Recombinant E.Coli Transcription Termination Factor Rho (RHO) Protein (His)

Name: Recombinant E.Coli Transcription Termination Factor Rho (RHO) Protein (His)
Brand: Beta LifeScience
SKU: BLC-02319P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Escherichia coli (strain K12) rho.

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Product Overview

Description	Recombinant E.Coli Transcription Termination Factor Rho (RHO) 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	P0AG30
Target Symbol	RHO
Synonyms	rho; nitA; psuA; rnsC; sbaA; tsu; b3783; JW3756; Transcription termination factor Rho; EC 3.6.4.-; ATP-dependent helicase Rho
Species	Escherichia coli (strain K12)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MNLTELKNTPVSELITLGENMGLENLARMRKQDIIFAILKQHAKSGEDIFGDGVLEILQDGFGFLRSADSSYLAGPDDIYVSPSQIRRFNLRTGDTISGKIRPPKEGERYFALLKVNEVNFDKPENARNKILFENLTPLHANSRLRMERGNGSTEDLTARVLDLASPIGRGQRGLIVAPPKAGKTMLLQNIAQSIAYNHPDCVLMVLLIDERPEEVTEMQRLVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVIILLDSITRLARAYNTVVPASGKVLTGGVDANALHRPKRFFGAARNVEEGGSLTIIATALIDTGSKMDEVIYEEFKGTGNMELHLSRKIAEKRVFPAIDYNRSGTRKEELLTTQEELQKMWILRKIIHPMGEIDAMEFLINKLAMTKTNDDFFEMMKRS
Expression Range	1-419aa
Protein Length	Full Length
Mol. Weight	51.0kDa
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	Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template. RNA-dependent NTPase which utilizes all four ribonucleoside triphosphates as substrates.
Protein Families	Rho family
Database References	KEGG: ecj:JW3756 STRING: 316385.ECDH10B_3972

Gene Functions References

Our findings further show that the RNA sequence specificity used for guiding Rho-dependent termination derives in part from an intrinsic ability of the motor to couple the recognition of pyrimidine patterns in nascent transcripts to RNA loading and activity. PMID: 27821776
results, together with existing data, support a model in which the connector segment plays a hitherto overlooked role in the regulation of Rho-dependent termination PMID: 28559482
Translational control and Rho-dependent transcription termination are intimately linked in riboswitch regulation. PMID: 28520932
NusG acts as both a positive and negative regulator of Rho in the course of the bacterial transcription termination. (Review) PMID: 27023849
Finally, identification of the NusG binding sites on the Rho hexamer led us to conclude that the former exerts its effect allosterically. PMID: 27605667
Rho inhibition leads to RNA polymerase readthrough, which in principle could displace H-NS from the DNA, thus leading to transcriptional derepression of H-NS-silenced genes. PMID: 24499790
Rho binds C-rich unstructured nascent RNA (high C/G ratio) prior to its ATP-dependent dissociation of transcription complexes PMID: 23207917
Tthe in vivo Rho-dependent termination process is kinetically controlled. PMID: 22442304
Here the authors provide direct evidence that the beta-sheet bundle of the C-terminal domain of NusG (NusG-CTD) has the binding determinants for Rho. PMID: 21040729
The authors mutated E211, R366, R212, and D265, and characterized the resulting proteins for oligomerization, ligand binding and RNA-dependent ATP hydrolysis that support the existing model of ATP hydrolysis. PMID: 20950626
Global hydrogen-deuterium exchange indicate net mass differences of about 15 Da after 1 h of exchange in the presence--versus in the absence--of the ligand MgATP or the RNA poly(C). PMID: 20708016
Results indicate that all three Rho catalytic sites must be filled with substrate to achieve the enhanced catalytic rate, both in pre-steady-state and in steady-state hydrolysis. PMID: 15703177
Results reinforce the importance of catalytic cooperativity in normal Rho function and suggest that several protein conformations exist along the catalytic pathway. PMID: 15703178
findings show that transcription termination of fimE is Rho dependent and is suppressed in a rho mutant or by bicyclomycin treatment when fimE mRNA is expressed by the fimE gene, either from a recombinant plasmid or in its native chromosomal location PMID: 16321930
mutant forms of Rho were defective in transcriptional termination, suggesting that those residues play an important role in the activation of Rho by bound RNA PMID: 16908525
interactions in the primary RNA binding domain and in the Q-loop are mandatory for RNA release to occur and propose that the interactions in the primary RNA binding modulate most of the other functions of Rho allosterically PMID: 17599352
results reveal Rho factor as a global regulator of gene expression under normal growth conditions; it serves role of maintaining transcriptional boundaries; Rho termination, supported by NusA & NusG, is required to suppress toxic activity of foreign genes PMID: 18487194
ADP but not P(i) dissociation contributes to rate limitation for Escherichia coli Rho PMID: 19837672
These data show that Rho forms uneven productive interactions with the track nucleotides and disrupts RNA-DNA duplexes in a succession of large (approximately 7-nucleotide-long) discrete steps triggered by 2'-hydroxyl activation events. PMID: 19915588

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.