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AB123224

Recombinant E. coli SSB protein

Recombinant E. coli SSB protein

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(4 Publications)

Recombinant E. coli SSB protein is a Escherichia coli K-12 Full Length protein, in the 2 to 178 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, FuncS.

別名を表示する

exrB, lexC, b4059, JW4020, ssb, Single-stranded DNA-binding protein, SSB, Helix-destabilizing protein

1 Images
SDS-PAGE - Recombinant E. coli SSB protein (AB123224)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant E. coli SSB protein (AB123224)

SDS-PAGE of ab123224

Key facts

精製度

>95% SDS-PAGE

発現系

Escherichia coli

タグ

Tag free

アプリケーション

SDS-PAGE, FuncS

applications

生物活性

No

アクセッション番号

P0AGE0

アニマルフリー

No

キャリアフリー

No

Escherichia coli K-12

バッファー組成

pH: 6.5 - 8.5 Constituents: 50% Glycerol (glycerin, glycerine), 1.17% Sodium chloride, 0.32% Tris HCl, 0.03% EDTA, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

配列情報

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":"18.9 kDa","actualMolecularWeight":null,"aminoAcidEnd":178,"aminoAcidStart":2,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P0AGE0","tags":[]}]

出荷温度及び保存条件

出荷温度
Blue Ice
短期保存温度
-20°C
長期保存温度
-20°C
False

補足情報

This supplementary information is collated from multiple sources and compiled automatically.

The single-stranded DNA-binding protein (SSB) also known as La protein in humans has a mechanical role in stabilizing single-stranded DNA (ssDNA) during replication recombination and repair processes. In E. coli the SSB protein weighs approximately 19 kDa and is essential for maintaining genome integrity. SSB expression occurs in various organisms with bacterial SSBs being key to prokaryotic cells while homologs like La/SSB in humans are more involved in post-transcriptional processes. Anti-SSB antibodies target this protein often in research and diagnostic applications.
Biological function summary

The single-stranded DNA-binding protein plays an important role in the orchestration of DNA metabolism. It binds to ssDNA substrates acting as a scaffold for recruiting other proteins and it frequently involves itself in complex formation with other cellular factors such as replication proteins. This function proves important in stabilizing unwound DNA and regulating access for proteins involved in DNA synthesis and repair. Anti-La SSB antibodies are typically used to study aberrant RNA processing events.

Pathways

The SSB protein influences the DNA replication and repair pathways. SSB's interaction with proteins like DNA polymerase and exonuclease suggests its cooperation with these enzymes to ensure precise DNA synthesis and to facilitate proper repair of DNA. Anti-SSB Ab can be used to investigate specific pathway dysregulations providing insights into pathway alterations that impact genome stability. Notably SSB's role in coordinating with other repair proteins emphasizes its centrality in maintaining steady state of DNA integrity.

The single-stranded DNA-binding protein has vital connections to autoimmune diseases. Sjögren's syndrome and systemic lupus erythematosus often see the presence of anti-SSB antibodies indicating an autoimmune response against this protein. These disorders associate with the human La protein an autoimmune target in these disease states. Understanding SSB's interaction with other proteins such as Ro60 in these conditions gives insights into disease pathology and potential areas for therapeutic intervention.

製品の性状

製品の状態

Liquid

一般的な情報

機能

Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism. Acts as a sliding platform that migrates on DNA via reptation. SSB or its 10 C-terminal amino acids stimulates the ATPase activity of RadD (PubMed : 27519413).

翻訳後修飾

Phosphorylated on tyrosine residue(s).

製品プロトコール

ターゲットの情報

Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism. Acts as a sliding platform that migrates on DNA via reptation. SSB or its 10 C-terminal amino acids stimulates the ATPase activity of RadD (PubMed : 27519413).
See full target information ssb

文献 (4)

Recent publications for all applications. Explore the full list and refine your search

Nucleic acids research 47:3127-3141 PubMed30605522

2019

YB-1, an abundant core mRNA-binding protein, has the capacity to form an RNA nucleoprotein filament: a structural analysis.

Applications

Unspecified application

Species

Unspecified reactive species

Dmitry A Kretov,Marie-Jeanne Clément,Guillaume Lambert,Dominique Durand,Dmitry N Lyabin,Guillaume Bollot,Cyril Bauvais,Anastasiia Samsonova,Karina Budkina,Rachid C Maroun,Loic Hamon,Ahmed Bouhss,Ewen Lescop,Flavio Toma,Patrick A Curmi,Alexandre Maucuer,Lev P Ovchinnikov,David Pastré

Molecular cell 65:832-847.e4 PubMed28257700

2017

Functions of Replication Protein A as a Sensor of R Loops and a Regulator of RNaseH1.

Applications

FuncS

Species

Unspecified reactive species

Hai Dang Nguyen,Tribhuwan Yadav,Sumanprava Giri,Borja Saez,Timothy A Graubert,Lee Zou

Biochemistry 20:5346-52 PubMed7028102

1981

Escherichia coli single-strand deoxyribonucleic acid binding protein: stability, specificity, and kinetics of complexes with oligonucleotides and deoxyribonucleic acid.

Applications

Unspecified application

Species

Unspecified reactive species

G Krauss,H Sindermann,U Schomburg,G Maass

The Journal of biological chemistry 250:1972-80 PubMed1090613

1975

The deoxyribonucleic acid unwinding protein of Escherichia coli. Properties and functions in replication.

Applications

Unspecified application

Species

Unspecified reactive species

J H Weiner,L L Bertsch,A Kornberg
View all publications

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