Analytical Data
-
Gene name
hfq
- Application
-
Alternative Names
hfq；RNA-binding Protein Hfq
-
Species
E.coli
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P0A6X3
-
Expression Region
2-102aa
-
AA Sequence
AKGQSLQDPFLNALRRERVPVSIYLVNGIKLQGQIESFDQFVILLKNTVSQMVYKHAISTVVPSRPVSHHSNNAGGGTSSNYHHGSSAQNTSAQQDSEETE
-
Molecular Weight
18.5 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
The study of hfq (host factor for phage Qβ) recombinant protein has gained significant attention in recent years due to its critical role in RNA metabolism and regulation within bacterial cells. Hfq is a RNA-binding protein that facilitates the interaction between small regulatory RNAs and their target mRNAs, thus influencing gene expression and cellular responses to environmental changes. Understanding hfq's structure and function is essential for unraveling the complexities of bacterial gene regulation, which can have implications for antibiotic resistance and pathogenicity. Furthermore, hfq's involvement in various cellular processes, such as biofilm formation and stress response, makes it a potential target for novel therapeutic strategies. The production of recombinant hfq protein provides a valuable tool for biochemical characterization, structural studies, and the development of inhibitors that could disrupt hfq's function, offering new avenues for combating bacterial infections. Overall, research on recombinant hfq protein not only enhances our understanding of bacterial physiology but also paves the way for innovative approaches in medical and biotechnological applications.
