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GDP-Fucose Protein O-Fucosyltransferase 1 (POFUT1) Pan Troglodytes Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures. Catalog #: MBS1368832

MBS1368832 is a recombinant protein targeting POFUT1. Also known as Recombinant Pan troglodytes GDP-fucose protein O-fucosyltransferase 1 (POFUT1). Host: E Coli or Yeast or Baculovirus or Mammalian Cell. More details

$1080 / 0.02 mg (E-Coli) +1 FREE 8GB USB
Product Documentation
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Sample Manual Insert View PDF
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Testing Data View PDF
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Certificate of Analysis (COA) View PDF
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QC Report View PDF
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Material Safety Data Sheet View PDF
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Technical Datasheet View PDF
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Protocol View PDF

Product Overview

Online Datasheet in PDF
Product Name
GDP-fucose protein O-fucosyltransferase 1 (POFUT1), Recombinant Protein
Full Product Name
Recombinant Pan troglodytes GDP-fucose protein O-fucosyltransferase 1 (POFUT1)
Product Synonym Gene Name
POFUT1
Sequence
GSWDPAGYLL YCPCMGRFGN QADHFLGSLA FAKLLNRTLA VPPWIEYQHH KPPFTNLHVS YQKYFKLEPL QAYHRVISLE DFMEKLAPTH WPPEKRVAYC FEVAAQRSPD KKTCPMKEGN PFGPFWDQFH VSFNKSELFT GISFSASYRE QWSQRFSPKE HPVLALPGAP AQFPVLEEHR PLQKYMVWSD EMVKTGEAQI HAHLVRPYVG IHLRIGSDWK NACAMLKDGT AGSHFMASPQ CVGYSRSTAA PLTMTMCLPD LKEIQRAVKL WVRSLDAQSV YVATDSESYV PELQQLFKGK VKVVSLKPEV AQVDLYILGQ ADHFIGNCVS SFTAFVKRER DLQGRPSSFF GMDRPPKLRD EF
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Form/Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Purity/Purification
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Preparation and Storage
Store at -20 degrees C. For long-term storage, store at -20 degrees C or -80 degrees C. Store working aliquots at 4 degrees C for up to one week. Repeated freezing and thawing is not recommended.
Molecular Weight
43,956 Da
Sequence Positions
27-388, Full length protein
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
3D Structure
ModBase 3D Structure for Q6EV69
Species
Pan troglodytes (Chimpanzee)
ISO Certification
Manufactured in an ISO 9001:2015 Certified Laboratory.

Other Notes

Small volumes of POFUT1 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Additional Details

NCBI/Uniprot data below describe general gene information for POFUT1. It may not necessarily be applicable to this product.

NCBI GI #
NCBI GeneID
NCBI Accession #
UniProt Primary Accession #
UniProt Related Accession #
GenBank Nucleotide #
NCBI Official Full Name
GDP-fucose protein O-fucosyltransferase 1
NCBI Official Synonym Full Names
protein O-fucosyltransferase 1
NCBI Official Symbol
POFUT1
NCBI Official Synonym Symbols
fut12
UniProt Protein Name
GDP-fucose protein O-fucosyltransferase 1
UniProt Synonym Protein Names
Peptide-O-fucosyltransferase 1; O-FucT-1
UniProt Gene Name
POFUT1
UniProt Synonym Gene Names
FUT12; O-FucT-1
NCBI Protein Information
GDP-fucose protein O-fucosyltransferase 1

UniProt Comments for POFUT1

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).
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Precautions

All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.

Disclaimer

While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.

Product Note

Select online data sheet information is drawn from bioinformatics databases, occasionally resulting in ambiguous or non-relevant product information. It is the responsibility of the customer to review, verify, and evaluate the information to make sure it matches their requirements before purchasing the kit. Our ELISA Kit assays are dynamic research tools and sometimes they may be updated and improved. If the format of this assay is important to you then please request the current manual or contact our technical support team with a presales inquiry before placing an order. We will confirm the current details of the assay. We cannot guarantee the sample manual posted online is the most current manual, it is intended to serve as an example only. Please refer to the instructions For Use provided with the assay kit for precise details.

Product PubMed Publications

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