|Calculated MW||41.5 kDa (384 aa, 1-364 aa + His Tag), confirmed by MALDI-TOF.|
|Other Names||Fructose bisphosphate Aldolase A, ALDOA, ALDA, GSD12|
|Sequence||MGSSHHHHHH SSGLVPRGSH MPYQYPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE NTEENRRFYR QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS KGGVVGIKVD KGVVPLAGTN GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKIGEHTPS ALAIMENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HIYLEGTLLK PNMVTPGHAC TQKFSHEEIA MATVTALRRT VPPAVTGITF LSGGQSEEEA SINLNAINKC PLLKPWALTF SYGRALQASA LKAWGGKKEN LKAAQEEYVK RALANSLACQ GKYTPSGQAG AAASESLFVS NHAY|
|Storage||-80°C; 1 mg/ml in 20 mM Tris-HCl buffer (pH 8.0) containing 100 mM NaCl and 10% glycerol.|
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Provided below are standard protocols that you may find useful for product applications.
Fructose bisphosphate aldolase A, also known as Aldolase A is a glycolytic enzyme that catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. It 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. Deficiency has been associated with myopathy and hemolytic anemia. Recombinant human Aldolase A, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
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Izzo P.,et al.Eur. J. Biochem. 164:9-13(1987).
Izzo P.,et al.Eur. J. Biochem. 174:569-578(1988).
Mukai T.,et al.Eur. J. Biochem. 195:781-787(1991).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
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