Analytical Data
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Gene name
SecB
- Application
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Alternative Names
secB;Protein-export Protein SecB
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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
P44853
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Expression Region
1-169aa
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AA Sequence
MSEQKQDVAATEEQQPVLQIQRIYVKDVSFEAPNLPHIFQQEWKPKLGFDLSTETTQVGDDLYEVVLNISVETTLEDSGDVAFICEVKQAGVFTISGLEDVQMAHCLTSQCPNMLFPYARELVSNLVNRGTFPALNLSPVNFDALFVEYMNRQQAENAEEKSEEEQTKH
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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
SecB is a chaperone protein in Escherichia coli that plays a critical role in the bacterial protein secretion pathway. It is involved in the post-translational transport of proteins across the cytoplasmic membrane, specifically for those that are secreted via the general secretion (Sec) pathway. SecB binds to nascent polypeptides in their unfolded state, preventing premature folding and aggregation while directing them to the SecA ATPase, which then translocates them through the SecYEG translocon. The study of SecB and its restructured proteins is crucial for understanding the mechanisms of protein folding and transport in prokaryotic cells. Research has shown that modifications to the SecB protein can enhance its ability to facilitate the secretion of heterologous proteins, making it potentially useful in biotechnological applications such as recombinant protein production. Additionally, understanding the structure and function of SecB can provide insights into the evolution of secretion systems in different bacteria and the development of novel antimicrobial strategies by targeting these essential pathways. The recombinant production of SecB also provides valuable tools for studying protein interaction networks and the unfolding-refolding processes that occur during protein translocation, contributing to a broader comprehension of cellular physiology and protein homeostasis. Thus, SecB stands as a significant focus of research, bridging fundamental science and practical applications in microbiology and biotechnology.
