GALNT11 Protein (AA 1-608) (Strep Tag)

Catalog No. ABIN3116652

Product Details

Target: GALNT11 (UDP-N-Acetyl-alpha-D-Galactosamine:polypeptide N-Acetylgalactosaminyltransferase 11 (GalNAc-T11) (GALNT11))

Protein Type: Recombinant

Protein Characteristics: AA 1-608

Origin: Human

Source: Tobacco (Nicotiana tabacum)

Purification tag / Conjugate: This GALNT11 protein is labelled with Strep Tag.

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

Sequence: MGSVTVRYFC YGCLFTSATW TVLLFVYFNF SEVTQPLKNV PVKGSGPHGP SPKKFYPRFT RGPSRVLEPQ FKANKIDDVI DSRVEDPEEG HLKFSSELGM IFNERDQELR DLGYQKHAFN MLISDRLGYH RDVPDTRNAA CKEKFYPPDL PAASVVICFY NEAFSALLRT VHSVIDRTPA HLLHEIILVD DDSDFDDLKG ELDEYVQKYL PGKIKVIRNT KREGLIRGRM IGAAHATGEV LVFLDSHCEV NVMWLQPLLA AIREDRHTVV CPVIDIISAD TLAYSSSPVV RGGFNWGLHF KWDLVPLSEL GRAEGATAPI KSPTMAGGLF AMNRQYFHEL GQYDSGMDIW GGENLEISFR IWMCGGKLFI IPCSRVGHIF RKRRPYGSPE GQDTMTHNSL RLAHVWLDEY KEQYFSLRPD LKTKSYGNIS ERVELRKKLG CKSFKWYLDN VYPEMQISGS HAKPQQPIFV NRGPKRPKVL QRGRLYHLQT NKCLVAQGRP SQKGGLVVLK ACDYSDPNQI WIYNEEHELV LNSLLCLDMS ETRSSDPPRL MKCHGSGGSQ QWTFGKNNRL YQVSVGQCLR AVDPLGQKGS VAMAICDGSS SQQWHLEG
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: GALNT11 (UDP-N-Acetyl-alpha-D-Galactosamine:polypeptide N-Acetylgalactosaminyltransferase 11 (GalNAc-T11) (GALNT11))

Alternative Name: GALNT11 (GALNT11 Products)

Synonyms: A430075I06Rik Protein, AI648252 Protein, E430002F06Rik Protein, GALNACT11 Protein, polypeptide N-acetylgalactosaminyltransferase 11 Protein, Galnt11 Protein, GALNT11 Protein

Background: Polypeptide N-acetylgalactosaminyltransferase 11 (EC 2.4.1.41) (Polypeptide GalNAc transferase 11) (GalNAc-T11) (pp-GaNTase 11) (Protein-UDP acetylgalactosaminyltransferase 11) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11),FUNCTION: Polypeptide N-acetylgalactosaminyltransferase that catalyzes the initiation of protein O-linked glycosylation and is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes activation of NOTCH1, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). Polypeptide N-acetylgalactosaminyltransferases catalyze the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Displays the same enzyme activity toward MUC1, MUC4, and EA2 than GALNT1. Not involved in glycosylation of erythropoietin (EPO). {ECO:0000269|PubMed:11925450, ECO:0000269|PubMed:24226769}.

Molecular Weight: 68.9 kDa

UniProt: Q8NCW6