ZDHC3 Antibody (N-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, E |
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Primary Accession | Q9NYG2 |
Other Accession | NP_057682.1, NP_001128651.1 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 34170 Da |
Antigen Region | 1-30 aa |
Gene ID | 51304 |
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Other Names | Palmitoyltransferase ZDHHC3, Protein DHHC1, Zinc finger DHHC domain-containing protein 3, DHHC-3, Zinc finger protein 373, ZDHHC3, ZNF373 |
Target/Specificity | This ZDHC3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human ZDHC3. |
Dilution | WB~~1:1000 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | ZDHC3 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | ZDHHC3 (HGNC:18470) |
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Function | Golgi-localized palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates (PubMed:19001095, PubMed:21926431, PubMed:22240897, PubMed:23034182, PubMed:22314500). Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (By similarity). Plays an important role in G protein-coupled receptor signaling pathways involving GNAQ and potentially other heterotrimeric G proteins by regulating their dynamic association with the plasma membrane (PubMed:19001095). Palmitoylates ITGA6 and ITGB4, thereby regulating the alpha-6/beta-4 integrin localization, expression and function in cell adhesion to laminin (PubMed:22314500). Plays a role in the TRAIL-activated apoptotic signaling pathway most probably through the palmitoylation and localization to the plasma membrane of TNFRSF10A (PubMed:22240897). In the brain, by palmitoylating the gamma subunit GABRG2 of GABA(A) receptors and regulating their postsynaptic accumulation, plays a role in synaptic GABAergic inhibitory function and GABAergic innervation (By similarity). Palmitoylates the neuronal protein GAP43 which is also involved in the formation of GABAergic synapses (By similarity). Palmitoylates NCDN thereby regulating its association with endosome membranes (By similarity). Probably palmitoylates PRCD and is involved in its proper localization within the photoreceptor (By similarity). Could mediate the palmitoylation of NCAM1 and regulate neurite outgrowth (By similarity). Could palmitoylate DNAJC5 and regulate its localization to Golgi membranes (By similarity). Also constitutively palmitoylates DLG4 (By similarity). May also palmitoylate SNAP25 (By similarity). Could palmitoylate the glutamate receptors GRIA1 and GRIA2 but this has not been confirmed in vivo (By similarity). Could also palmitoylate the D(2) dopamine receptor DRD2 (PubMed:26535572). May also palmitoylate LAMTOR1, promoting its localization to lysosomal membranes (PubMed:35893977). |
Cellular Location | Golgi apparatus membrane; Multi-pass membrane protein. Note=Localizes to the Golgi cis cisterna. {ECO:0000250|UniProtKB:Q8R173} |
Tissue Location | Widely expressed with significant expression in heart, lung, liver, skeletal muscle, kidney, testis, thymus, small intestine and leukocyte. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Palmitoyltransferase with broad specificity. Palmitoylates GABA receptors on their gamma subunit (GABRG1, GABRG2 and GABRG3), which regulates synaptic clustering and/or cell surface stability. Palmitoylates glutamate receptors GRIA1 and GRIA2, which leads to their retention in Golgi (By similarity).
References
Hines, R.M., et al. J. Biol. Chem. 285(7):4621-4628(2010)
Lim, J., et al. Cell 125(4):801-814(2006)
Colland, F., et al. Genome Res. 14(7):1324-1332(2004)
Uemura, T., et al. Biochem. Biophys. Res. Commun. 296(2):492-496(2002)
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