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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.

查看别名

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

关键信息

纯度

>95% SDS-PAGE

表达系统

Escherichia coli

标签

Tag free

应用

SDS-PAGE, FuncS

applications

生物活性

No

访问

P0AGE0

不含动物源

No

不含载体蛋白

No

种属

Escherichia coli K-12

存储溶液

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

反应性数据

{ "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>" } } }

序列信息

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

性能和储存信息

运输条件
Blue Ice
推荐的短期储存条件
-20°C
推荐的长期储存条件
-20°C
False

补充信息

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.

特殊说明

形式

Liquid

常规信息

功能

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).

翻译后修饰

Phosphorylated on tyrosine residue(s).

产品实验方案

靶点信息

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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