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Fatty Acylation (Myristoylation, Palmitoylation) Specific Antibody Discovery Service

Background Product Services

Background

Creative Biolabs provides fatty acylation-specific antibodies with high affinity to global customers based on our excellent High-Affi™ technology. The antibodies include N-myristoylation and palmitoylation specific antibodies.

Fatty acylation is the covalent attachment of fatty acid moieties to proteins. This distinguishes acylation from other hydrophobic modifications such as prenylation and cholesterol modification, where a myristate or a palmitate is directly linked to proteins to form N-myristoylation or palmitoylation, respectively.

Protein N-myristoylation is a ubiquitous co-translational and post-translational modification which attaches myristate, a 14-carbon saturated fatty acid, to an N-terminal glycine residue. The enzyme N-myristoyltransferase (NMT) catalyzes the irreversible covalent addition, and this modification event is found commonly in many organisms including animals, plants, fungi, protozoans and viruses. N-myristoylation plays an essential role in intracellular trafficking, membrane targeting, protein-protein and protein-lipid interactions and implicates in diverse physiological processes, such as apoptosis, morphology change, and virus assembly. Aberrant regulation of N-myristoylation can lead to tumorigenesis and viral infectivity. The expression and activity of NMT are considerably enhanced in a number of cancers. Increased myristoylation of c-Src may result in upregulation of angiogenesis, cancer cells proliferation and invasion. Therefore, the myristoylation process has become a novel therapeutic strategy for anticancer drug design.

Fig.1 Protein N-Myristoylation. (From Wikipedia: By Lengkr, CC BY-SA 3.0, https://commons.wikimedia.org/wiki/File:Co-_and_Post-Translational_Myristoylation.png) Fig.1 Protein N-Myristoylation.1

S-palmitoylation, the only reversible post-translational lipid modification, is the covalent attachment of a 16-carbon atom fatty acid to a cysteine residue of target proteins. S-palmitoylation is dynamically regulated by two opposite enzymes, transferred by palmitoyl acyltransferases (PAT), and removed by acyl protein thioesterases. Palmitoylation is widely distributed in eukaryotes, bacteria, and viruses, and affects multiple regulatory processes by modulating protein stability, folding, and trafficking, altering subcellular localization and affecting protein-protein interactions. To date, palmitoylation has been reported to be associated with various human diseases, including neurodegenerative diseases and cancer.

Fig. 2 Protein S-palmitoylation. (C. Kim and I. Ross, 2013) Fig. 2 Protein S-palmitoylation.2, 3

Myristoylation and palmitoylation are usually coupled modifications on proteins. Myristoylation alone promotes membrane interactions transiently due to quick dissociation. However, further palmitoylation can more tightly anchor to the membrane and slower the separation of the palmitoylated protein from membranes. GPCR pathways are profit from this specific dual fatty acylation. The two fatty acylations also make cross-talk to other modifications. For example, in the process of G protein signal transduction, the α subunit of G protein becomes palmitoylated and the γ subunit prenylated, then G protein becomes myristoylated so as to be tethered to the inner surface of the plasma membrane. Finally, the G protein can interact with its receptor.

Creative Biolabs is an undoubted pioneer and experienced expert in antibody research and development field, especially in PTM antibodies exploitation. Based on the advanced technology, our scientists offer the most comprehensive antibody production services to meet our customers’ specific requirements.

Product

  • Anti-pan palmitoylated cysteine polyclonal antibody (CBL-PTM-pal)

    • Derivation: Rabbit
    • Application: ELISA, Dot blot, WB
    COA 1; COA 2

Services

In addition to the fatty acylation-specific antibody, Creative Biolabs also provides a comprehensive list of PTM-specific antibody production services of your choice.

References

  1. From Wikipedia: By Lengkr, CC BY-SA 3.0,
    https://commons.wikimedia.org/wiki/File:Co-_and_Post-Translational_Myristoylation.png
  2. C. Kim and I. Ross, "Regulatory Role of Free Fatty Acids (FFAs)—Palmitoylation and Myristoylation," Food and Nutrition Sciences, Vol. 4 No. 9A, 2013, pp. 202-211.
  3. under Open Access license CC BY 4.0, without modification.

All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

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