alpha-N-Acetylgalactosaminide alpha-2,6-Sialyltransferase 3 (SIA7C) (AA 1-305) protein (Strep Tag)
Quick Overview for alpha-N-Acetylgalactosaminide alpha-2,6-Sialyltransferase 3 (SIA7C) (AA 1-305) protein (Strep Tag) (ABIN3103682)
Target
See all alpha-N-Acetylgalactosaminide alpha-2,6-Sialyltransferase 3 (SIA7C) ProteinsProtein Type
Origin
Source
Application
Purity
Grade
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Protein Characteristics
- AA 1-305
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Purification tag / Conjugate
- Strep Tag
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Sequence
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MACILKRKSV IAVSFIAAFL FLLVVRLVNE VNFPLLLNCF GQPGTKWIPF SYTYRRPLRT HYGYINVKTQ EPLQLDCDLC AIVSNSGQMV GQKVGNEIDR SSCIWRMNNA PTKGYEEDVG RMTMIRVVSH TSVPLLLKNP DYFFKEANTT IYVIWGPFRN MRKDGNGIVY NMLKKTVGIY PNAQIYVTTE KRMSYCDGVF KKETGKDRVQ SGSYLSTGWF TFLLAMDACY GIHVYGMIND TYCKTEGYRK VPYHYYEQGR DECDEYFLHE HAPYGGHRFI TEKKVFAKWA KKHRIIFTHP NWTLS
Sequence without tag. The proposed Strep-Tag is based on experience with the expression system. Our team may suggest an additional tag depending on the complexity of the protein. If 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 in one-step affinity chromatography
- State-of-the-art algorithm used for plasmid design (Gene synthesis).
This protein is a predefined custom protein and will be made for the first time for your order. Our experts in the lab try to ensure that you receive soluble protein.
The big advantage of ordering our predefined custom 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 against its specific reference buffer.
- We use the Expasy's ProtParam tool to determine the absorption coefficient of each protein.
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Purification
- One-step Strep-tag purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®).
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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.
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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
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Buffer
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The buffer composition is at the discretion of the manufacturer.
Standard Storage Buffer: PBS pH 7.4, 10 % Glycerol Might differ depending on protein. -
Handling Advice
- Avoid repeated freeze-thaw cycles.
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Storage
- -80 °C
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Storage Comment
- Store at -80°C.
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Expiry Date
- 12 months
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- alpha-N-Acetylgalactosaminide alpha-2,6-Sialyltransferase 3 (SIA7C)
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Alternative Name
- ST6GALNAC3
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Background
- Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 3 (EC 2.4.3.7) (GalNAc alpha-2,6-sialyltransferase III) (ST6GalNAc III) (ST6GalNAcIII) (STY) (Sialyltransferase 7C) (SIAT7-C),FUNCTION: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the GalNAc residue on the NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc sequence of glycoproteins and glycolipids forming an alpha-2,6-linkage. Produces branched type disialyl structures by transfer of a sialyl group onto a GalNAc residue inside the backbone core chains. ST6GalNAcIII prefers glycolipids to glycoproteins, predominantly catalyzing the biosynthesis of ganglioside GD1alpha from GM1b (PubMed:16169874, PubMed:17123352). GD1alpha is a critical molecule in the communication and interaction between neuronal cells and their supportive cells, particularly in brain tissues, and functions as an adhesion molecule in the process of metastasis (By similarity). Sialylation of glycoproteins or glycosphingolipids is very important in tumor development, neuronal development, nerve repair, immunological processes and regulation of hormone sensitivity (PubMed:17123352). {ECO:0000250|UniProtKB:Q9QYJ1, ECO:0000269|PubMed:16169874, ECO:0000269|PubMed:17123352}.
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Molecular Weight
- 35.4 kDa
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UniProt
- Q8NDV1
Target
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