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Human FUT7 Recombinant Protein (N-His) (HD175012)

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概要
カタログ番号HD175012
説明
Recombinant Human FUT7 Protein, N-His (HD175012) expressed in E. coli, spanning Pro37-Ala342. Purity: >90% by SDS-PAGE.
Highlights
  • ●His-Tagged — N-terminal 6×His tag for IMAC purification.
  • ●E. coli Expression — High-yield, cost-effective production.
  • ●High Purity — >90% purity verified by SDS-PAGE.
発現システムE. coli
アクセッション番号Q11130
タンパク質長Pro37-Ala342
アプリケーションELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
種Homo sapiens (Human)
性質 Recombinant
エンドトキシンレベル Please contact with the lab for this information.
純度 >90% as determined by SDS-PAGE.
予測分子量 37.81 kDa
形態 Lyophilized
保存バッファー Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.

データシートのハードコピーまたはロット固有のCOAに記載された具体的なバッファー情報を参照してください。

再構成 Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
発送 In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
安定性と保存 Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
別名Alpha-(1,3)-fucosyltransferase 7, EC:2.4.1.-, FUT7, Fuc-TVII, FucT-VII, Fucosyltransferase 7, Fucosyltransferase VII, Galactoside 3-L-fucosyltransferase, Selectin ligand synthase
背景

Alpha-(1,3)-fucosyltransferase 7 is a ~39 kDa protein. 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. In vitro, also synthesizes sialyl-dimeric-Lex structures, from VIM-2 structures and both di-fucosylated and trifucosylated structures from mono-fucosylated precursors. 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. 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. 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.

1. Bengtson, P. et al. (2001) The Journal of biological chemistry 276, 31575-82. PMID: 11404359
2. Miyashiro, M. et al. (2004) Journal of biochemistry 136, 723-31. PMID: 15632313
3. Prorok-Hamon, M. et al. (2005) The Biochemical journal 391, 491-502. PMID: 15926890
4. Zhang, Y. et al. (2009) Fertility and sterility 91, 908-14. PMID: 18402946
5. Liu, S. et al. (2008) IUBMB life 60, 461-6. PMID: 18553500
6. Mondal, N. et al. (2018) The Journal of biological chemistry 293, 7300-7314. PMID: 29593094
7. Natsuka, S. et al. (1994) The Journal of biological chemistry 269, 16789-94. PMID: 8207002
8. Knibbs, RN. et al. (1996) The Journal of cell biology 133, 911-20. PMID: 8666674
9. Malý, P. et al. (1996) Cell 86, 643-53. PMID: 8752218
10. Stroud, MR. et al. (1997) Biochemical and biophysical research communications 238, 165-8. PMID: 9299472
注意事項 For research use only
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参考文献
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