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AB154054

Anti-HIP14 antibody

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(1 Publication)

Rabbit Polyclonal HIP14 antibody. Suitable for WB and reacts with Mouse, Human samples. Cited in 1 publication. Immunogen corresponding to Recombinant Fragment Protein within Human ZDHHC17 aa 1-300.

View Alternative Names

HIP14, HIP3, HYPH, KIAA0946, HSPC294, ZDHHC17, Palmitoyltransferase ZDHHC17, Acyltransferase ZDHHC17, DHHC domain-containing cysteine-rich protein 17, Huntingtin yeast partner H, Huntingtin-interacting protein 14, Huntingtin-interacting protein 3, Huntingtin-interacting protein H, Putative MAPK-activating protein PM11, Putative NF-kappa-B-activating protein 205, Zinc finger DHHC domain-containing protein 17, DHHC17, HIP-14, HIP-3

2 Images
Western blot - Anti-HIP14 antibody (AB154054)
  • WB

Unknown

Western blot - Anti-HIP14 antibody (AB154054)

7.5% SDS PAGE

All lanes:

Western blot - Anti-HIP14 antibody (ab154054) at 1/3000 dilution

All lanes:

U-87 MG whole cell lysate at 30 µg

Predicted band size: 73 kDa

false

Western blot - Anti-HIP14 antibody (AB154054)
  • WB

Unknown

Western blot - Anti-HIP14 antibody (AB154054)

7.5% SDS PAGE

All lanes:

Western blot - Anti-HIP14 antibody (ab154054) at 1/2000 dilution

All lanes:

C8D30 whole cell lysate at 30 µg

Predicted band size: 73 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Mouse, Human

Applications

WB

applications

Immunogen

Recombinant Fragment Protein within Human ZDHHC17 aa 1-300. The exact immunogen used to generate this antibody is proprietary information.

Q8IUH5

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Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7 Preservative: 0.01% Thimerosal (merthiolate) Constituents: 20% Glycerol (glycerin, glycerine), 1.21% Tris, 0.75% Glycine
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

HIP14 also known as huntingtin-interacting protein 14 or ZDHHC17 is a palmitoyl transferase weighing approximately 75 kilodaltons. This enzyme catalyzes the reversible addition of palmitic acid to cysteine residues a process known as S-palmitoylation. HIP14 is widely expressed in the brain and other tissues. It localizes primarily to the Golgi apparatus but can also be found in endosomes and synaptic vesicles. Its expression pattern and enzyme activity suggest significant roles in cellular signaling and protein trafficking.
Biological function summary

HIP14 interacts with a variety of proteins functioning as part of the palmitoyl acyltransferase complex. This complex modulates membrane localization and function of target proteins through palmitoylation. HIP14 directly interacts with huntingtin protein influencing neuronal morphology and stability. By regulating protein palmitoylation HIP14 affects neural development and synaptic function. Its activity extends to modulating neurotransmitter receptors such as NMDA receptors impacting synaptic plasticity.

Pathways

HIP14 engages in important signaling cascades. It plays a role in synaptic signaling and neuronal survival by affecting the Ras and Wnt pathways. In the Ras pathway HIP14 modifies proteins like HRas altering signal transduction and cellular responses. Through the Wnt pathway HIP14 impacts downstream components such as β-catenin contributing to neurodevelopment processes and homeostasis. The functional relationship with other palmitoyl transferases highlights HIP14's distinct yet cooperative role in cellular signaling networks.

HIP14 shows strong association with neurodegenerative diseases and neuropathologies. It is specifically implicated in Huntington's disease where mutant huntingtin disrupts HIP14 function. The interaction between HIP14 and huntingtin protein is pivotal affecting neuronal integrity and function. In peripheral neuropathy HIP14's altered activity can lead to abnormal neuron structure and function. Dysregulated palmitoylation may impact neurofilament-mediated axonal transport indicating HIP14's critical role in neurodegenerative conditions.
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Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:
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Target data

Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates and is involved in a variety of cellular processes (PubMed : 15489887, PubMed : 15603740, PubMed : 24705354, PubMed : 27911442, PubMed : 28757145). 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). Palmitoyltransferase specific for a subset of neuronal proteins, including SNAP25, DLG4/PSD95, GAD2, SYT1 and HTT (PubMed : 15489887, PubMed : 15603740, PubMed : 19139280, PubMed : 28757145). Also palmitoylates neuronal protein GPM6A as well as SPRED1 and SPRED3 (PubMed : 24705354). Could also play a role in axonogenesis through the regulation of NTRK1 and the downstream ERK1/ERK2 signaling cascade (By similarity). May be involved in the sorting or targeting of critical proteins involved in the initiating events of endocytosis at the plasma membrane (PubMed : 12393793). May play a role in Mg(2+) transport (PubMed : 18794299). Could also palmitoylate DNAJC5 and regulate its localization to the Golgi membrane (By similarity). Palmitoylates CASP6, thereby preventing its dimerization and subsequent activation (PubMed : 27911442).
See full target information ZDHHC17
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Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Scientific reports 14:9571 PubMed38671086

2024

Hyper-N-glycosylated SEL1L3 as auto-antigenic B-cell receptor target of primary vitreoretinal lymphomas.

Applications

Unspecified application

Species

Unspecified reactive species

Michelle Elbert,Frank Neumann,Maximilian Kiefer,Konstantinos Christofyllakis,Benedikt Balensiefer,Igor Kos,Gabi Carbon,Dominic Kaddu-Mulindwa,Joerg Thomas Bittenbring,Natalie Fadle,Evi Regitz,Falko Fend,Irina Bonzheim,Lorenz Thurner,Moritz Bewarder
View all publications
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