Recombinant Human FUT7 protein (denatured) (His tag N-Terminus)
Be the first to review this product! Submit a review
|
(0 Publication)
Recombinant Human FUT7 protein (denatured) (His tag N-Terminus) is a Human Fragment protein, in the 37 to 342 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE.
View Alternative Names
Fucosyltransferase 7, Fucosyltransferase VII, Galactoside 3-L-fucosyltransferase, Selectin ligand synthase, Fuc-TVII, FucT-VII, FUT7
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human FUT7 protein (denatured) (His tag N-Terminus) (AB180311)
15% SDS-PAGE analysis of ab180311 (3 μg).
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
FUT7 is critical in mediating cell-cell interaction during the immune response. Its enzymatic activity facilitates leukocyte rolling and adhesion essential processes during inflammation and immune surveillance. FUT7 does not operate as part of a multi-protein complex relying instead on its ability to modify glycoproteins and glycolipids on the cell surface. These modifications are important for proper immune cell function.
Pathways
FUT7 involves directly in the selectin-mediated cell adhesion pathway. This function integrates it into the broader context of leukocyte migration a process important in immune responses. The pathway often includes interactions with proteins such as L-selectin or E-selectin both of which recognize and bind to sialyl Lewis X the product of FUT7's enzymatic activity. This pathway helps ensure leukocytes reach sites of infection or injury efficiently.
Specifications
Form
Liquid
General info
Function
Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a distal alpha2,3 sialylated lactosamine unit of a glycoprotein or a glycolipid-linked sialopolylactosamines chain through an alpha-1,3 glycosidic linkage and participates in the final fucosylation step in the biosynthesis of the sialyl Lewis X (sLe(x)), a carbohydrate involved in cell and matrix adhesion during leukocyte trafficking and fertilization (PubMed : 11404359, PubMed : 15632313, PubMed : 15926890, PubMed : 18402946, PubMed : 18553500, PubMed : 29593094, PubMed : 8207002, PubMed : 8666674, PubMed : 8752218, PubMed : 9299472, PubMed : 9405391, PubMed : 9461592, PubMed : 9473504, PubMed : 9499379). In vitro, also synthesizes sialyl-dimeric-Lex structures, from VIM-2 structures and both di-fucosylated and trifucosylated structures from mono-fucosylated precursors (PubMed : 9499379). However does not catalyze alpha 1-3 fucosylation when an internal alpha 1-3 fucosylation is present in polylactosamine chain and the fucosylation rate of the internal GlcNAc residues is reduced once fucose has been added to the distal GlcNAc (PubMed : 9473504, PubMed : 9499379). Also catalyzes the transfer of a fucose from GDP-beta-fucose to the 6-sulfated a(2,3)sialylated substrate to produce 6-sulfo sLex mediating significant L-selectin-dependent cell adhesion (PubMed : 10200296, PubMed : 8752218). Through sialyl-Lewis(x) biosynthesis, can control SELE- and SELP-mediated cell adhesion with leukocytes and allows leukocytes tethering and rolling along the endothelial tissue thereby enabling the leukocytes to accumulate at a site of inflammation (PubMed : 10386892, PubMed : 29138114, PubMed : 8666674, PubMed : 9473504, PubMed : 9834120). May enhance embryo implantation through sialyl Lewis X (sLeX)-mediated adhesion of embryo cells to endometrium (PubMed : 18402946, PubMed : 18553500). May affect insulin signaling by up-regulating the phosphorylation and expression of some signaling molecules involved in the insulin-signaling pathway through SLe(x) which is present on the glycans of the INSRR alpha subunit (PubMed : 17229154).
Sequence similarities
Belongs to the glycosyltransferase 10 family.
Post-translational modifications
N-glycosylated.
Target data
Complementary Products
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com