Analytical Data
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Gene name
RHBDL3
- Application
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Alternative Names
RHBDL3; RHBDL4; VRHO; Rhomboid-related protein 3; Ventrhoid transmembrane protein
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P58872
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Expression Region
1-306 aa
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AA Sequence
MSNKRSNSFRQAILQGNRRLSSKALLEEKGLSLSQRLIRHVAYETLPREIDRKWYYDSYTCCPPPWFMITVTLLEVAFFLYNGVSLGQFVLQVTHPRYLKNSLVYHPQLRAQVWRYLTYIFMHAGIEHLGLNVVLQLLVGVPLEMVHGATRIGLVYVAGVVAGSLAVSVADMTAPVVGSSGGVYALVSAHLANIVMNWSGMKCQFKLLRMAVALICMSMEFGRAVWLRFHPSAYPPCPHPSFVAHLGGVAVGITLGVVVLRNYEQRLQDQSLWWIFVAMYTVFVLFAVFWNIFAYTLLDLKLPPPP
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Molecular Weight
60.9 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
RHBDL3, a member of the rhomboid protease family, has emerged as a significant focus of research due to its vital role in cellular processes and disease mechanisms. Located in the endoplasmic reticulum, RHBDL3 is involved in the regulated intramembrane proteolysis of various substrates, including the Notch signaling pathway components and other key proteins related to cell fate determination and differentiation. Its unique mechanism of action in cleaving membrane proteins has implications for understanding how cells communicate and respond to external signals. Furthermore, aberrant RHBDL3 activity has been linked to various pathological conditions, such as cancer, where its dysregulation can contribute to tumor progression and metastasis. Investigating RHBDL3's functional roles and regulatory mechanisms could uncover potential therapeutic targets for diseases influenced by proteolytic processes. Given the increasing recognition of the importance of rhomboid proteases in both normal physiology and disease states, research on RHBDL3 is crucial for elucidating its biological significance and potential as a biomarker or therapeutic target. Understanding the intricate details of RHBDL3's function and interactions may pave the way for innovative treatments that leverage its proteolytic activity in clinical applications. As a result, RHBDL3 stands out as a promising candidate for further exploration in the context of protease biology and its implications in health and disease.
