Analytical Data
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Gene name
JMJD1C
- Application
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Alternative Names
Jumonji domain-containing protein 1C Thyroid receptor-interacting protein 8
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q15652
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Expression Region
2274-2498aa
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Molecular Weight
45.5 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
JMJD1C (Jumonji domain-containing protein 1C) is a member of the Jumonji C domain-containing protein family, which is known for its role as a histone demethylase, particularly in the demethylation of lysine residues on histone proteins. This function is crucial for the regulation of gene expression and has implications in various biological processes, including development, differentiation, and cellular response to environmental stimuli. Research has shown that JMJD1C is involved in critical physiological pathways, linking it to various cancers and developmental disorders. Its expression patterns and activities are tightly regulated, making it a potential target for therapeutic interventions. Given its role in epigenetic modifications, there is increasing interest in understanding the mechanistic pathways mediated by JMJD1C, as well as the structural characteristics that govern its enzymatic function. As a result, the study of recombinant JMJD1C proteins has gained prominence to elucidate its biochemical properties, interactions with other proteins, and its potential as a biomarker or therapeutic target in diseases associated with epigenetic dysregulation. These investigations are essential not only to expand our knowledge of JMJD1C but also to explore its relevance in pathophysiological conditions, thereby contributing to the broader field of epigenetics and its implications in health and disease.
