Recombinant Staphylococcus aureus Acyl carrier protein (Tagged)
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Recombinant Staphylococcus aureus Acyl carrier protein (Tagged) is a Staphylococcus aureus subsp. aureus Mu50 Full Length protein, in the 1 to 77 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.
View Alternative Names
hmrB, SAV1232, acpP, Acyl carrier protein, ACP
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Staphylococcus aureus Acyl carrier protein (Tagged) (AB235813)
(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel analysis of ab235813.
Reactivity data
Sequence info
Properties and storage information
Form
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Acyl carrier proteins play an essential role in lipid metabolism by ensuring the transfer of acyl intermediates. ACP acts as a cofactor to enzymes in the fatty acid synthase complex enabling the elongation of carbon chains during lipid synthesis. By binding acyl groups ACP facilitates their transfer to specific enzymes within this complex ensuring efficient synthesis.
Pathways
The acyl carrier proteins are integral to the fatty acid synthesis pathway. This pathway involves enzymes such as acetyl-CoA carboxylase which initiates the conversion of acetyl-CoA to malonyl-CoA a substrate modified later by ACP. In addition to fatty acid synthesis ACP is involved in the polyketide synthesis pathway working alongside polyketide synthase to play a role in the production of secondary metabolites.
General info
Function
Carrier of the growing fatty acid chain in fatty acid biosynthesis. Is able to confer high methicillin resistance to S.aureus when overproduced (By similarity).
Sequence similarities
Belongs to the acyl carrier protein (ACP) family.
Post-translational modifications
4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Target data
Product promise
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