Analytical Data
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Gene name
JOSD2
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简介
The JOSD2 protein serves as an enzymatic entity capable of cleaving "Lys-63"-linked polyubiquitin chains and, to a lesser extent, "Lys-48"-linked polyubiquitin chains in vitro. This suggests its potential role as a deubiquitinating enzyme involved in the removal of specific ubiquitin linkages. JOSD2 Protein, Human is the recombinant human-derived JOSD2 protein, expressed by E. coli , with tag free.
- Application
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Alternative Names
JOSD2; Josephin-2; Josephin domain-containing protein 2
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Species
Human
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8TAC2
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Expression Region
S2-D188
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Protein Length
Partial
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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
JOSD2, or Jumonji domain containing 2, is a member of the Jumonji C (JmjC) domain-containing protein family, which is known for its role as a histone demethylase, influencing chromatin remodeling and gene expression. Recent research has highlighted JOSD2's involvement in various cellular processes, including embryonic development, cell differentiation, and response to stress. Notably, JOSD2 has been implicated in several diseases, including cancer, where it may act as a potential oncogene or tumor suppressor, depending on the context. The quest to understand JOSD2's full biological function and its potential as a therapeutic target has sparked considerable interest in the scientific community. Producing recombinant JOSD2 protein is essential for studying its structure, enzymatic activity, and interaction with other proteins. By utilizing techniques such as bacterial or eukaryotic expression systems, researchers aim to obtain functional JOSD2 for biochemical assays, protein-protein interaction studies, and high-throughput screening for potential inhibitors. This research could pave the way for novel therapeutic approaches in cancer and other diseases linked to JOSD2 dysregulation, making it a focal point for ongoing investigations in molecular biology and biochemistry.
