rho Antibody, Biotin conjugated

Code CSB-PA16629D0Rb
Size US$166
Order now
Have Questions? Leave a Message or Start an on-line Chat

Product Details

Full Product Name
Rabbit anti-Escherichia coli rho Polyclonal antibody
Uniprot No.
Target Names
rho
Alternative Names
rho antibody; nitA antibody; psuA antibody; rnsC antibody; sbaA antibody; tsu antibody; b3783 antibody; JW3756 antibody; Transcription termination factor Rho antibody; EC 3.6.4.- antibody; ATP-dependent helicase Rho antibody
Raised in
Rabbit
Species Reactivity
Escherichia coli
Immunogen
Recombinant Escherichia coli Transcription termination factor Rho protein (1-419AA)
Immunogen Species
Escherichia coli
Conjugate
Biotin
Clonality
Polyclonal
Isotype
IgG
Purification Method
>95%, Protein G purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4
Form
Liquid
Tested Applications
ELISA
Protocols
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

Customer Reviews and Q&A

 Customer Reviews

There are currently no reviews for this product.

Submit a Review here

Target Background

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.
Gene References into Functions
  1. 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
  2. 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
  3. Translational control and Rho-dependent transcription termination are intimately linked in riboswitch regulation. PMID: 28520932
  4. NusG acts as both a positive and negative regulator of Rho in the course of the bacterial transcription termination. (Review) PMID: 27023849
  5. Finally, identification of the NusG binding sites on the Rho hexamer led us to conclude that the former exerts its effect allosterically. PMID: 27605667
  6. 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
  7. Rho binds C-rich unstructured nascent RNA (high C/G ratio) prior to its ATP-dependent dissociation of transcription complexes PMID: 23207917
  8. Tthe in vivo Rho-dependent termination process is kinetically controlled. PMID: 22442304
  9. 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
  10. 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
  11. 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
  12. 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
  13. Results reinforce the importance of catalytic cooperativity in normal Rho function and suggest that several protein conformations exist along the catalytic pathway. PMID: 15703178
  14. 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
  15. 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
  16. 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
  17. 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
  18. ADP but not P(i) dissociation contributes to rate limitation for Escherichia coli Rho PMID: 19837672
  19. 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

Show More

Hide All

Protein Families
Rho family
Database Links
CUSABIO guaranteed quality
icon of phone
Call us
301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
icon of address
Address
7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
icon of social media
Join us with

Subscribe newsletter

Leave a message

* To protect against spam, please pass the CAPTCHA test below.
CAPTCHA verification
© 2007-2024 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1
webinars: DT3C facilitates antibody internalization X
Place an order now

I. Product details

*
*
*
*

II. Contact details

*
*

III. Ship To

*
*
*
*
*
*
*

IV. Bill To

*
*
*
*
*
*
*
*