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Recombinant human N (4)- (beta-N-acetylglucosaminyl)-L-asparaginase

Recombinant human N (4)- (beta-N-acetylglucosaminyl)-L-asparaginase

Baculovirus
Mammalian cell

Code
MSDS	MSDS Datasheet
Size	Pls inquire
Source
Conjugate
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Product Details
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Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

AGA

Uniprot NO.

P20933

Research Area

Signal Transduction

Alternative Names

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)

Source

Yeast

Expression Region

206-346aa

Target Protein Sequence

TIGMVVIHKTGHIAAGTSTNGIKFKIHGRVGDSPIPGAGAYADDTAGAAAATGNGDILMRFLPSYQAVEYMRRGEDPTIACQKVISRIQKHFPEFFGAVICANVTGSYGAACNKLSTFTQFSFMVYNSEKNQPTEEKVDCI
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Mol. Weight

31.1kD

Protein Length

Glycosylasparaginase beta chain

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage Condition

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Shelf Life

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Target Background

Function(From Uniprot)

Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins.

Gene References into Functions

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