Analytical Data
-
Gene name
JMJD8
- Application
-
Alternative Names
(Jumonji domain-containing protein 8)
-
Species
Human
-
Source
E. coli
-
Tag
N- His & C- Myc
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q96S16
-
Expression Region
24-264aa
-
Molecular Weight
34.8 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Related Products
Protein Description
JMJD8 (Jumonji domain-containing protein 8) is a member of the Jumonji C (JmjC) domain-containing family of proteins, which are known for their role as histone demethylases, regulating gene expression through epigenetic modifications. The research on JMJD8 has garnered interest due to its involvement in various biological processes, including cellular differentiation, development, and response to stress. Recent studies have suggested that JMJD8 is implicated in the regulation of key signaling pathways and may play a role in specific diseases, including cancer and metabolic disorders. The ability of JMJD8 to modify histones and other substrates positions it as a potential therapeutic target, making the understanding of its structure and function crucial. Recombinant JMJD8 protein production allows researchers to investigate its biochemical properties, binding interactions, and functional mechanisms in detail. By utilizing advanced techniques such as crystallography and mass spectrometry, scientists aim to uncover the precise role of JMJD8 in cellular processes and its potential implications in disease. This research not only adds to the fundamental knowledge of epigenetic regulators but also explores the therapeutic possibilities of targeting JMJD8 in disease management.
