Recombinant E.Coli Rna Polymerase Sigma Factor Rpos (RPOS) Protein (His)

Name: Recombinant E.Coli Rna Polymerase Sigma Factor Rpos (RPOS) Protein (His)
Brand: Beta LifeScience
SKU: BLC-01724P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant E.Coli Rna Polymerase Sigma Factor Rpos (RPOS) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P13445
Target Symbol	RPOS
Synonyms	Sigma S Sigma-38
Species	Escherichia coli (strain K12)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MSQNTLKVHDLNEDAEFDENGVEVFDEKALVEQEPSDNDLAEEELLSQGATQRVLDATQLYLGEIGYSPLLTAEEEVYFARRALRGDVASRRRMIESNLRLVVKIARRYGNRGLALLDLIEEGNLGLIRAVEKFDPERGFRFSTYATWWIRQTIERAIMNQTRTIRLPIHIVKELNVYLRTARELSHKLDHEPSAEEIAEQLDKPVDDVSRMLRLNERITSVDTPLGGDSEKALLDILADEKENGPEDTTQDDDMKQSIVKWLFELNAKQREVLARRFGLLGYEAATLEDVGREIGLTRERVRQIQVEGLRRLREILQTQGLNIEALFRE
Expression Range	1-330aa
Protein Length	Full Length
Mol. Weight	42.1 kDa
Research Area	Transcription
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the master transcriptional regulator of the stationary phase and the general stress response. Controls, positively or negatively, the expression of several hundred genes, which are mainly involved in metabolism, transport, regulation and stress management.; Protects stationary phase cells from killing induced by endoribonuclease MazF.
Subcellular Location	Cytoplasm.
Protein Families	Sigma-70 factor family, RpoS subfamily
Database References	KEGG: ecj:JW5437 STRING: 316385.ECDH10B_2909

