Analytical Data
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Gene name
HRBL
- Application
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Alternative Names
AGFG2; HRBL; RABR; Arf-GAP domain and FG repeat-containing protein 2; HIV-1 Rev-binding protein-like protein; Rev/Rex activation domain-binding protein related; RAB-R
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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
O95081
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Expression Region
1-155aa
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AA Sequence
MVMAAKKGPGPGGGVSGGKAEAEAASEVWCRRVRELGGCSQAGNRHCFECAQRGVTYVDITVGSFVCTTCSGLLRGLNPPHRVKSISMTTFTEPEVVFLQSRGNEVCRKIWLGLFDARTSLVPDSRDPQKVKEFLQEKYEKKRWPDTFPRRLCQL
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Molecular Weight
43.6 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
HRBL (Human RNA-binding protein with a leucine-rich repeat) is a member of the RNA-binding protein family, which plays a crucial role in various cellular processes including RNA splicing, stability, and translation. The study of HRBL has gained significant attention due to its involvement in vital biological functions and its potential implications in various diseases, particularly cancer. Abnormal expression of RNA-binding proteins like HRBL has been linked to the progression of tumors, making it a critical target for therapeutic intervention. Recent advances in molecular biology and bioinformatics have enabled researchers to probe deeper into the structure and function of HRBL, revealing its interactions with RNA and other cellular components. Furthermore, HRBL's distinctive leucine-rich repeats suggest that it may have unique binding properties that could be exploited for drug design and development. Understanding the mechanisms by which HRBL exerts its effects on gene regulation can provide valuable insights into both fundamental biology and potential clinical applications. Therefore, ongoing research is focused on elucidating the molecular pathways involving HRBL and assessing its utility as a biomarker for disease prognosis or as a target for novel therapeutic strategies. This multifaceted approach underscores the importance of HRBL research in advancing our knowledge of cellular mechanisms and developing innovative treatments for RNA-related disorders.
