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Adenylylation-Specific Antibody Production Services

Creative Biolabs offers adenylylation-specific antibody production services to our global customers based on our excellent High-Affi™ technology. The antibodies are produced with high affinity by immunization of animals with AMP-bovine serum albumin conjugate and purification with affinity column chromatography. These antibodies specifically bind to the AMP moiety of adenylylated proteins but do not cross-react with ADP or RNA.

Adenylylation, also known as AMPylation, is a post-translational modification (PTM) that is the covalent addition of adenosine monophosphate (AMP) molecule to a hydroxyl side chain of protein. This modification involves the formation of a phosphodiester bond between a hydroxyl group of the target proteins and the phosphate group of the adenosine monophosphate nucleotide (i.e. adenylic acid). Adenylylation is a stable and reversible process that usually occurs to tyrosine, serine, and threonine residues.

The enzymes that catalyze adenylylation are called AMPylators. To date, the proteins containing either the adenylyltransferase (ATase) domain or the filamentation induced by cAMP (fic) domain have been identified as candidate adenylyltransferases or AMPylators from bacteria to humans. Adenylyltransferases are common difunctional enzymes which are involved in the addition and removal of AMP. GS-ATasE (GlnE) is an AMPylator that has been shown to catalyze de-AMPylation of glutamine synthetase.

Targets, Functions, and Pathogenicity of Adenylylation

Adenylylation is particularly taken place in the context of infections by bacterial pathogens. The bacterial proteins, such as VopS, IbpA, and DrrA, serve as enzymes to adenylylated host proteins, including glutamine synthetase (GS), Rho, Rab, and GTPases. As a result, adenylylation disabled the host cell’s actin cytoskeleton control, leading to cell rounding. Glutamine synthetase, an enzyme that plays an important role in the metabolism of nitrogen, was the first found to be regulated by adenylylation. The rate of adenylylation depends on the ratio of glutamine to α-ketoglutarate. A low ratio is a sign of cellular nitrogen sufficiency, whereas a high ratio is evidence of a limited nitrogen supply and the need for ammonia fixation by glutamine synthetase. GTPases are commonly modified by AMPylators which appear to modulate cytoskeletal rearrangement and vesicular trafficking. They also play roles in cellular control mechanisms such as phagocytosis in the host cell, in which the pathogen enhances or prevents its internalization by either inducing or inhibiting host cell phagocytosis.

Adenylylation of small GTPases by Fic domains and the structures of adenylylated GTPases Fig. 1 Adenylylation of small GTPases by Fic domains and the structures of adenylylated GTPases. (Itzen A, et. al 2011)

Modification-specific antibodies are used to detect the adenylylated proteins, especially widely used in the state of bacterial infections. Creative Biolabs can tailor customers’ requirement with cutting-edge technology in producing antibodies. The productions are 100% guaranteed.

Creative Biolabs can provide a comprehensive list of PTM-specific antibody production services of your choice.


  1. Itzen A, Blankenfeldt W, and Goody R S.  (2011). “Adenylylation: Renaissance of a forgotten post-translational modification”. Trends Biochem Sci, 36(4): 221-228.

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