GALNT12 Protein (AA 1-576) (Strep Tag)
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- Target See all GALNT12 Proteins
- GALNT12 (UDP-N-Acetyl-alpha-D-Galactosamine:polypeptide N-Acetylgalactosaminyltransferase 12 (GalNAc-T12) (GALNT12))
- Protein Type
- Recombinant
- Protein Characteristics
- AA 1-576
- Origin
- Mouse
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Source
- Tobacco (Nicotiana tabacum)
- Purification tag / Conjugate
- This GALNT12 protein is labelled with Strep Tag.
- Application
- ELISA, Western Blotting (WB), SDS-PAGE (SDS)
- Sequence
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MWGRAVRRRC PRGLRRGREA LLALLALAGL GALLRARSRS GTVDPGPPRT PLPGRHEPVL PRPPLPADAL GAHGEAVRLQ LQGEELRLQE ESVKQHQINI YLSDRISLHR RLPERWNPLC REVKYDYDNL PKTSVVIAFY NEAWSTLLRT VYSVLETSPD ILLEEVILVD DYSDREHLKE RLANELSQLP KVRLIRASRR EGLVRARLLG ASAARGEVLT FLDCHCECHE GWLEPLLQRI HEKESAVVCP VIDVIDWNTF EYLGNSGEPQ IGGFDWRLVF TWHVVPQRER QSMRSPIDVI RSPTMAGGLF AVSKRYFDYL GSYDTGMEVW GGENLEFSFR IWQCGGTLET HPCSHVGHVF PKQAPYSRSK ALANSVRAAE VWMDEFKELY YHRNPQARLE PFGDVTERKK LRAKLQCKDF KWFLDTVYPE LHVPEDRPGF FGMLQNRGLR GYCLDYNPPN ENHVEGHQVL LYLCHGMGQN QFFEYTTRKE IRYNTRQPEA CITVEDGKDT LVMDLCRETV PENQEFILQE DGTLVHKHSR KCVEATEKVL DNGFAPYLRD CTNSDNQRWF FKERMS
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
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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
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Two step purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®):
- 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.
- 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)
- Top Product
- Discover our top product GALNT12 Protein
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- 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
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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
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- 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)
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- Target
- GALNT12 (UDP-N-Acetyl-alpha-D-Galactosamine:polypeptide N-Acetylgalactosaminyltransferase 12 (GalNAc-T12) (GALNT12))
- Alternative Name
- Galnt12 (GALNT12 Products)
- Synonyms
- 9130206E10 Protein, A630062B03Rik Protein, CRCS1 Protein, GalNAc-T12 Protein, polypeptide N-acetylgalactosaminyltransferase 12 Protein, Galnt12 Protein, GALNT12 Protein
- Background
- Polypeptide N-acetylgalactosaminyltransferase 12 (EC 2.4.1.41) (Polypeptide GalNAc transferase 12) (GalNAc-T12) (pp-GaNTase 12) (Protein-UDP acetylgalactosaminyltransferase 12) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12),FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward non-glycosylated peptides such as Muc5AC, Muc1a and EA2, and no detectable activity with Muc2 and Muc7. Displays enzymatic activity toward the Gal-NAc-Muc5AC glycopeptide, but no detectable activity to mono-GalNAc-glycosylated Muc1a, Muc2, Muc7 and EA2. May play an important role in the initial step of mucin-type oligosaccharide biosynthesis in digestive organs (By similarity). {ECO:0000250}.
- Molecular Weight
- 66.5 kDa
- UniProt
- Q8BGT9
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