Analytical Data
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Gene name
Histatin-3/HTN3
- Application
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Alternative Names
HIS2; HTN2; HTN5; Hst; PB; Histidine-rich protein 3; Basic histidine-rich protein
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P15516
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Expression Region
Asp20~Asn51
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Molecular Weight
36kDa
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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
Related Products
Protein Description
Histatin-3 (HTN3) is a significant salivary protein that plays a crucial role in oral health, particularly in antimicrobial activity and wound healing. It is part of the histatin family, which is known for its ability to inhibit the growth of various pathogens, including bacteria and fungi, particularly Candida species. The increasing prevalence of drug-resistant microbial infections highlights the necessity for novel antimicrobial agents, making HTN3 an attractive candidate for therapeutic applications. Recent studies have demonstrated its potential not only in combating oral infections but also in influencing the inflammatory response during wound healing. Furthermore, recombinant technologies have enabled the production of HTN3 in sufficient quantities for research, allowing for detailed investigations into its structure-function relationships. This has paved the way for exploring its mechanism of action at the molecular level, including its interactions with microbial membranes and its influence on host immune responses. The growing interest in HTN3 is also driven by its potential use in developing new treatments for conditions where microbial resistance is a concern. Overall, the study of Histatin-3 represents a promising avenue for advancing our understanding of antimicrobial peptides and their potential applications in clinical settings.
