Analytical Data
-
Gene name
Optineurin
- Application
-
Alternative Names
E3-14.7K-interacting protein (FIP-2) (Huntingtin yeast partner L) (Huntingtin-interacting protein 7) (HIP-7) (Huntingtin-interacting protein L) (NEMO-related protein) (Optic neuropathy-inducing protein) (Transcription factor IIIA-interacting protein) (TFIIIA-IntP)
-
Species
Human
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q96CV9
-
Expression Region
1-577aa
-
Molecular Weight
69.9 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
Optineurin is a protein that plays a crucial role in various cellular processes, including maintaining cellular homeostasis, regulating inflammatory responses, and mediating autophagy. It has been implicated in the pathogenesis of several neurodegenerative diseases, notably Amyotrophic Lateral Sclerosis (ALS) and glaucoma, where mutations in the optineurin gene have been identified. As research continues to uncover the diverse functions of optineurin, the production of recombinant optineurin protein has become essential for investigating its mechanisms of action and establishing its potential as a therapeutic target. Recombinant protein technology allows for the generation of large quantities of optineurin that can be used in functional assays, structural studies, and drug screening. Moreover, understanding the structural and functional properties of optineurin can provide insights into its role in disease progression and facilitate the development of new interventions for conditions associated with its dysregulation. Additionally, the study of optineurin is relevant not only for its direct involvement in neurodegeneration but also for its broader implications in cellular signaling pathways and immune responses. Researchers are increasingly focused on elucidating the pathways affected by optineurin, often using recombinant protein to explore its interactions with other cellular components and to identify small-molecule inhibitors or activators that may offer clinical benefits. Overall, the investigation of recombinant optineurin protein is a promising frontier in biomedical research, with the potential to reveal significant insights into molecular mechanisms underlying a range of diseases.
