protein

O-GlcNAcase/OGA Protein, B. thetaiotaomicron (His)

HY-P79242

5 μg;10 μg;50 μg;100 μg

135;230;650;1105 USD

O-GlcNAcase/OGA Protein, B. thetaiotaomicron (His)

proteins

E. coli

5 μg;10 μg;50 μg;100 μg

135;230;650;1105 USD

O-GlcNAcase (OGA) is an enzyme responsible for the hydrolysis of glycosidic bonds in O-GlcNA acylated proteins. It exhibits its enzymatic activity in vitro by efficiently utilizing substrates such as p-nitrophenyl-β-GlcNAc and 4-methylumbelliferone-GlcNAc. O-GlcNAcase/OGA Protein, B. thetaiotaomicron (His) is the recombinant O-GlcNAcase/OGA protein, expressed by E. coli , with N-6*His labeled tag. The total length of O-GlcNAcase/OGA Protein, B. thetaiotaomicron (His) is 716 a.a., with molecular weight of 80-95 kDa.

Others

O-GlcNAcase (OGA) is an enzyme responsible for the hydrolysis of the glycosidic link in O-GlcNAcylated proteins. It exhibits its enzymatic activity in vitro by efficiently utilizing substrates like p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc. OGA plays a crucial role in regulating O-GlcNAcylation, a post-translational modification that involves the attachment of N-acetylglucosamine (GlcNAc) to serine or threonine residues of proteins. By catalyzing the removal of O-GlcNAc groups, OGA contributes to the dynamic control of O-GlcNAcylation levels, thereby influencing various cellular processes such as signal transduction, gene expression, and protein stability. Further investigation is necessary to fully comprehend the complex regulatory mechanisms and physiological significance of OGA in cellular functions and disease pathways.

O-GlcNAcase BT_4395; Beta-N-acetylglucosaminidase; Beta-N-acetylhexosaminidase; Beta-hexosaminidase; Hexosaminidase B; N-acetyl-beta-glucosaminidase

Greater than 95% as determined by reducing SDS-PAGE

Lyophilized from a 0.2 μm filtered solution of 50 mM Tris-HCL, 300 mM NaCl, pH 7.4.

Room temperature in continental US; may vary elsewhere.