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AB139789

Recombinant Human Pofut1 protein (denatured)

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Recombinant Human Pofut1 protein (denatured) is a Human Full Length protein, in the 27 to 388 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE.

View Alternative Names

FUT12, KIAA0180, POFUT1, GDP-fucose protein O-fucosyltransferase 1, Peptide-O-fucosyltransferase 1, O-FucT-1

1 Images
SDS-PAGE - Recombinant Human Pofut1 protein (denatured) (AB139789)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human Pofut1 protein (denatured) (AB139789)

15% SDS-PAGE analysis of ab139789 (3μg).

Key facts

Purity

>85% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q9H488

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 12.01% Urea, 10% Glycerol (glycerin, glycerine), 0.32% Tris HCl

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMGSGSWDPAGYLLYCPCMGRFGNQADHFLGSLAFAKLLNRTLAVPPWIEYQHHKPPFTNLHVSYQKYFKLEPLQAYHRVISLEDFMEKLAPTHWPPEKRVAYCFEVAAQRSPDKKTCPMKEGNPFGPFWDQFHVSFNKSELFTGISFSASYREQWSQRFSPKEHPVLALPGAPAQFPVLEEHRPLQKYMVWSDEMVKTGEAQIHAHLVRPYVGIHLRIGSDWKNACAMLKDGTAGSHFMASPQCVGYSRSTAAPLTMTMCLPDLKEIQRAVKLWVRSLDAQSVYVATDSESYVPELQQLFKGKVKVVSLKPEVAQVDLYILGQADHFIGNCVSSFTAFVKRERDLQGRPSSFFGMDRPPKLRDEF","proteinLength":"Full Length","predictedMolecularWeight":"43.7 kDa","actualMolecularWeight":null,"aminoAcidEnd":388,"aminoAcidStart":27,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q9H488","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
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
False

Supplementary information

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

The protein known as Pofut1 or protein O-fucosyltransferase 1 functions mechanically by adding fucose a sugar molecule to serine or threonine residues on proteins specifically within the epidermal growth factor-like (EGF-like) repeats of substrates. Pofut1 has a molecular weight of approximately 50 kDa. This protein is expressed in various tissues including heart liver and brain indicating its significant role across different biological systems. Researchers commonly refer to Pofut1 in studies focused on protein glycosylation processes.
Biological function summary

Pofut1 is responsible for the proper folding and functioning of specific proteins that undergo fucosylation. It does not technically form part of a multi-protein complex but interacts tightly with substrates it modifies. Through its enzymatic action Pofut1 influences essential biological activities in cell communication and signaling. This glycosyltransferase also plays a pivotal role in modulating Notch signaling a critical pathway in the development and tissue regeneration processes.

Pathways

The significance of Pofut1 is most notable within the Notch signaling pathway where it modifies the Notch receptor enabling effective ligand-receptor interactions. Dysregulation of this pathway can lead to critical developmental defects. Pofut1 also connects to other pathways such as the Fringe-mediated glycosylation pathway. In this context Pofut1-related proteins like Fringe glycosyltransferases operate to further influence Notch signaling outcomes through additional glycosylation processing.

The functionality of Pofut1 has links to specific syndromes and malignancies. For instance aberrations in its activity are associated with congenital heart defects due to disrupted Notch signaling affecting cardiac development. Additionally overexpression or mutations in Pofut1 relate to cancer as improper Notch signaling can lead to tumor progression. Relatedly proteins like Notch1 serve as intermediaries linking Pofut1 activity to such conditions thereby highlighting Pofut1's involvement in disease etiologies.

Specifications

Form

Liquid

General info

Function

Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines. Specifically uses GDP-fucose as donor substrate and proper disulfide pairing of the substrate EGF domains is required for fucose transfer. Plays a crucial role in NOTCH signaling. Initial fucosylation of NOTCH by POFUT1 generates a substrate for FRINGE/RFNG, an acetylglucosaminyltransferase that can then extend the fucosylation on the NOTCH EGF repeats. This extended fucosylation is required for optimal ligand binding and canonical NOTCH signaling induced by DLL1 or JAGGED1. Fucosylates AGRN and determines its ability to cluster acetylcholine receptors (AChRs).

Sequence similarities

Belongs to the glycosyltransferase 65 family.

Post-translational modifications

N-glycosylated.

Product protocols

Target data

Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines. Specifically uses GDP-fucose as donor substrate and proper disulfide pairing of the substrate EGF domains is required for fucose transfer. Plays a crucial role in NOTCH signaling. Initial fucosylation of NOTCH by POFUT1 generates a substrate for FRINGE/RFNG, an acetylglucosaminyltransferase that can then extend the fucosylation on the NOTCH EGF repeats. This extended fucosylation is required for optimal ligand binding and canonical NOTCH signaling induced by DLL1 or JAGGED1. Fucosylates AGRN and determines its ability to cluster acetylcholine receptors (AChRs).
See full target information POFUT1

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