SecB

Protein Export Protein SecB Recombinant
Cat. No.
BT14949
Source
Escherichia Coli.
Synonyms
Protein-export protein secB, secB, b3609, JW3584.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Recombinant E.Coli SecB produced in E.Coli is a single, non-glycosylated polypeptide chain containing 155 amino acids and having a molecular mass of 17.2 kDa. SecB was over-expressed in E. coli and purified by conventional chromatography.

Product Specs

Introduction
SecB is a key chaperone protein involved in protein export. It exhibits rapid binding to a variety of ligands with high affinity but low specificity. In the general secretory pathway, SecB plays a crucial role by regulating the balance between precursor proteins folding, aggregating, or being delivered to the membrane-bound translocation machinery for export. Beyond its role in protein export, SecB may act as a general chaperone, preventing aggregation and maintaining a pool of unfolded proteins in the cytoplasm.
Description
Recombinant E. coli SecB, expressed in E. coli, is a non-glycosylated polypeptide chain consisting of 155 amino acids. With a molecular weight of 17.2 kDa, it is purified through conventional chromatography.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
The SecB protein solution is provided at a concentration of 1 mg/ml in a buffer containing 20 mM Tris-HCl at pH 8.0 and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is advisable for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
The purity is determined to be greater than 95% using SDS-PAGE analysis.
Synonyms
Protein-export protein secB, secB, b3609, JW3584.
Source
Escherichia Coli.
Amino Acid Sequence

MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ LADDVYEVVL RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA.

Product Science Overview

Introduction

Protein export is a crucial process in bacterial cells, enabling the translocation of proteins from the cytoplasm to various cellular compartments or the extracellular environment. One of the key players in this process is the Sec pathway, which includes several essential proteins. Among these, the SecB protein plays a significant role in ensuring the proper export of proteins. This article delves into the background of the Protein Export Protein SecB Recombinant, its function, and its importance in bacterial protein export.

The Sec Pathway

The Sec pathway is a highly conserved mechanism in bacteria responsible for the translocation of proteins across the cytoplasmic membrane. The pathway involves several components, including the SecYEG translocon, SecA ATPase, and chaperone proteins like SecB. The SecYEG translocon forms a channel through which proteins are transported, while SecA provides the energy required for translocation through ATP hydrolysis .

Role of SecB

SecB is a cytosolic chaperone protein that plays a pivotal role in the Sec pathway. It is responsible for maintaining precursor proteins in an unfolded, translocation-competent state and delivering them to the SecA-SecYEG complex. SecB binds to nascent polypeptides and prevents their premature folding or aggregation, ensuring they remain suitable for translocation .

Mechanism of Action

SecB recognizes and binds to specific signal sequences on precursor proteins, forming a complex that is targeted to the SecA ATPase. Upon interaction with SecA, the precursor protein is transferred to the SecYEG translocon. SecA then drives the translocation of the precursor protein through the SecYEG channel using energy derived from ATP hydrolysis. Once translocation is complete, the precursor protein is released and can fold into its native conformation .

Recombinant SecB Protein

Recombinant SecB protein is produced through genetic engineering techniques, where the secB gene is cloned and expressed in a suitable host organism, such as Escherichia coli. This allows for the large-scale production and purification of SecB protein for research and industrial applications. Recombinant SecB is used to study the protein export process, investigate the interactions between Sec pathway components, and develop potential therapeutic interventions targeting bacterial protein export .

Importance in Research and Medicine

Understanding the function and mechanism of SecB is crucial for several reasons:

  1. Antibiotic Development: The Sec pathway, including SecB, is a potential target for novel antibiotics. Inhibiting this pathway can disrupt protein export, leading to bacterial cell death .
  2. Protein Engineering: Recombinant SecB can be used to enhance the production of recombinant proteins by preventing their aggregation and facilitating their proper folding and export .
  3. Basic Research: Studying SecB provides insights into the fundamental processes of protein translocation and the intricate interactions between chaperones and translocons .

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