Analytical Data
-
Gene name
pulB
-
简介
PulB is a protein belonging to the glycosyl hydrolase 13 family. The glycosyl hydrolase 13 family contains enzymes involved in the breakdown of complex carbohydrates by catalyzing the hydrolysis of glycosidic bonds. pulB Protein, Pullulanibacillus naganoensis is the recombinant pulB protein, expressed by E. coli , with tag free.
- Application
-
Alternative Names
pulB; Alpha-dextrin endo-1; 6-alpha-glucosidase; Pullulan 6-glucanohydrolase
-
Species
Others
-
Source
E. coli
-
Tag
Tag Free
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
G9JLV4
-
Expression Region
D1-K926
-
Protein Length
Full Length
-
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
PulB is a key protein involved in the Type II secretion system (T2SS) utilized by various Gram-negative bacteria to transport proteins across the outer membrane. This system plays a crucial role in the pathogenicity of several species, including Pseudomonas aeruginosa, by enabling the secretion of virulence factors and extracellular enzymes that enhance survival and infection. The PulB protein specifically functions as a component of the Pul system, which is essential for the secretion of specific proteins involved in biofilm formation and nutrient acquisition. Research on PulB has garnered significant attention due to its implications in microbial physiology and its potential as a target for antibacterial strategies. Understanding the structure and function of PulB can provide insights into the mechanistic details of the T2SS, revealing how bacteria adapt to environmental challenges and contribute to their pathogenic traits. Characterizing PulB recombinant proteins allows scientists to explore its interaction with other secretion components and to assess its role in the protein export process. This research is not only vital for understanding bacterial biology but also holds promise for developing novel therapeutic approaches aimed at disrupting the secretion mechanisms that contribute to bacterial virulence. As antibiotic resistance becomes a growing concern, targeting the secretion systems may represent a promising avenue for innovative antimicrobial therapies. Thus, the study of PulB and its associated pathways is essential for advancing our understanding of bacterial pathogenesis and designing effective interventions against infectious diseases.
