Recombinant Human Polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1), partial

Code CSB-YP607410HU
MSDS
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Source Yeast
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Code CSB-EP607410HU
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Source E.coli
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Code CSB-EP607410HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP607410HU
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Source Baculovirus
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Code CSB-MP607410HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
GALNT1
Uniprot No.
Alternative Names
GALNAC T1; GalNAc transferase 1; GalNAc-T1; GALNT 1; GALNT1; GALT1_HUMAN; Polypeptide GalNAc transferase 1; Polypeptide N acetylgalactosaminyltransferase 1; Polypeptide N-acetylgalactosaminyltransferase 1 soluble form; pp GaNTase 1; pp-GaNTase 1; Protein UDP acetylgalactosaminyltransferase 1; Protein-UDP acetylgalactosaminyltransferase 1; UDP GalNAc:polypeptide N acetylgalactosaminyltransferase 1; UDP N acetyl alpha D galactosamine:polypeptide N acetylgalactosaminyltransferase 1 (GalNAc T1); UDP N acetyl alpha D galactosamine:polypeptide N acetylgalactosaminyltransferase 1; UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1
Species
Homo sapiens (Human)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

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 a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7.
Gene References into Functions
  1. We have elucidated a novel miR-30-GALNT1/2 axis whose dysregulation increases the proportion of inactive proBNP secreted by the heart and impairs the compensatory actions of BNP during the progression of heart failure. PMID: 28188250
  2. the GalNAc-T13 isoform is predicted to function similarly to GalNAc-T1 against peptide substrates in vivo, in contrast to a prior report, but is unique by being selectively expressed in the brain. PMID: 27913570
  3. Expression of GALNT3 was reduced in CAD patients, and down regulation of GALNT3 contributed to endothelial injury by promoting apoptosis and up-regulating the expression of MMP-2 and MMP-14 genes via p38 MAPK activation. PMID: 26714046
  4. appears to be responsive to the inhibition of GALNT1 and SHH signaling PMID: 26676748
  5. Study demonstrates that down-regulation of GALNT1 is sufficient to suppress malignant phenotype of HCC cells by decreasing EGFR signaling. PMID: 25730904
  6. High ppGalNAc T1 expresdsion is associated with bladder cancer. PMID: 23317233
  7. The GALNT1 is the glycosyltransferase enzyme family covering a single known glycosidic linkage. PMID: 22183981
  8. Utilizing unnatural glycopeptide substrates for GalNAc-T3 we demonstrated that the GalNAc-specific sugar recognition of the lectin domain regulates further glycosylation. PMID: 22042768
  9. each ppGalNAc T isoform may be uniquely sensitive to peptide sequence and overall charge, which together dictates the substrate sites that will be glycosylated PMID: 21349845
  10. Growth factor stimulation regulates O-glycosylation initiation in a Src-dependent fashion by GalNac-T redistribution from golgi to the endoplasmic reticulum. PMID: 20498016
  11. the present analysis fails to replicate an earlier reported association of a GALNT1 variant with risk of ovarian cancer PMID: 20142253
  12. First simultaneous kinetic description of O-glycosylation events by recombinant UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase I at all putative O-glycosylation sites within human mucin MUC1 containing 5 tandem repeats. PMID: 14636048
  13. The results indicated that IL-4-treated LS174T cells are able to produce mucins with a higher degree of O-glycosylation than untreated counterparts. PMID: 17916404
  14. GalNAc T10 has a large and pronounced glycopeptide preference for Ser/Thr-O-GalNAc only at the +1 position from the acceptor site, whereas T1 and T2 have significantly reduced and variable preferences for Ser/Thr-O-GalNAc. PMID: 19460755
  15. A direct link between miR-129 and the two putative targets GALNT1 and SOX4 in bladder cancer. PMID: 19487295
  16. Data show that the sequences and O-glycosylation patterns direct the addition of the first and second sugar residues by ppGalNAc-T and C1GalT which act in a site directed fashion. PMID: 19524017

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Subcellular Location
[Polypeptide N-acetylgalactosaminyltransferase 1]: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein.; [Polypeptide N-acetylgalactosaminyltransferase 1 soluble form]: Secreted.
Protein Families
Glycosyltransferase 2 family, GalNAc-T subfamily
Tissue Specificity
Widely expressed. Expressed in all tissues tested.
Database Links

HGNC: 4123

OMIM: 602273

KEGG: hsa:2589

STRING: 9606.ENSP00000269195

UniGene: Hs.514806

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