Aldolase A, 1-364aa, Human

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01-1781-A
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Proteins, Recombinant
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Product Name Aldolase A, 1-364aa, Human
Background 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.
Synonyms ALDOA, ALDA, GSD12, Fructose bisphosphate aldolase A Aldolase A, Aldolase A fructose bisphosphatase, Aldolase A fructose bisphosphate, Fructose 1 6 bisphosphate triosephosphate lyase, Fructose bisphosphate aldolase, Lung cancer antigen NY LU 1, MGC10942, MGC17716, MGC17767, Muscle type aldolase,
Species Human
Amino Acid 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
Molecular Weight 52.5 kDa (473aa)
Concentration 0.5 mg/ml (determined by Bradford assay)
Form Liquid, in 20mM Tris-HCl buffer (pH8.0) containing 10% glycerol 0.1M NaCl
Purity > 95% by SDS-PAGE
Applications SDS-PAGE
NCBI Accession # NP_908930
Host E.coli
Tag His-tag
Storage Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -20C or -70C. Avoid repeated freezing and thawing cycles.
Intended Use For Research Use Only
References Pfleiderer G., et al. (1975) Beitr Pathol. 156(3):266-79.
Kishi H., et al. (1987) Proc Natl Acad USA. 84(23):8623-7.

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