Recombinant E.Coli Rna-Binding Protein Hfq (HFQ) Protein (His&Myc)

Name: Recombinant E.Coli Rna-Binding Protein Hfq (HFQ) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-06982P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant E.Coli Rna-Binding Protein Hfq (HFQ) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P0A6X3
Target Symbol	HFQ
Species	Escherichia coli (strain K12)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	AKGQSLQDPFLNALRRERVPVSIYLVNGIKLQGQIESFDQFVILLKNTVSQMVYKHAISTVVPSRPVSHHSNNAGGGTSSNYHHGSSAQNTSAQQDSEETE
Expression Range	2-102aa
Protein Length	Full Length of Mature Protein
Mol. Weight	18.5 kDa
Research Area	Others
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	RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Involved in the regulation of stress responses mediated by the sigma factors RpoS, sigma-E and sigma-32. Binds with high specificity to tRNAs. Binds sRNA antitoxin RalA. In vitro, stimulates synthesis of long tails by poly(A) polymerase I. Required for RNA phage Qbeta replication. Seems to play a role in persister cell formation; upon overexpression decreases persister cell formation while deletion increases persister formation.
Protein Families	Hfq family
Database References	KEGG: ecj:JW4130 STRING: 316385.ECDH10B_4367

Gene Functions References

By interacting with the mutS leader, Hfq serves as a critical switch that modulates bacteria from high-fidelity DNA replication to stress-induced mutagenesis PMID: 28794186
Here, de novo Rosetta modeling and competitive binding experiments show that the acidic tip of the Escherichia coli Hfq CTD transiently binds the basic Sm core residues necessary for RNA annealing. PMID: 28826489
Compaction and condensation of DNA mediated by the C-terminal domain of Hfq has been reported. PMID: 28521053
Global mapping of small RNA-Hfq target interactions have been described in the bacterial genome. PMID: 27588604
We describe a refined system - consisting solely of purified Hfq, polynucleotide phosporylase (PNP) and ADP - that allows reconstitution in vitro of characteristic 'SDS-insensitive' Hfq6-Hfq6 assemblies observed in experiments with whole-cell extracts obtained from exponentially-growing cells. We also optimized conditions for the extraction of intact native dodecameric Hfq complexes. PMID: 28366634
The 3' terminal oligo(U) stretch and the base-pairing region enable small RNA to interact with Hfq. PMID: 26531825
Hfq has at least two distinct ways in which it interacts with sRNAs; these different binding properties have strong effects on the stability of the sRNA in vivo and the sequence requirements of regulated mRNAs. PMID: 26373314
The authors show that an interaction between the distal surface of Hfq and the ribosome-binding site of IS10 transposase mRNA (RNA-IN) is required for repressing translation initiation of the transposase. PMID: 25649688
This study demonstrated that random-order binding of Hfq to sRNA and mRNA in each pair can cause high Hfq concentrations to suppress rather than promote sRNA activity in Escherichia coli. PMID: 26261213
Study shows that Hfq does not affect the transcriptional readthrough event itself; also find that the readthrough products no longer bind to Hfq in vivo. PMID: 26106215
these results suggest that Hfq could function as an anchor/coupling factor responsible for de-solubilization of RNA and its tethering to the degradosome complex. PMID: 25896386
The study verified that the A-rich linker region of OxyS sRNA binds Hfq at its distal side. PMID: 25670676
Data show that the mRNA wraps entirely around the host Ffactor 1 protein Hfq protein, specifically contacting both surfaces. PMID: 25404287
The data indicated that the simultaneous binding to the opposite faces of Hfq was enabled by separate adenosine-rich and uridine-rich sequences in the long, single-stranded region of ChiX. PMID: 25582129
Identification of RNA binding sites of Hfq. PMID: 24288369
Hfq acts as the repressor of cirA mRNA translation in the absence of sRNA. PMID: 24065131
Based on the results presented here, we suggest that Hfq could be involved in regulating RNA pairing in other antisense systems, including systems encoded by other transposable elements. PMID: 23510801
