protein

AGA/Aspartylglucosaminidase Protein, Human (HEK293, His)

HY-P76737

50 μg

510 USD

AGA/Aspartylglucosaminidase Protein, Human (HEK293, His)

proteins

HEK293

50 μg

510 USD

The AGA (aspartate glucosaminidase) protein plays a vital role in glycoprotein processing as an enzyme by cleaving the GlcNAc-Asn bond that connects the oligosaccharide to asparagine in the peptide chain of the glycoprotein. connect them. This cleavage represents the specificity of AGA in removing N-linked glycan structures from glycoproteins, a process necessary for the maturation and modification of these proteins. AGA/Aspartylglucosaminidase Protein, Human (HEK293, His) is the recombinant human-derived AGA/Aspartylglucosaminidase protein, expressed by HEK293 , with C-10*His labeled tag. The total length of AGA/Aspartylglucosaminidase Protein, Human (HEK293, His) is 323 a.a., with molecular weight of ~47 & 29 & 23 & 20 kDa, respectively.

Human

Aspartylglucosaminidase (AGA) is an enzyme that plays a crucial role in glycoprotein metabolism by cleaving the GlcNAc-Asn bond, which links oligosaccharides to the peptide moiety of asparagine-linked glycoproteins. This specific enzymatic activity enables AGA to participate in the degradation and processing of glycoproteins, contributing to the recycling and turnover of these molecules within the cell. The cleavage of the GlcNAc-Asn bond is a key step in the hydrolysis of glycoproteins, facilitating the release of oligosaccharides and peptides. While further research is needed to fully understand its physiological significance, AGA's role in glycoprotein catabolism underscores its importance in cellular processes related to protein turnover and recycling (

N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase; Glycosylasparaginase

Greater than 95% as determined by reducing SDS-PAGE

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.

Room temperature in continental US; may vary elsewhere.