Recombinant Human N (AGA) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-09876P
Greater than 90% as determined by SDS-PAGE.
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. 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
  2. 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
  3. 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
  4. [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
  5. Molecular mechanism for the autoproteolytic activation of aspartylglucosaminidase. PMID: 14616088
  6. 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
  7. aspartylglucosaminidase may have a role in development of congenital disorders of glycosylation type I PMID: 16435229
  8. The amino acid substitutions in aspartylglucosaminidase responsible for aspartylglucosaminuria were classified and divided in three groups. PMID: 18992224
  9. Increased AGA plasma activity, although a consistent finding in congenital disorders of glycosylation patients, is not specific to this group of disorders. PMID: 19100247

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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