FUT7 Protein (AA 1-389) (Strep Tag)

Catalog No. ABIN3121595

Product Details

Target: FUT7 (Fucosyltransferase 7 (Alpha (1,3) Fucosyltransferase) (FUT7))

Protein Type: Recombinant

Protein Characteristics: AA 1-389

Origin: Mouse

Source: Tobacco (Nicotiana tabacum)

Purification tag / Conjugate: This FUT7 protein is labelled with Strep Tag.

Application: ELISA, Western Blotting (WB), SDS-PAGE (SDS)

Sequence: MPTPCPPACL STPGTHRLLP FPDWKAPSWE SRKEATCNSS SPGPWAEPTV QGYHPTRRLR AWGGLAGGAT FMVIWFFWLW GSAPGSAPVP QSTLTILIWH WPFTNRPPEL PGDTCTRYGM ASCRLSANRS LLASADAVVF HHRELQTRQS LLPLDQRPHG QPWVWASMES PSNTHGLHRF RGIFNWVLSY RRDSDIFVPY GRLEPLSGPT SPLPAKSRMA AWVISNFQER QQRAKLYRQL APHLQVDVFG RASGRPLCAN CLLPTLARYR FYLAFENSQH RDYITEKFWR NALAAGAVPV ALGPPRATYE AFVPPDAFVH VDDFSSAREL AVFLVSMNES RYRGFFAWRD RLRVRLLGDW RERFCTICAR YPYLPRSQVY EDLESWFQA
Sequence without tag. The proposed Strep-Tag is based on experience s with the expression system, a different complexity of the protein could make another tag necessary. In case you have a special request, please contact us.

Characteristics: Key Benefits:

• Made in Germany - from design to production - by highly experienced protein experts.
• Protein expressed with ALiCE® and purified by multi-step, protein-specific process to ensure correct folding and modification.
• These proteins are normally active (enzymatically functional) as our customers have reported (not tested by us and not guaranteed).
• State-of-the-art algorithm used for plasmid design (Gene synthesis).

This protein is a made-to-order protein and will be made for the first time for your order. Our experts in the lab will ensure that you receive a correctly folded protein.

The big advantage of ordering our made-to-order proteins in comparison to ordering custom made proteins from other companies is that there is no financial obligation in case the protein cannot be expressed or purified.

Expression System:

• ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
• During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein!

Concentration:

• The concentration of our recombinant proteins is measured using the absorbance at 280nm.
• The protein's absorbance will be measured in several dilutions and is measured against its specific reference buffer.
• We use the Expasy's protparam tool to determine the absorption coefficient of each protein.

Purification: Two step purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®):

1. In a first purification step, the protein is purified from the cleared cell lysate using StrepTag capture material. Eluate fractions are analyzed by SDS-PAGE.
2. Protein containing fractions of the best purification are subjected to second purification step through size exclusion chromatography. Eluate fractions are analyzed by SDS-PAGE and Western blot.

Purity: ≥ 80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.

Endotoxin Level: Low Endotoxin less than 1 EU/mg (< 0.1 ng/mg)

Grade: Crystallography grade

Application Details

Application Notes: In addition to the applications listed above we expect the protein to work for functional studies as well. As the protein has not been tested for functional studies yet we cannot offer a guarantee though.

Comment:

ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein!

Restrictions: For Research Use only

Handling

Format: Liquid

Buffer: The buffer composition is at the discretion of the manufacturer. If you have a special request, please contact us.

Handling Advice: Avoid repeated freeze-thaw cycles.

Storage: -80 °C

Storage Comment: Store at -80°C.

Expiry Date: Unlimited (if stored properly)

Target Details

Target: FUT7 (Fucosyltransferase 7 (Alpha (1,3) Fucosyltransferase) (FUT7))

Alternative Name: Fut7 (FUT7 Products)

Synonyms: FCT3A Protein, FT1A Protein, Fuc-TVI Protein, FucT-VI Protein, zgc:152705 Protein, fuct-vii Protein, CFTII Protein, FucT-VII Protein, AI853193 Protein, FTVII Protein, Fuc-TVII Protein, fucosyltransferase 6 Protein, fucosyltransferase 7 Protein, fucosyltransferase 7 (alpha (1,3) fucosyltransferase) Protein, FUT6 Protein, FUT7 Protein, fut7 Protein, Fut7 Protein

Background: Alpha-(1,3)-fucosyltransferase 7 (EC 2.4.1.-) (Fucosyltransferase 7) (Fucosyltransferase VII) (Fuc-TVII) (FucT-VII) (Galactoside 3-L-fucosyltransferase),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:8752218, PubMed:8626519, PubMed:15843584, PubMed:10882744, PubMed:11535629, PubMed:12359718, PubMed:11485743). In vitro, also synthesizes sialyl-dimeric-Lex structures, from VIM-2 structures and both di-fucosylated and trifucosylated structures from mono-fucosylated precursors (By similarity). 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 (By similarity). 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:8752218, PubMed:10894166). 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:15843584, PubMed:8752218, PubMed:10882744, PubMed:11535629). May enhance embryo implantation through sialyl Lewis X (sLeX)-mediated adhesion of embryo cells to endometrium (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:Q11130, ECO:0000269|PubMed:10882744, ECO:0000269|PubMed:10894166, ECO:0000269|PubMed:11535629, ECO:0000269|PubMed:12359718, ECO:0000269|PubMed:15843584, ECO:0000269|PubMed:8626519, ECO:0000269|PubMed:8752218}.

Molecular Weight: 44.5 kDa

UniProt: Q11131