|Application ||WB, IHC-P, E|
|Calculated MW||39420 Da|
|Antigen Region||303-331 aa|
|Other Names||Fructose-bisphosphate aldolase A, Lung cancer antigen NY-LU-1, Muscle-type aldolase, ALDOA, ALDA|
|Target/Specificity||This ALDOA antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 303-331 amino acids from the C-terminal region of human ALDOA.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||ALDOA Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein (By similarity).|
|Cellular Location||Cytoplasm, myofibril, sarcomere, I band. Cytoplasm, myofibril, sarcomere, M line. 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+)|
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Provided below are standard protocols that you may find useful for product applications.
Aldolase A (fructose-bisphosphate aldolase) is a glycolytic enzyme that catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. Three aldolase isozymes (A, B, and C), encoded by three different genes, are differentially expressed during development. Aldolase A is found in the developing embryo and is produced in even greater amounts in adult muscle. Aldolase A expression is repressed in adult liver, kidney and intestine and similar to aldolase C levels in brain and other nervous tissue. Aldolase A deficiency has been associated with myopathy and hemolytic anemia.
Gizak,A., Proteins 72 (1), 209-216 (2008) Lu,J., Biochem. Biophys. Res. Commun. 369 (3), 948-952 (2008) Valis,K., Mol. Cell. Biochem. 311 (1-2), 225-231 (2008)
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