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Phosphorylation: One of the Hottest Topics in Cell Biology Research

Published: Tuesday, November 26, 2013
Last Updated: Tuesday, November 26, 2013
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Over 140 phosphospecific antibodies are developed in AbboMax, Inc.

Phosphorylation plays critical roles in the regulation of many cellular processes. It is tightly associated with protein activity and is a key point of protein function regulation.

Phosphorylation is the attachment of a phosphate group to a protein or other organic molecule.

Once the new phosphate group is added by protein phosphorylation, it changes the structure of its host protein. The new phosphorus group alters the role of the protein: it can activate, deactivate, or cause a change in function. It turns many protein enzymes on and off.

Reversible phosphorylation of proteins is an important regulatory mechanism that occurs in both prokaryotic and eukaryotic organisms.

Protein phosphorylation is a post-translational modification of proteins in which a serine, a threonine, and/or tyrosine residue are phosphorylated by a protein kinase.

Sometimes a cell uses a phosphorylation cascade, to produce an outcome. Upon the deactivating signal, the protein becomes dephosphorylated again and stops working. A phosphatase is an enzyme that removes a phosphate group from the protein.

AbboMax, Inc. has developed over 140 phosphospecific antibodies. The unique Universal phosphotyrosine antibody is among them.

Another group, anti-AMP-activated protein kinase (AMPK) antibodies are highly conserved from yeast to plants and animals and play a key role in the regulation of energy balance at both the cellular and the whole body levels.

Once activated, it affects a metabolic switch from an anabolic to a catabolic state, both by acutely phosphorylating metabolic enzymes and, in the longer term, by regulating gene expression. AbboMax offers a group of anti-estrogen receptor (ER) antibodies. ER is a member of the steroid receptor superfamily.

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