Analytical Data
-
Gene name
hmfA
- Application
-
Alternative Names
hmfA;DNA-binding Protein HMf-1
-
Species
E.coli
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P48781
-
Expression Region
1-69aa
-
AA Sequence
MGELPIAPIGRIIKNAGAERVSDDARIALAKVLEEMGEEIASEAVKLAKHAGRKTIKAEDIELARKMFK
-
Molecular Weight
14.9 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
HmfA (Hemolysin-encoding factor A) is a significant protein found in certain bacterial species, particularly those associated with pathogenicity. The study of HmfA is crucial due to its role in the virulence mechanisms of bacteria, where it contributes to the formation of pores in host cell membranes, facilitating pathogen invasion and evasion of the immune response. Research on HmfA recombinant proteins has gained attention as they can serve as valuable tools for understanding the molecular interactions between pathogens and host cells. Additionally, the potential application of HmfA in vaccine development and therapeutic avenues makes it an area of intense investigation. Scientists are employing advanced techniques such as genetic engineering and structural biology to elucidate the functional properties of HmfA and its interactions with host immune components. Furthermore, understanding the evolution and expression regulation of HmfA can provide insights into bacterial adaptability and resistance mechanisms. As antibiotic resistance becomes a growing concern, characterizing the functionality and properties of HmfA may inform the design of novel antimicrobial strategies. This research not only aims to deepen the comprehension of bacterial pathogenesis but also holds promise for public health by contributing to the development of innovative treatment methods and preventive measures against bacterial infections linked to HmfA-expressing organisms.