Thus, Hfq is intrinsically essential to pathogenic Escherichia coli for survival and virulence exerted in the Caenorhabditis elegans host. PMID: 22713744
The authors show that Hfq is most active in RNA annealing when the hexamer is present. PMID: 22326348
sRNAs compete with each other for Hfq binding. PMID: 22040174
expression of hfq was repressed by the CRP-cAMP complex. PMID: 21840983
the purification, crystallization and structural data of the full 102-amino-acid protein are presented. These data revealed that the presence of the C-terminus changes the crystal packing of E. coli Hfq PMID: 21543856
Results revealed that the C-terminus of Hfq is intrinsically disordered and flexible, which appears to contribute to the interactions of Hfq with RNA substrates. PMID: 21330354
role of Hfq in LF82 virulence was independent of its function in regulating RpoS and RpoE activity PMID: 21298102
Hfq negatively regulate Tn10/IS10 transposition by promoting anti-sense inhibition of RNA-IN10 translation. PMID: 20815820
Hfq mediates the binding of sRNAs to their target mRNAs; without Hfq, most sRNAs cannot efficiently regulate target mRNA expression. PMID: 21189298
examined the ability of Hfq derivatives, consisting of the conserved core and short C-terminal extensions, to support the regulation of rpoS expression and riboregulation by various well-characterized small regulatory RNAs PMID: 20888338
LEE regulator (GrlA) is critically involved in the regulating the presence of L0045. PMID: 20587027
show that both Hfq and this Hfq binding site are required for RprA or ArcZ to act in vivo and to form a stable complex with rpoS mRNA in vitro PMID: 20457943
The alteration of rpsO, rpsT and rpsB-tsf transcript levels observed under conditions of Hfq deficiency is not caused by the post-transcriptional events. PMID: 20167073
Hfq has two independent RNA-binding surfaces; Hfq can simultaneously bind a ncRNA and its mRNA target to facilitate the strand displacement reaction required for Hfq-dependent translational regulation PMID: 15531892
Hfq synthesis is autoregulated at the translational level. PMID: 15872186
E.coli Hfq polymerizes into well-ordered fibres whose morphologies closely resemble those found for Sm-like archaeal proteins PMID: 16337963
findings indicate that Hfq regulates traM and traJ transcript stability by a mechanism separate from FinOP-mediated repression PMID: 16352828
Study shows that SgrS RNA forms a stable duplex with the phosphoenolpyruvate-glucose phosphotransferase mRNA, and that Hfq markedly facilitates the rate of duplex formation. PMID: 16859494
Hfq may play a general role in stress response regulation in E. coli. PMID: 17158661
Hfq modulates the interaction between a small non-coding RNA, DsrA, and its regulatory target mRNA, rpoS. PMID: 17259214
structure and function of Hfq [review] PMID: 17395525
The increase of the CCA-addition in the presence of Hfq suggests that this protein acts as a stimulating factor not only for PAP, but also for the CCA-adding enzyme. PMID: 17949481
The C-terminal extension of E. coli Hfq constitutes a hitherto unrecognized RNA interaction surface with specificity for mRNAs. PMID: 18000007
tRNA binding and reduced fidelity are linked by a role for Hfq in tRNA modification. PMID: 18230766
Hfq negatively affects LEE expression in exponential phase by regulating the expression of the LEE-encoded regulators GrlA and GrlR at the post-transcriptional level by destabilizing grlRA mRNA. PMID: 19570135
HFq protein is involved in the regulation of bacterial cytoskeleton and cell division proteins. PMID: 19571680
Study showed a novel property of Escherichia coli Hfq protein: it possibly influenced extracellular indole levels. PMID: 19657572
the crystal structure of Escherichia coli Hfq bound to the poly(A) RNA, A(15) is reported. PMID: 19889981
Hfq binds with high specificity and nanomolar affinity to both D-stem and T-stem of tRNAs using its proximal surface. PMID: 18230766

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

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.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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