Recombinant Human AGA Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0100

Recombinant Human AGA Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0100
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Product Overview

Tag His
Host Species Human
Accession CAA39029.1
Synonym AGU, ASRG, GA
Background S1 proteinis a family of low molecular weight protein found in vertebrates characterized by twoEF-hand calcium-binding motifs. There are at least 21 different S1 proteins, and the name is derived from the fact that the protein is1%soluble in ammonium sulfateat neutralpH. Most S1 proteins are disulfide-linked homodimer, and is normally present in cells derived from theneural crest, chondrocytes, macrophages, dendritic cells, etc. S1 proteins have been implicated in a variety of intracellular and extracellular functions. They are involved in regulation of protein phosphorylation, transcription factors, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response. Human Protein S1-A8, also known as S1 calcium-binding protein A8, Cystic fibrosis antigen, Migration inhibitory factor-related protein 8, S1A8, and CAGA, is a member of the S-1 family. S1A8 plays a role in various functions of myeloid cells by forming a heterocomplex with S1A9. S1A8 and S1A9 are known to be overexpressed in certain species of carcinomas. S1A8 plays an important role in dedifferentiation of thyroid carcinoma possibly by forming a complex with S1A9. S1A8 and S1A9 may also play a key role in inflammation-associated cancer.
Description A DNA sequence encoding the human AGA (CAA39029.1) (Met1-Ile346) was expressed with a C-terminal His tag.
Source HEK293
Predicted N Terminal Ser 24
AA Sequence Met1-Ile346
Molecular Weight The recombinant human AGA comprises 334 a.a. and has a predicted molecular mass of 36.1 kDa. The apparent molecular mass of the protein is approximately 47, 29, 23 and 20 kDa in SDS-PAGE under reducing conditions due to glycosylation.
Purity (5.2+44.1+46.8+3.4)% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, pH 7.4..
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

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


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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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