Analytical Data
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Gene name
gtfB
- Application
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Alternative Names
gtfB；Glucosyltransferase-I
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Species
Human
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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
P08987
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Expression Region
426-597aa
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AA Sequence
WLHFLMNFGNIYANDPDANFDSIRVDAVDNVDADLLQIAGDYLKAAKGIHKNDKAANDHLSILEAWSDNDTPYLHDDGDNMINMDNKLRLSLLFSLAKPLNQRSGMNPLITNSLVNRTDDNAETAAVPSYSFIRAHDSEVQDLIRDIIKAEINPNVVGYSFTMEEIKKAFEI
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Molecular Weight
26.8 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
GtfB is a crucial protein primarily found in various Streptococcus species, notably Streptococcus mutans, which is a major contributor to dental caries. It plays a significant role in the synthesis of glucans from sucrose, facilitating biofilm formation on tooth surfaces. Understanding the structure and function of GtfB is vital for comprehending its role in caries development and microbial colonization in the oral cavity. Research has increasingly focused on the potential of GtfB as a target for preventive dentistry, with the aim of developing novel therapeutic strategies that can inhibit its activity, thereby preventing plaque formation and subsequent dental issues. Additionally, due to its enzymatic nature, the recombinant production of GtfB has become a valuable tool for studying its biochemical properties, interactions with other oral bacteria, and its impact on dental health. The investigation of GtfB not only provides insights into microbial ecology within the oral environment but also opens avenues for innovative approaches to combat oral diseases through targeted inhibition of glucan synthesis. The recombinant expression of GtfB also facilitates the exploration of its potential as a biomarker in dental diagnostics or its use in vaccine development against caries-causing pathogens. Overall, the study of GtfB and its recombinant protein forms continues to enhance our understanding of oral microbiology and offers promising directions for improving oral health interventions.
