acnB Antibody

E. coli acnB Antibody Datasheet

E. coli acnB Antibody Product Information

• Immunogen: Recombinant E. coli acnB protein (Catalog#13102-ENAE)
• Antibody Type: Rabbit Monoclonal Antibody ( Rabbit mAb Service Platform )
• Clone ID: 102
• Ig Type: Rabbit IgG
• Formulation: 0.2 μm filtered solution in PBS with 5% trehalose
• Preparation: This antibody was obtained from a rabbit immunized with purified, recombinant E. coli acnB (rE. coli acnB; Catalog#13102-ENAE; P36683; Met 1-Val 865).

E. coli acnB Antibody Usage Guide

• Specificity: E. coli acnB
• Direct ELISA: This antibody can be used at 0.1-0.2 μg/mL with the appropriate secondary reagents to detect E. coli ACNB. The detection limit for E. coli ACNB is approximately 0.0049 ng/well.
• Storage: This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -70℃. Preservative-Free.
  Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles.

E. coli acnB Antibody Background

Escherichia coli contains two major aconitases (Acns), AcnA and AcnB. They are distantly related monomeric Fe-S proteins that contain different arrangements of four structural domains. acnA is specifically subject to SoxRS-mediated activation, whereas acnB encodes the major aconitase that is synthesized earlier in the growth cycle than AcnA. It is concluded that AcnB is the major citric acid cycle enzyme. Aconitate hydratase 2 (acnB) catalyzes the isomerization of citrate to isocitrate via cis-aconitate as well as the dehydration of 2-methylisocitrate to cis-2-methylaconitate, thus it functions as the major citric-acid-cycle enzyme during exponential growth. Escherichia coli acnB serves as either an enzymic catalyst or a mRNA-binding post-transcriptional regulator, depending on the status of its iron sulfur cluster. AcnB represents a large, distinct group of Gram-negative bacterial aconitases that have an altered domain organization relative to mitochondrial aconitase and other aconitases.

References

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3. Jordan PA. et al., 1999, Biochem J. 344 Pt 3: 739-46.
4. Williams CH. et al., 2002, Nat Struct Biol. 9 (6): 447-52.