SIAT4A (ST3GAL1) (NM_003033) Human Mass Spec Standard

CAT#: PH317696

ST3GAL1 MS Standard C13 and N15-labeled recombinant protein (NP_003024)


  View other "SIAT4A" proteins (5)

USD 3,255.00

3 Weeks*

Size
    • 10 ug

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Frequently bought together (2)
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Transient overexpression lysate of ST3 beta-galactoside alpha-2,3-sialyltransferase 1 (ST3GAL1), transcript variant 2
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Other products for "SIAT4A"

Specifications

Product Data
Tag C-Myc/DDK
Species Human
Expression Host HEK293
Expression cDNA Clone or AA Sequence RC217696
Predicted MW 39.1 kDa
Protein Sequence
Purity > 80% as determined by SDS-PAGE and Coomassie blue staining
Concentration >0.05 µg/µL as determined by microplate BCA method
Labeling Method Labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine
Buffer 25 mM Tris-HCl, 100 mM glycine, pH 7.3
Storage Store at -80°C. Avoid repeated freeze-thaw cycles.
Stability Stable for 3 months from receipt of products under proper storage and handling conditions.
Reference Data
RefSeq NP_003024
RefSeq Size 6971
RefSeq ORF 1020
Synonyms 1; Gal-NAc6S; SIAT4A; SIATFL; ST3GalA; ST3GalA.1; ST3GalIA; ST3O
Locus ID 6482
UniProt ID Q11201, A0A024R9L6
Cytogenetics 8q24.22
Summary The protein encoded by this gene is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The encoded protein is normally found in the Golgi but can be proteolytically processed to a soluble form. Correct glycosylation of the encoded protein may be critical to its sialyltransferase activity. This protein, which is a member of glycosyltransferase family 29, can use the same acceptor substrates as does sialyltransferase 4B. Two transcript variants encoding the same protein have been found for this gene. Other transcript variants may exist, but have not been fully characterized yet. [provided by RefSeq, Jul 2008]
Protein Families Secreted Protein, Transmembrane
Protein Pathways Glycosphingolipid biosynthesis - ganglio series, Glycosphingolipid biosynthesis - globo series, Keratan sulfate biosynthesis, Metabolic pathways, O-Glycan biosynthesis

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