Analytical Data
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Gene name
RHBDL2
- Application
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Alternative Names
RHBDL2；Rhomboid-related Protein 2
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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
Q9NX52
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Expression Region
12-132aa
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AA Sequence
MNLNMGREMKEELEEEEKMREDGGGKDRAKSKKVHRIVSKWMLPEKSRGTYLERANCFPPPVFIISISLAELAVFIYYAVWKPQKQWITLDTGILESPFIYSPEKREEAWRFISYMLVHAG
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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 (Rhomboid-5-like 2) is a member of the rhomboid protease family, known for their role in intramembrane proteolysis. Research into RHBDL2 has gained momentum due to its implications in various biological processes, including the regulation of protein turnover, cellular signaling pathways, and development. This enzyme is thought to participate in the modulation of the Notch signaling pathway, which is crucial for cell fate determination and tissue patterning. Dysregulation of RHBDL2 has been linked to several diseases, including cancer, where it may influence tumor progression and metastasis. Given its potential as a therapeutic target, the study of RHBDL2's structure, function, and substrate specificity is pivotal. Scientists aim to elucidate the molecular mechanisms underlying RHBDL2's activity, as well as its interactions with other cellular components. Understanding its role at a mechanistic level could pave the way for developing novel interventions in diseases associated with aberrant rhomboid protease activity. Additionally, RHBDL2's evolutionary conservation across species highlights its fundamental biological importance, making it a target of interest not only in human health but also in broader biological research.
