Recombinant Human Fructose-bisphosphate aldolase A (ALDOA)

Recombinant Human Fructose-bisphosphate aldolase A (ALDOA) — Catalyzes the reversible conversion of beta-D-fructose 1,6-bisphosphate (FBP) into two triose phosphate and plays a key role in glycolysis and gluconeogenesis. Purity >90%.

SKU: BCRECP-000057 Category:

Product Specifications

Product SkuBCRECP-000057
Product DescriptionRecombinant Human Fructose-bisphosphate aldolase A (ALDOA) Protein is expressed from Baculovirus with C-terminal 6xHis-tagged. It contains 2-364aa. [Accession | P04075].
Uniprot No.P04075
Gene NamesALDOA
PurityGreater than 90% as determined by SDS-PAGE.
Expression SystemBaculovirus
Expression Region2-364aa
SpeciesHomo sapiens (Human)
Tag InfoC-terminal 6xHis-tagged
Molecular weight40.4kDa
ActivityPlease contact us to obtain bioactivity data.
BufferIf the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.
StorageStore at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Research AreasMetabolism

Function

Catalyzes the reversible conversion of beta-D-fructose 1,6-bisphosphate (FBP) into two triose phosphate and plays a key role in glycolysis and gluconeogenesis. In addition, also functions as a scaffolding protein. In response to glucose deprivation, FBP dissociates from aldolase and acts as an adapter that promotes AMP-activated protein kinase (AMPK) activity: mechanistically, associates with transient receptor potential channels TrpV (TRPV1-TRPV4), promoting inhibition of the V-ATPase complex on lysosomes and AMPK activation via the AXIN1-STK11/LKB1 axis.

Biological Context

Subcellular Location: Cytoplasm, myofibril, sarcomere, I band; Cytoplasm, myofibril, sarcomere, M line
Disease Association: Glycogen storage disease 12 (GSD12) : A metabolic disorder associated with increased hepatic glycogen and hemolytic anemia. It may lead to myopathy with exercise intolerance and rhabdomyolysis. [The disease is caused by variants affecting the gene represented in this entry]
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4

Product Specifications

Recombinant Human Fructose-bisphosphate aldolase A (ALDOA) is a recombinant protein from Homo sapiens (Human), expressed in Baculovirus, covering amino acids 2-364aa, with C-terminal 6xHis-tagged tag, molecular weight 40.4kDa, purity Greater than 90% as determined by SDS-PAGE.. Suitable for ELISA and Western Blot applications.

SDS-PAGE: Single band at expected molecular weight confirming purity.

ELISA: Suitable as coating antigen or detection standard.

Western Blot: Compatible with standard Western Blot protocols.

Protein Interaction: Validated for SPR (Surface Plasmon Resonance) and BLI (Bio-Layer Interferometry) studies.

Shipping: Shipped at ambient temperature. Lyophilized protein is stable during transit.

Storage: Store lyophilized protein at -20°C to -80°C. Reconstituted protein should be aliquoted and stored at -80°C. Avoid repeated freeze-thaw cycles.

Shelf Life: 12 months from date of receipt when stored as recommended.

Shipping Time: Orders placed before 2 PM EST ship same day. International orders typically deliver within 5-10 business days.

Protein Biology

Function

Catalyzes the reversible conversion of beta-D-fructose 1,6-bisphosphate (FBP) into two triose phosphate and plays a key role in glycolysis and gluconeogenesis (PubMed:14766013). In addition, also functions as a scaffolding protein (By similarity). In response to glucose deprivation, FBP dissociates from aldolase and acts as an adapter that promotes AMP-activated protein kinase (AMPK) activity: mechanistically, associates with transient receptor potential channels TrpV (TRPV1-TRPV4), promoting inhibition of the V-ATPase complex on lysosomes and AMPK activation via the AXIN1-STK11/LKB1 axis (By similarity)

Subcellular Location

Cytoplasm, myofibril, sarcomere, I band; Cytoplasm, myofibril, sarcomere, M line

Disease Association

Glycogen storage disease 12 (GSD12) : A metabolic disorder associated with increased hepatic glycogen and hemolytic anemia. It may lead to myopathy with exercise intolerance and rhabdomyolysis. [The disease is caused by variants affecting the gene represented in this entry]

Subunit

Homotetramer (By similarity). Interacts with SNX9 and WAS (By similarity). Interacts with FBP2; the interaction blocks FBP2 inhibition by physiological concentrations of AMP and reduces inhibition by Ca(2+) (PubMed:18214967)

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4

Gene: ALDOA  |  Organism: Homo sapiens  |  Synonyms: Lung cancer antigen NY-LU-1; Muscle-type aldolase
Key Publications

Frequently Asked Questions

How do I order or inquire about this product?

Fill out the Online Inquiry form with your required quantity and specifications. You can also email sales@biocrestsci.com. Our team typically responds within 4 business hours with a quote and availability confirmation.

What is the shipping and delivery time?

Orders placed before 2 PM EST ship the same day. Domestic (US) delivery typically takes 2-3 business days. International orders deliver within 5-10 business days. All products are shipped at ambient temperature with appropriate packaging to ensure stability.

How should I store this recombinant protein?

Lyophilized proteins should be stored at -20°C to -80°C upon receipt. After reconstitution, aliquot and store at -80°C. Avoid repeated freeze-thaw cycles. Shelf life is 12 months from date of receipt when stored as recommended.

What quality controls are performed on your products?

Each product undergoes SDS-PAGE purity analysis (typically >85-95%), endotoxin testing, and bioactivity validation. Products are validated for ELISA, Western Blot, and SPR/BLI applications as specified on this product page. A Certificate of Analysis (CoA) is available upon request.

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