Analytical Data
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Gene name
RHBDD2
- Application
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Alternative Names
RHBDD2; RHBDL7; Rhomboid domain-containing protein 2
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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
Q6NTF9
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Expression Region
1-223 aa
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AA Sequence
MLGVTTVRSRMRRALVFGMVVPSVLVPWLLLGASWLIPQTSFLSNVCGLSIGLAYGLTYCYSIDLSERVALKLDQTFPFSLMRRISVFKYVSGSSAERRAAQSRKLNPVPGSYPTQSCHPHLSPSHPVSQTQHASGQKLASWPSCTPGHMPTLPPYQPASGLCYVQNHFGPNPTSSSVYPASAGTSLGIQPPTPVNSPGTVYSGALGTPGAAGSKESSRVPMP
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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
RHBDD2, also known as RING finger and HD domain containing E3 ubiquitin-protein ligase 2, has emerged as a pivotal protein in cellular signaling and protein degradation pathways. This E3 ligase plays a crucial role in the ubiquitin-proteasome system, which regulates various cellular processes such as cell cycle progression, apoptosis, and responses to stress. Research has shown that RHBDD2 is involved in endoplasmic reticulum-associated degradation (ERAD), a mechanism that eliminates misfolded proteins from the endoplasmic reticulum, thereby ensuring cellular homeostasis and preventing the accumulation of potentially toxic aggregates. Dysregulation of RHBDD2 expression has been linked to various diseases, including cancer and neurodegenerative disorders, highlighting its potential as a therapeutic target. Recent studies have focused on characterizing the structural and functional properties of RHBDD2 to better understand its role in disease pathways. The generation of recombinant RHBDD2 proteins allows researchers to investigate its enzymatic activity and interaction with substrates in vitro, contributing to the elucidation of its biological functions. Understanding the molecular mechanisms underlying RHBDD2's activity could pave the way for novel strategies to manipulate its function for therapeutic purposes. Furthermore, as the field of targeted protein degradation continues to advance, RHBDD2 stands out as a candidate for the development of small-molecule modulators that can adjust its ligase activity, thereby offering new avenues for experimental and clinical applications in disease management.
