Chicken Salmonella Enteritidis IgY ELISA Kit (DEIABL37)

Regulatory status: For research use only, not for use in diagnostic procedures.

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Size
96T
Sample
Serum, Plasma, other biological fluids
Species Reactivity
Chick
Intended Use
The Chicken Salmonella Enteritidis IgY (CSE-IgY) ELISA Kit is to be used for the vitro quantitative determination of Chicken CSE-IgY in Serum, Plasma and other biological fluids. The Kit is intended for research use only, not for diagnostic or therapeutic procedure. If detection of other special sample, please contact our technical support.
Contents of Kit
1. Wash solution: 20 mL×1bottle
2. HRP-Conjugate reagent: 6 mL×1 bottle
3. Microelisa stripplate: 12well×8strips
4. Sample diluent: 6 mL×1 bottle
5. Chromogen Solution A: 6 mL×1 bottle
6. Chromogen Solution B: 6 mL×1 bottle
7. Standard 100ng/ml: 0.5 mL×1 bottle
8. Standard diluent: 6 mL×1 bottle
9. Stop Solution: 6 mL×1 bottle
10. Instruction: 1
11. Closure plate membrane: 2
12. Sealed bags: 1
Storage
Storage:2-8°C
Validity: 6 months
Precision
Intra-Assay: CV≤ 15%
Inter-Assay: CV≤15%
Detection Range
3.5ng/mL - 100ng/mL
Sensitivity
< 1.2ng/mL

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References


Ribonucleases control distinct traits of Pseudomonas putida lifestyle

ENVIRONMENTAL MICROBIOLOGY

Authors: Apura, Patricia; de Lorenzo, Victor; Arraiano, Cecilia M.; Martinez-Garcia, Esteban; Viegas, Sandra C.

The role of archetypal ribonucleases (RNases) in the physiology and stress endurance of the soil bacterium and metabolic engineering platform Pseudomonas putida KT2440 has been inspected. To this end, variants of this strain lacking each of the most important RNases were constructed. Each mutant lacked either one exoribonuclease (PNPase, RNase R) or one endoribonuclease (RNase E, RNase III, RNase G). The global physiological and metabolic costs of the absence of each of these enzymes were then analysed in terms of growth, motility and morphology. The effects of different oxidative chemicals that mimic the stresses endured by this microorganism in its natural habitats were studied as well. The results highlighted that each ribonuclease is specifically related with different traits of the environmental lifestyle that distinctively characterizes this microorganism. Interestingly, the physiological responses of P. putida to the absence of each enzyme diverged significantly from those known previously in Escherichia coli. This exposed not only species-specific regulatory functions for otherwise known RNase activities but also expanded the panoply of post-transcriptional adaptation devices that P. putida can make use of for facing hostile environments.

The inner membrane protein YhdP modulates the rate of anterograde phospholipid flow in Escherichia coli

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Authors: Grimm, Jacqueline; Shi, Handuo; Wang, Wei; Mitchell, Angela M.; Wingreen, Ned S.; Huang, Kerwyn Casey; Silhavy, Thomas J.

The outer membrane (OM) of Gram-negative bacteria is a selective permeability barrier that allows uptake of nutrients while simultaneously protecting the cell from harmful compounds. The basic pathways and molecular machinery responsible for transporting lipopolysaccharides (LPS), lipoproteins, and beta-barrel proteins to the OM have been identified, but very little is known about phospholipid (PL) transport. To identify genes capable of affecting PL transport, we screened for genetic interactions with mlaA*, a mutant in which anterograde PL transport causes the inner membrane (IM) to shrink and eventually rupture; characterization of mlaA* mediated lysis suggested that PL transport can occur via a highflux diffusive flow mechanism. We found that YhdP, an IM protein involved in maintaining the OM permeability barrier, modulates the rate of PL transport during mlaA*-mediated lysis. Deletion of yhdP from mlaA* reduced the rate of IM transport to the OM by 50%, slowing shrinkage of the IM and delaying lysis. As a result, the weakened OM of AyhdP cells was further compromised and ruptured before the IM during mlaA*-mediated death. These findings demonstrate the existence of a high-flux diffusive pathway for PL flow in Escherichia coli that is modulated by YhdP.

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