Recombinant E.Coli Ferric Uptake Regulation Protein (FUR) Protein (His)

Name: Recombinant E.Coli Ferric Uptake Regulation Protein (FUR) Protein (His)
Brand: Beta LifeScience
SKU: BLC-08963P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant E.Coli Ferric Uptake Regulation Protein (FUR) 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	P0A9A9
Target Symbol	FUR
Synonyms	fur; b0683; JW0669Ferric uptake regulation protein; Ferric uptake regulator
Species	Escherichia coli (strain K12)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	TDNNTALKKAGLKVTLPRLKILEVLQEPDNHHVSAEDLYKRLIDMGEEIGLATVYRVLNQFDDAGIVTRHNFEGGKSVFELTQQHHHDHLICLDCGKVIEFSDDSIEARQREIAAKHGIRLTNHSLYLYGHCAEGDCREDEHAHEGK
Expression Range	2-148aa
Protein Length	Full Length of Mature Protein
Mol. Weight	20.7kDa
Research Area	Microbiology
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	Acts as a global negative controlling element, employing Fe(2+) as a cofactor to bind the operator of the repressed genes. Regulates the expression of several outer-membrane proteins including the iron transport operon.
Subcellular Location	Cytoplasm.
Protein Families	Fur family
Database References	KEGG: ecj:JW0669 STRING: 316385.ECDH10B_0748

Gene Functions References

The influence of oxygen availability on the levels of active Fur adds a previously undescribed layer of regulation in maintaining cellular iron homeostasis in E. coli. PMID: 29087312
High iron supply inhibits the synthesis of the genotoxin colibactin by pathogenic Escherichia coli through a non-canonical Fur/RyhB-mediated pathway. PMID: 28637194
Finally, Fur derepression and RecA activation in enterohemorrhagic Escherichia coli O157 were shown to participate in the nitric oxide-enhanced Stx1 and Stx2 production, respectively. PMID: 28294553
The authors report that O2 availability affects the gene expression programs of two Escherichia coli master regulators that function in iron homeostasis: the transcription factor Fur and the small RNA regulator RyhB. PMID: 26670385
The key regulator of the response to serum-active and inactive-is the iron regulator Fur, which controls the expression of more than 80% of the serum-upregulated genes. PMID: 25118243
Fur exhibits a comprehensive regulatory role affecting many fundamental cellular processes linked to iron metabolism in order to coordinate the overall response of E. coli to iron availability. PMID: 25222563
Authors demonstrated that the EHEC lpf2 operon is regulated in response to temperature, pH, bile salts and iron, during the exponential phase of growth, and is controlled by Fur. PMID: 24966050
In a murine model of urinary tract infection (UTI), deletion of fur alone did not attenuate virulence, whereas a DeltaryhB mutant and a Deltafur DeltaryhB double mutant showed significantly reduced bladder colonization. PMID: 25245805
There is a transient change in the activity of the iron regulator Fur and of the oxidative stress regulator SoxS after Zn addition. PMID: 22016571
results presented here show that ftnA iron induction is independent of RyhB and instead involves direct interaction of Fe(2+)-Fur with an 'extended' Fur binding site (containing five tandem Fur boxes) located upstream (-83) of the ftnA promoter. PMID: 20015147
H2O2-inducible antioxidant defense system leading to an increase in catalase; hydroperoxidase HPI activity, is unaltered in Deltafur mutants PMID: 15878120
Tyr 55 of Escherichia coli Fur, as well as the two thymines in positions 18 and 19 of the consensus Fur Box, are involved with binding. PMID: 16212958
Affinity of Fur for different metals was determined & ranges over several orders of magnitude in the order: Zn(II)>> Co(II)> Fe(II)> Mn(II). Only Fe(II) binds with sufficient affinity to activate Fur significantly at physiological metal levels. PMID: 16216078
an activation mechanism for E. coli Fur involves the folding/unfolding of the N-terminal helix PMID: 16690618
Fur protein translation is coupled to that of an upstream open reading frame, translation of which is downregulated by the non-coding RNA RyhB. PMID: 17268550
Fur function may be antagonized by intracellular H2O2 by oxidizing the Fur:Fe(2+) complex and inactivating repressor function. PMID: 17462026
In this study, information theory was used to identify new Fur binding sites, 13 of which we confirmed experimentally. PMID: 17921503
In the fur+ strain compared to those in the fur- strain, expression of chromosomal dihydroorotase activity and beta-galactosidase activity of pyrC-lacZ fusion plasmid was repressed to about 30% and 17%, respectively. PMID: 18176545
The characteristic metabolism of rpoS mutants required the activity of Fur (ferric uptake regulator) in order to decrease the synthesis of the small RNA RyhB that might otherwise inhibit the synthesis of iron-rich proteins. PMID: 18556786
Binding of both zinc and iron ions induced a similar change in Fur conformations, but shifted residues closer to DNA in a different manner. PMID: 19023664
transcriptomic data identified the global transcription regulators ArcA, CRP, Fis, FNR, Fur, BaeR, CpxR, and IHF as targets and potential CO sensors PMID: 19091747

FAQs

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.