Gene Functions References

RpoS contributes to the resistance of E. coli to protozoan predation and that RpoS is crucial for the increased fitness of soil-persistent E. coli against predation and reduced moisture in soil. PMID: 28967947
bolA plays a major role in the presence and absence of rpoS in attachment to the stainless steel and silicone surfaces. PMID: 27842452
RNA polymerase is pausing during initial transcription. PMID: 27618490
Our study indicates that the RNA chaperone Hfq contributes to the persistent infection of E. coli by maintaining the expression of bacterial genes, including one coding for sigma(38), that help bacteria evade host immunity. PMID: 27357148
A promoter's responsiveness to indirect regulation by sigma factor competition is determined by the sequence-dependent kinetics of the rate limiting steps of transcription initiation. PMID: 27452766
results suggested that the determinant for sigma38-dependent promoter lies in the promoter upstream sequence PMID: 25845539
the bacterial cell responds to lowered levels of acetyl-CoA by inducing RpoS, allowing reprogramming of E. coli metabolism. PMID: 25847996
It was thus verified that the reinforcement of csgA gene in the DeltarpoS cells induced the enhanced colonization on the solid surfaces with the increased flagellum and curli expressions. PMID: 25252647
Environmental stresses resulting in reduction in growth rate stimulate the expression of the rpoS gene. [review] PMID: 24596257
All the relocated AAN binding sites restored tight Hfq binding in vitro, but only insertion at the natural position restored Hfq-dependent sRNA annealing in vitro and sRNA regulation of rpoS translation in vivo. PMID: 24051417
Dependence on MiaA may therefore provide yet another way for RpoS levels to respond to growth conditions. PMID: 24296670
Exposure to H2O2 during extreme-acid treatment increased the death rate slightly for W3110 and to a greater extent for the rpoS deletion strain. PMID: 23520457
We finally demonstrate that the RpoS general stress regulator prevents oxidative stress-mediated DNA damage formation in E. coli. PMID: 23613664
These results suggest that rpoS does have an influence on both biofilm formation and survival of Escherichia coli O157:H7 and that the advantage conferred by rpoS is contingent on the environmental conditions. PMID: 23001657
Peroxide resistance was greater (P<0.05) in biofilm cells than in planktonic cells, and full resistance required rpoS but not oxyR. PMID: 22700652
findings demonstrate that naturally occurring rare codons in rpoS contribute to protecting the rpoS transcript against RNase E-mediated degradation PMID: 21788735
The inactivation of rpoS systematically reduced transformation frequency, while over-expressing rpoS increased plasmid transformation. PMID: 22438941
These data suggest that cellular ATP levels directly control RpoS stability. PMID: 22426532
We propose that RpoS-regulated functions are responsible for the increase in membrane resilience as cells enter stationary phase and that this plays a major role in the development of pressure resistance. PMID: 21705547
OxyS represses rpoS mRNA translation by sequestering Hfq rather than binding to rpoS mRNA PMID: 21889623
Expression of the flagellar sigma(F) factor (FliA), another sigma(70) family protein, is controlled positively by RpoN but negatively by RpoS. PMID: 21219458
K(+) is responsible for influencing the binding of sigma(70) and sigma(S) to core RNA polymerase. PMID: 21143318
Increased mutation frequency is observed in redox-impaired Escherichia coli due to RelA- and RpoS-mediated repression of DNA repair. PMID: 20581184
Found that the level of the small regulatory RNA RprA, which is involved in the promotion of rpoS translation, is higher in pgsA3 cells than in pgsA(+) cells. PMID: 20455949
The results identify a second DNA polymerase contributing to stress-induced mutagenesis and show that RpoS promotes mutagenesis by more than the simple upregulation of dinB. PMID: 20639336
sigma(70) and sigma(38) dependent promoters in all glycolytic genes and operons could allow a differential transcription of these central metabolism genes by both sigma subunits as an adaptation response to carbon limitation PMID: 19838295
Polyamines, in particular putrescine, are involved in regulation of the rpoS expression by concentration-dependent stimulation at the levels of translation and stability of the protein sigmaS PMID: 15377267
RpoS proteolysis is regulated upon carbon starvation by a mechanism that does not require the SprE (RssB) response regulator phosphorylation site. PMID: 15489452
low shear simulated microgravity rendered rpoS less stable in exponential phase and increased rpoS mRNA translational efficiency PMID: 15576768
identification of genes that require RpoS for expression PMID: 15576800
required for activation of gab operon in stress induced pathway mediated by loss of LPS inner core PMID: 15576807
Esigma(s) favours the presence of a distal UP-element half-site, and at the same time is unable to take advantage of a proximal half-site or a full UP-element. Esigma70, however, exhibits the opposite preference. PMID: 15612932
we demonstrate that RpoS levels following ammonia starvation are only slightly increased compared to growing cells and are 10-fold below the levels observed under glucose or phosphate limitation. PMID: 15629914
Genome-wide expression profiling data presented here indicate that up to 10% of the E. coli genes are under direct or indirect control of sigmaS. PMID: 15716429
An increased level of alternative sigma factor RpoS partially suppresses drug hypersensitivity associated with inactivation of the multidrug resistance pump AcrAB in Escherichia coli. PMID: 15808939
mediates differential growth-dependent expressions of the tktA and tktB genes PMID: 15968503
findings show that 24 nucleotides of the rpoS ribosome-binding site (RBS) are necessary and sufficient for a large part of the increase in rpoS translation as cells grow to stationary phase PMID: 16237004
Inactivation of IHF in vivo abolishes the sigma (S)-dependent transcription initiation of the pst operon. PMID: 16404567
The data suggest that an ensemble of -35 region elements exists at sigma38 promoters and these can help mediate responsiveness to physiological challenges through interactions involving region 4 of the sigma38 protein. PMID: 16420371
analysis of rpoS mutations in Escherichia coli populations PMID: 16489226
Analysis of the stability of sigmaS and the levels of RssB indicate that the absence of PAPI enhances RssB-mediated sigmaS proteolysis specifically in starved cells. PMID: 16556229
Regulated interplay between the mobile modules of the beta' and the sigma subunits of the RNA Polymerase appears to be necessary for stable Open promoter Complex formation. PMID: 16725156
Pfs transcription is shown to rely on both sigma 70 and sigma 38 (rpoS), and the latter is subject to induction that increases pfs expression. PMID: 16950920
The regulatory protein Crl increases the activity of RpoS by direct interaction with the RpoS holoenzyme. PMID: 17224607
study elucidates rules governing RpoS selectivity in presence of a class II activator, provide insight into transcriptional activation by Fis from this position & clarify, why the proP promoter is activated during a short time when Fis & RpoS are present PMID: 17302803
the accumulation and activation of sigma(S) upon carbon starvation, which are linked to alterations in both ribosomal fidelity and efficiency. PMID: 17403784
Results suggest that the regulatory RNA SsrA may indirectly improve RpoS translation by limiting ribosome stalling and depletion of some component of the translation machinery. PMID: 17449615
cell use of ppGpp to mediate a variety of starvation responses operates in part by modulating sigma(S) levels PMID: 17640895
This study presented evidence that the CsgD protein, a transcription regulator involved in biofilm formation in Escherichia coli, modulates the expression of the rpoS (sigma(S)) regulon. PMID: 17873038
Real-time PCR (RT-PCR) analysis confirmed the important role of RpoS in the PTS- strains and allowed the identification of 19 genes including almost all the glycolytic genes, not previously reported, to be at least partially dependent on RpoS. PMID: 17938565

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Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

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