LFNG Protein (AA 1-378) (Strep Tag)

N° du produit ABIN3131367

Détail du produit

Antigène: LFNG (LFNG O-Fucosylpeptide 3-beta-N-Acetylglucosaminyltransferase (LFNG))

Type de proteíne: Recombinant

Attributs du protein: AA 1-378

Origine: Souris

Source: Tobacco (Nicotiana tabacum)

Purification/Conjugué: Cette LFNG protéine est marqué à la Strep Tag.

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

Séquence: MLQRCGRRLL LALVGALLAC LLVLTADPPP TPMPAERGRR ALRSLAGSSG GAPASGSRAA VDPGVLTREV HSLSEYFSLL TRARRDADPP PGVASRQGDG HPRPPAEVLS PRDVFIAVKT TRKFHRARLD LLFETWISRH KEMTFIFTDG EDEALAKLTG NVVLTNCSSA HSRQALSCKM AVEYDRFIES GKKWFCHVDD DNYVNLRALL RLLASYPHTQ DVYIGKPSLD RPIQATERIS EHKVRPVHFW FATGGAGFCI SRGLALKMGP WASGGHFMST AERIRLPDDC TIGYIVEALL GVPLIRSGLF HSHLENLQQV PTTELHEQVT LSYGMFENKR NAVHIKGPFS VEADPSRFRS VHCHLYPDTP WCPRSAIF
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.

Attributs du produit: 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.

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

niveau d'endotoxine: Low Endotoxin less than 1 EU/mg (< 0.1 ng/mg)

Classe de qualité: Crystallography grade

Information d'application

Indications d'application: 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.

Commentaires:

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

Stockage

Format: Liquid

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

Conseil sur la manipulation: Avoid repeated freeze-thaw cycles.

Stock: -80 °C

Stockage commentaire: Store at -80°C.

Date de péremption: Unlimited (if stored properly)

Détail du antigène

Antigène: LFNG (LFNG O-Fucosylpeptide 3-beta-N-Acetylglucosaminyltransferase (LFNG))

Autre désignation: Lfng (LFNG Produits)

Synonymes: SCDO3 Protein, AW061165 Protein, id:ibd2614 Protein, id:ibd5029 Protein, id:ibd5138 Protein, l-fng Protein, wu:fc69h02 Protein, wu:fi34c01 Protein, LFNG O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase Protein, LFNG O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase S homeolog Protein, LFNG Protein, Lfng Protein, lfng.S Protein, lfng Protein

Sujet: Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe (EC 2.4.1.222) (O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase),FUNCTION: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules (PubMed:10935626). Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG1 and enhancement of NOTCH1 activation by DLL1 via an increase in its binding to DLL1 (PubMed:28089369, PubMed:16385447). Decreases the binding of JAG1 to NOTCH2 but not that of DLL1 (By similarity). Essential mediator of somite segmentation and patterning. During somite boundary formation, it restricts Notch activity in the presomitic mesoderm to a boundary-forming territory in the posterior half of the prospective somite. In this region, Notch function activates a set of genes that are involved in boundary formation and in anterior-posterior somite identity (PubMed:10330372). Ectopically expressed in the thymus, Lfgn inhibits Notch signaling which results in inhibition of T-cell commitment and promotes B-cell development in lymphoid progenitors (PubMed:11520458). May play a role in boundary formation of the enamel knot (PubMed:12167404). {ECO:0000250|UniProtKB:Q8NES3, ECO:0000269|PubMed:10330372, ECO:0000269|PubMed:10935626, ECO:0000269|PubMed:11520458, ECO:0000269|PubMed:12167404, ECO:0000269|PubMed:16385447, ECO:0000269|PubMed:28089369}.

Poids moléculaire: 42.0 kDa

UniProt: O09010

Pathways: Signalisation Notch