Analytical Data
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Gene name
JBP1
- Application
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Alternative Names
J-binding protein 1;Thymidine hydroxylase JBP1
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Species
Leishmania infantum
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Source
E. coli
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Tag
N- His-V5
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A4HU70
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Expression Region
200-600aa
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Molecular Weight
53.4 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
JBP1, or JunB-binding protein 1, is a relatively novel protein that has garnered attention in the field of molecular biology and biomedicine due to its potential roles in cellular processes and disease mechanisms. Research indicates that JBP1 may be involved in various signaling pathways that regulate cell proliferation, apoptosis, and differentiation, particularly in the context of cancer and immune responses. Its interaction with JunB, a transcription factor that plays a critical role in gene expression, suggests that JBP1 may influence transcriptional regulation, thereby impacting oncogenic processes. Furthermore, studies have linked JBP1 to inflammatory responses, highlighting its potential as a therapeutic target in inflammatory diseases. The recombinant production of JBP1 presents a significant opportunity to delve deeper into its functional roles and interactions, enabling researchers to elucidate its mechanistic pathways and evaluate its potential as a biomarker for disease. Through advanced techniques in protein expression and purification, the study of JBP1 can facilitate the development of novel therapeutic strategies and contribute to a better understanding of its implications in various pathologies. As research progresses, the elucidation of the precise biological functions of JBP1 will pave the way for its application in clinical contexts, emphasizing the necessity for continued exploration of this intriguing protein.
