Analytical Data
-
Gene name
hfb2
- Application
-
Alternative Names
hfb2；Hydrophobin-2
-
Species
E.coli
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P79073
-
Expression Region
16-86aa
-
AA Sequence
AVCPTGLFSNPLCCATNVLDLIGVDCKTPTIAVDTGAIFQAHCASKGSKPLCCVAPVADQALLCQKAIGTF
-
Molecular Weight
12.7kDa
-
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
The HFB2 (Huntingtin-interacting protein 1, also known as Hit1) recombinant protein has garnered significant attention in biomedical research due to its involvement in key cellular processes and potential implications in neurodegenerative disorders. HFB2 was initially identified as a protein that interacts with huntingtin, the gene product responsible for Huntington's disease, suggesting its role in cellular pathways associated with this and potentially other neurodegenerative diseases. Understanding HFB2's structure, function, and interaction with other cellular components is crucial for elucidating its role in neuronal survival and degeneration. Researchers have increasingly focused on HFB2 recombinant proteins to explore their biochemical properties, interaction networks, and physiological impacts in cellular models. These studies aim to provide insight into the molecular mechanisms involving HFB2, which could eventually lead to the identification of novel therapeutic targets for diseases characterized by protein misfolding and aggregation. Furthermore, the production of HFB2 as a recombinant protein allows for high yield and purity, facilitating in vitro and in vivo studies. As a result, HFB2 stands as a promising candidate for further exploration in neurobiology, with the potential to contribute to the development of strategies to combat neurodegenerative conditions.
