B3GALTL Protein (His Tag)

03.05.2013

Sino Biological Inc. liefert B3GALTL Protein (His Tag) mit höherer Qualität und günstiger Kosten im Vergleich mit anderen globalen Lieferanten.

Weitere Informationen über B3GALTL Protein (His Tag) lesen Sie bitte: http://www.sinobiological.com/B3GALTL-Protein-Antibody-a-5907.html

Produkt-Information von B3GALTL Protein

Synonym	B3GALTL, B3GTL
Protein Construction	A DNA sequence encoding the human B3GALTL (Ser29-Phe494) was expressed with an N-terminal polyhistidine tag.
Source	Human
Expression Host	Human Cells

QC Testing von B3GALTL Protein

Purity	> 95 % as determined by SDS-PAGE	SDS-PAGE: B3GALTL protein
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Stability	Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N terminal	His
Molecular Mass	The recombinant human B3GALTL comprises 486 amino acids and has a predicted molecular mass of 55.4 kDa. The apparent molecular mass of the protein is approximately 54 kDa in SDS-PAGE under reducing conditions due to glycosylation.
Formulation	Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA. Please contact us for any concerns or special requirements.

Usage Guide von B3GALTL Protein

Storage	Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution	A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

Beschreibung von B3GALTL Protein

B3GALTL is a beta-1,3-glucosyltransferase that transfers glucose to O-linked fucosylglycans on thrombospondin type-1 repeats (TSRs) of several proteins. B3GALTL is a type II membrane protein. Defects in B3GALTL gene are a cause of Peters-plus syndrome (PPS). As an O-fucosyltransferase, B3GALTL transfers glucose toward fucose with a beta-1,3 linkage. It specifically glucosylates O-linked fucosylglycan on TSP type-1 domains of proteins, thereby contributing to elongation of O-fucosylglycan.

References

Heinonen TY. et al., 2003, Biochem Biophys Res Commun. 309 (1): 166-74.
Sato T. et al., 2006, Glycobiology. 16 (12): 1194-206.
Kozma K. et al., 2006, J Biol Chem. 281 (48): 36742-51.