ALDOA Antibody (internal region, near N-Term)
Peptide-affinity purified goat antibody
- SPECIFICATION
 - CITATIONS
 - PROTOCOLS
 - BACKGROUND
 
Application 
  | WB, E | 
|---|---|
| Primary Accession | P04075 | 
| Other Accession | NP_000025.1, NP_001230106.1, 226, 11674 (mouse), 24189 (rat) | 
| Reactivity | Human, Mouse, Rat | 
| Predicted | Dog | 
| Host | Goat | 
| Clonality | Polyclonal | 
| Concentration | 0.5 mg/ml | 
| Isotype | IgG | 
| Calculated MW | 39420 Da | 
| Gene ID | 226 | 
|---|---|
| Other Names | Fructose-bisphosphate aldolase A, 4.1.2.13, Lung cancer antigen NY-LU-1, Muscle-type aldolase, ALDOA, ALDA | 
| Dilution | WB~~1:1000 E~~N/A  | 
| Format | 0.5 mg/ml in Tris saline, 0.02% sodium azide, pH7.3 with 0.5% bovine serum albumin | 
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. | 
| Precautions | ALDOA Antibody (internal region, near N-Term) is for research use only and not for use in diagnostic or therapeutic procedures. | 
| Name | ALDOA (HGNC:414) | 
|---|---|
| Synonyms | ALDA | 
| 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, may also function as scaffolding protein (By similarity). | 
| Cellular Location | Cytoplasm, myofibril, sarcomere, I band {ECO:0000250|UniProtKB:P00883}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000250|UniProtKB:P00883}. Note=In skeletal muscle, accumulates around the M line and within the I band, colocalizing with FBP2 on both sides of the Z line in the absence of Ca(2+) {ECO:0000250|UniProtKB:P00883} | 

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Provided below are standard protocols that you may find useful for product applications.
Background
This antibody is expected to recognize both reported isoforms (P_000025.1; NP_001230106.1). Reported variants represent identical protein: NP_908930.1, NP_908932.1, NP_001121089.1, NP_000025.1.
References
Human aldolase A natural mutants: relationship between flexibility of the C-terminal region and enzyme function. Esposito G, Vitagliano L, Costanzo P, Borrelli L, Barone R, Pavone L, Izzo P, Zagari A, Salvatore F. The Biochemical journal 2004 May 380 (Pt 1): 51-6. PMID: 14766013
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