Analytical Data
-
Gene name
vjbR
- Application
-
Alternative Names
vjbR；HTH-type quorum sensing-dependent transcriptional regulator VjbR
-
Species
E.coli
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q2YJ50
-
Expression Region
1-259aa
-
AA Sequence
MSLDLVHFPNYKKTFFGSSFQSDTLALLTRIRDEIGCRYVTHTYRGRVGDCTKVNSADLTVLMTLPATWVARYSSKNYFAIDPVFQEDAPYYRNDTSAIARDLKEDADICPAVAELLHDAEKHGLGNLFIAVSARNPKGVAGCTVFTFEVEDEDRTQFLARMRPRLLSLAGIIHGTVCGCKDANSVASLLTPREVDCLRWAANGKTDGEIAEILSIARWTVVTYLQNAKIKLNCSNRTSAVATALSLGIIDMPEVQHLV
-
Molecular Weight
30.6 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
VjbR is a key regulatory protein identified in various bacterial species, particularly within the context of virulence and pathogenicity. It is part of a broader family of transcriptional regulators that influence gene expression in response to environmental stimuli. Research into VjbR has gained momentum due to its crucial role in the life cycle of important pathogens, including those that affect both plants and animals. Understanding the structural and functional characteristics of VjbR can provide insights into its mechanism of action, particularly how it interacts with DNA and other cellular components to modulate gene expression related to virulence factors. Such studies are vital as they can elucidate the pathways employed by pathogens to adapt to host environments and evade immune responses. Moreover, advances in recombinant protein technologies allow for the production of VjbR in a laboratory setting, facilitating detailed studies of its biochemical properties and functional roles. This research has significant implications for the development of novel therapeutic strategies and vaccines, potentially targeting the regulatory mechanisms that VjbR influences in pathogenic organisms. Overall, VjbR represents an important target for understanding microbial pathogenicity and developing interventions to combat infectious diseases.
