AASD-PPT polyclonal antibody; host Rabbit; reactivity Human, Mouse, Rat
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aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase(AASDHPPT) Homo sapiens The protein encoded by this gene is similar to Saccharomyces cerevisiae LYS5, which is required for the activation of the alpha-aminoadipate dehydrogenase in the biosynthetic pathway of lysine. Yeast alpha-aminoadipate dehydrogenase converts alpha-biosynthetic-aminoadipate semialdehyde to alpha-aminoadipate. It has been suggested that defects in the human gene result in pipecolic acidemia. [provided by RefSeq, Jul 2008],
Fully tested in-house by ABMIUM, or supported by an advanced validation report from a partner reviewed by ABMIUM. Highest confidence. Non-conformities fully supported under the ABMIUM Product Promise.
Quality verified. Independent collaborator or expected-performance data available. Product meets ABMIUM quality standards.
Expected to work based on structural and biochemical data. Not yet directly tested by ABMIUM or a collaborator. No non-conformity support for this combination.
Not recommended for this application or species/sample combination. This may indicate either evidence of unsuitability or that the combination has not been tested and therefore cannot currently be recommended.
Evidence status by application and model.
| Species / reactivity | WB | IHC-P | IF | ELISA |
|---|---|---|---|---|
| Human,Mouse,Rat |
This product is manufactured by Reed Biotech and sold through ABMIUM without relabelling.
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AASDHPPT (aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase; also called holo-ACP synthase) is the human 4′-phosphopantetheinyl transferase that converts apo carrier-protein domains to their active holo forms by transferring the phosphopantetheine arm from coenzyme A. This post-translational step enables carrier-protein chemistry in lipid and other phosphopantetheine-dependent biosynthetic systems.
Biological function: AASDHPPT transfers the 4′-phosphopantetheine moiety of coenzyme A to a conserved serine on compatible acceptor proteins. Reviewed UniProt evidence includes phosphopantetheinylation of the acyl-carrier domain of fatty acid synthase (FASN), enabling that carrier domain to shuttle pathway intermediates during fatty-acid synthesis.
