Recombinant Human N (AGA) Protein (His-SUMO)
Beta LifeScience
SKU/CAT #: BLC-09876P

Greater than 90% as determined by SDS-PAGE.
Recombinant Human N (AGA) Protein (His-SUMO)
Beta LifeScience
SKU/CAT #: BLC-09876P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.
Product Overview
Description | Recombinant Human N (AGA) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment. |
Purity | Greater than 90% as determined by SDS-PAGE. |
Uniprotkb | P20933 |
Target Symbol | AGA |
Synonyms | Aga; AGU; Aspartylglucosaminidase; Aspartylglucosylamine deaspartylase; Aspartylglycosaminuria; ASPG_HUMAN; ASRG; GA; Glycosylasparaginase; Glycosylasparaginase beta chain; N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase; N4 (N acetyl beta glucosaminyl) L asparagine amidase; N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase |
Species | Homo sapiens (Human) |
Expression System | E.coli |
Tag | N-6His-SUMO |
Target Protein Sequence | SSPLPLVVNTWPFKNATEAAWRALASGGSALDAVESGCAMCEREQCDGSVGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAIGVARKVLEHTTHTLLVGESATTFAQSMGFINEDLSTTASQALHSDWLARNCQPNYWRNVIPDPSKYCGPYKPPGILKQDIPIHKETEDDRGHD |
Expression Range | 24-205aa |
Protein Length | Partial |
Mol. Weight | 35.6kDa |
Research Area | Signal Transduction |
Form | Liquid or Lyophilized powder |
Buffer | Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. |
Reconstitution | Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%. |
Storage | 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C. |
Notes | Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week. |
Target Details
Target Function | Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins. |
Subcellular Location | Lysosome. |
Protein Families | Ntn-hydrolase family |
Database References | |
Associated Diseases | Aspartylglucosaminuria (AGU) |
Gene Functions References
- 1.8A resolution crystal structure of mature G172D mutant of a model missense GA corresponding to a Canadian aspartylglucosaminuria allele; studied the effect of its single amino acid change on substrate processing PMID: 28457719
- We show that gene-silenced cells show specifically reduced AGA activity and store globotriaosylceramide. In gene-silenced cells, release of the neurotransmitter acetylcholine is significantly reduced, demonstrating that this model may be used to study specific neuronal functions such as neurotransmitter release in Fabry disease PMID: 27471012
- study reports 2 novel aspartylglucosaminidase gene mutations, one in Qatari twins with an early, perinatal presentation not previously described for aspartylglucosaminuria and the other in 3 Turkish children with newly diagnosed aspartylglucosaminuria and a more classical disease course PMID: 23271757
- [review] Natural killer (NK) cell tumors, subtypes of myeloid leukemias and T-cell lymphomas respond to ASNase; ovarian carcinomas and other solid tumors have been proposed as additional targets for ASNase, with a potential role for glutaminase. activity. PMID: 21854356
- Molecular mechanism for the autoproteolytic activation of aspartylglucosaminidase. PMID: 14616088
- A new point mutation, c.44T>G, found in a Finnish compound heterozygote causes a L15R AA substitution in the signal sequence of the AGA enzyme, affecting AGA translocation by altering a critical hydrophobic core structure in the signal sequence. PMID: 15365992
- aspartylglucosaminidase may have a role in development of congenital disorders of glycosylation type I PMID: 16435229
- The amino acid substitutions in aspartylglucosaminidase responsible for aspartylglucosaminuria were classified and divided in three groups. PMID: 18992224
- Increased AGA plasma activity, although a consistent finding in congenital disorders of glycosylation patients, is not specific to this group of disorders. PMID: 19100247