names
Rhomboid-like protein 2
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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
Q9NX52
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Expression Region
12-132aa
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Molecular Weight
18.2 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
Related Products
Protein Description
RHBDL2 is a member of the rhomboid family of intramembrane serine proteases, which play crucial roles in various cellular processes, including signaling pathways and protein quality control. The study of RHBDL2 has garnered significant interest due to its involvement in key biological functions such as the regulation of epidermal growth factor receptor (EGFR) signaling and its potential implications in cancer biology and other diseases. Unlike other rhomboid proteases, RHBDL2 is known for its unique substrate specificity and its role in the regulated intramembrane proteolysis (RIP) of specific membrane proteins. Recent research has suggested its involvement in modulating the stability and activity of several signaling mediators, highlighting its potential as a therapeutic target. Understanding the structure-function relationship of RHBDL2 through recombinant protein studies could provide insights into its mechanism of action and pave the way for novel intervention strategies in diseases where RHBDL2 is dysregulated. As such, the development and characterization of RHBDL2 recombinant proteins are pivotal for elucidating its biological roles, investigating its interactions with substrates, and exploring its therapeutic potential in clinical settings.
