Analytical Data
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Gene name
rgpB
- Application
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Alternative Names
rgpB；HIS2；Histatin-3
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P95493
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Expression Region
230-473aa
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AA Sequence
YTPVEEKENGRMIVIVPKKYEEDIEDFVDWKNQRGLRTEVKVAEDIASPVTANAIQQFVKQEYEKEGNDLTYVLLVGDHKDIPAKITPGIKSDQVYGQIVGNDHYNEVFIGRFSCESKEDLKTQIDRTIHYERNITTEDKWLGQALCIASAEGGPSADNGESDIQHENIIANLLTQYGYTKIIKCYDPGVTPKNIIDAFNGGISLANYTGHGSETAWGTSHFGTTHVKQLTNSNQLPFIFDVAC
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Molecular Weight
33.3 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
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Protein Description
RgpB, a crucial protein in the study of bacterial pathogenesis and virulence, is predominantly associated with the invasive capabilities of certain pathogens, particularly those within the genus *Pseudomonas* and *Neisseria*. As a member of the extracellular proteins, RgpB plays a significant role in biofilm formation, immune evasion, and tissue colonization, which are key factors in the development and progression of infectious diseases. Understanding the structural and functional characteristics of RgpB is essential for uncovering its mechanisms of action and its interactions with host immune responses. The recombinant expression of RgpB has enabled researchers to produce this protein in a controlled laboratory setting, facilitating in-depth studies on its biochemical properties and potential as a target for therapeutic intervention. Investigations into the immunogenicity of RgpB have also gained traction, as it may offer insights into vaccine development strategies to combat infections. The ongoing research efforts aimed at elucidating the roles of RgpB not only advance our comprehension of microbial pathogenesis but also pave the way for novel biomedical applications, including vaccine design and the development of inhibitors that may disrupt its function in the context of bacterial infections. Thus, the exploration of RgpB as a recombinant protein represents a significant stride in microbiological and immunological research, highlighting its importance in contemporary healthcare challenges.
