GAA
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Official Full Name
glucosidase, alpha; acid
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Overview
This gene encodes acid alpha-glucosidase, which is essential for the degradation of glycogen to glucose in lysosomes. Different forms of acid alpha-glucosidase are obtained by proteolytic processing. Defects in this gene are the cause of glycogen storage disease II, also known as Pompes disease, which is an autosomal recessive disorder with a broad clinical spectrum. Three transcript variants encoding the same protein have been found for this gene. -
Synonyms
GAA; glucosidase, alpha; acid; lysosomal alpha-glucosidase; glycogen storage disease type II; Pompe disease; 70 kDa lysosomal alpha-glucosidase; Acid alpha glucosidase; Acid maltase; Aglucosidase alfa; Alpha glucosidase; Glucosidase alpha acid (Pompe disease glycogen storage disease type II); Glucosidase alpha acid; Glucosidase alpha; LYAG; LYAG_HUMAN; Lysosomal alpha glucosidase;
- Recombinant Proteins
- Therapeutic Proteins
- Cell & Tissue Lysates
- Protein Pre-coupled Magnetic Beads
- Assay Kits
- Human
- Mouse
- Rat
- CHO
- E.coli
- HEK293
- HEK293T
- In Vitro Cell Free System
- Mamanlian cells
- Mammalian Cell
- Wheat Germ
- Flag
- GST
- His
- Fc
- Avi
- Myc
- DDK
- Non
- Involved Pathway
- Protein Function
- Interacting Protein
- Other Resource
GAA involved in several pathways and played different roles in them. We selected most pathways GAA participated on our site, such as Galactose metabolism, Starch and sucrose metabolism, Metabolic pathways, which may be useful for your reference. Also, other proteins which involved in the same pathway with GAA were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|---|
| Galactose metabolism | GANC;G6PC3;G6PC2;G6PCA.2;HK2;GALE;AKR1B1;AKR1B1L;HK3 |
| Starch and sucrose metabolism | AMY2B;GPI1;G6PC3;GUSB;AMY2A4;UGP2B;G6PC2;PGM1;GYS1 |
| Metabolic pathways | POLR2A;POLR2K;PFAS;ATP5I;GCNT3;AKR1B10;CYP11B2;CYP2B6;CYP2C54 |
| Lysosome | IDUA;ENTPD4;LAMP1;ACP2;AP1G2;AP1S3B;NPC2;CTSJ;CTSSB.1 |
GAA has several biochemical functions, for example, . Some of the functions are cooperated with other proteins, some of the functions could acted by GAA itself. We selected most functions GAA had, and list some proteins which have the same functions with GAA. You can find most of the proteins on our site.
| Function | Related Protein |
|---|
GAA has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with GAA here. Most of them are supplied by our site. Hope this information will be useful for your research of GAA.
HIVEP1; STAT2; EP300; ypiP; q9wmx2-pro_0000037548; NUMBL; pi3p; cona_canen
Research Area
Related articles
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Customer Reviews (3)
Write a reviewAdditionally, cost-effectiveness, competitive pricing, and bulk purchase options can also be advantageous for researchers working within limited budgets.
The ability to customize the GAA protein variants or modifications offered by the manufacturer is also advantageous, as it allows me to tailor the protein to my specific research objectives.
I appreciate the manufacturer's commitment to maintaining exceptional protein quality standards, which ensures reliable and consistent results in my trials.
Q&As (5)
Ask a questionGAA protein is one of several enzymes involved in glycogen metabolism, each playing a specific role in glycogen breakdown.
Enzyme replacement therapy (ERT) and gene therapy are two treatment options available for Pompe disease patients to replace or correct the deficient GAA protein.
GAA protein deficiency is primarily associated with Pompe disease, but there are other glycogen storage diseases related to deficiencies of different enzymes.
ERT involves the infusion of recombinant GAA protein to replace the missing or deficient enzyme in Pompe disease patients.
While GAA protein therapy can improve the symptoms and quality of life for Pompe disease patients, it may not fully reverse the damage caused by the disease.
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