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Fructose-bisphosphate aldolase A (EC 4.1.2.13) (Muscle-type aldolase)

 ALDOA_RABIT             Reviewed;         364 AA.
P00883; Q28671;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
30-AUG-2017, entry version 155.
RecName: Full=Fructose-bisphosphate aldolase A;
EC=4.1.2.13;
AltName: Full=Muscle-type aldolase;
Name=ALDOA;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6546378;
Tolan D.R., Amsden A.B., Putney S.D., Urdea M.S., Penhoet E.E.;
"The complete nucleotide sequence for rabbit muscle aldolase A
messenger RNA.";
J. Biol. Chem. 259:1127-1131(1984).
[2]
PRELIMINARY PROTEIN SEQUENCE OF 2-364.
TISSUE=Muscle;
PubMed=4417717;
Sajgo M., Hajos G.;
"The amino acid sequence of rabbit muscle aldolase.";
Acta Biochim. Biophys. Acad. Sci. Hung. 9:239-241(1974).
[3]
PROTEIN SEQUENCE OF 2-364.
TISSUE=Muscle;
PubMed=4812352; DOI=10.1126/science.183.4130.1204;
Lai C.-Y., Nakai N., Chang D.;
"Amino acid sequence of rabbit muscle aldolase and the structure of
the active center.";
Science 183:1204-1206(1974).
[4]
PROTEIN SEQUENCE OF 2-165.
PubMed=1122141; DOI=10.1016/0003-9861(75)90397-5;
Nakai N., Chang D., Lai C.-Y.;
"Studies on the structure of rabbit muscle aldolase. Ordering of the
tryptic peptides; sequence of 164 amino acid residues in the NH2-
terminal BrCN peptide.";
Arch. Biochem. Biophys. 166:347-357(1975).
[5]
PROTEIN SEQUENCE OF 174-201, AND SEQUENCE REVISION.
PubMed=534504; DOI=10.1042/bj1830429;
Benfield P.A., Forcina B.G., Gibbons I., Perham R.N.;
"Extended amino acid sequences around the active-site lysine residue
of class-I fructose 1,6-bisphosphate aldolases from rabbit muscle,
sturgeon muscle, trout muscle and ox liver.";
Biochem. J. 183:429-444(1979).
[6]
PROTEIN SEQUENCE OF 252-364, AND SEQUENCE REVISION.
PubMed=1122142; DOI=10.1016/0003-9861(75)90398-7;
Lai C.-Y.;
"Studies on the structure of rabbit muscle aldolase. Determination of
the primary structure of the COOH-terminal BrCN peptide; the complete
sequence of the subunit polypeptide chain.";
Arch. Biochem. Biophys. 166:358-368(1975).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 38-56 AND 350-364.
PubMed=6687628; DOI=10.1038/302718a0;
Putney S.D., Herlihy W.C., Schimmel P.R.;
"A new troponin T and cDNA clones for 13 different muscle proteins,
found by shotgun sequencing.";
Nature 302:718-721(1983).
[8]
ACTIVE SITE, AND DEAMIDATION AT ASN-361.
PubMed=4857186; DOI=10.1016/S0006-291X(74)80360-8;
Hartman F.C., Welch M.H.;
"Identification of the histidyl residue of rabbit muscle aldolase
alkylated by N-bromoacetylethanolamine phosphate.";
Biochem. Biophys. Res. Commun. 57:85-92(1974).
[9]
ACTIVE SITE.
PubMed=5453;
Hartman F.C., Brown J.P.;
"Affinity labeling of a previously undetected essential lysyl residue
in class I fructose bisphosphate aldolase.";
J. Biol. Chem. 251:3057-3062(1976).
[10]
SUBSTRATE-BINDING SITE.
PubMed=499203; DOI=10.1111/j.1432-1033.1979.tb13258.x;
Patthy L., Varadi A., Thesz J., Kovacs K.;
"Identification of the C-1-phosphate-binding arginine residue of
rabbit-muscle aldolase. Isolation of 1,2-cyclohexanedione-labeled
peptide by chemisorption chromatography.";
Eur. J. Biochem. 99:309-313(1979).
[11]
INTERACTION WITH FBP2, AND SUBCELLULAR LOCATION.
PubMed=15757649; DOI=10.1016/j.febslet.2005.01.071;
Mamczur P., Rakus D., Gizak A., Dus D., Dzugaj A.;
"The effect of calcium ions on subcellular localization of aldolase-
FBPase complex in skeletal muscle.";
FEBS Lett. 579:1607-1612(2005).
[12]
INTERACTION WITH FBP2.
PubMed=18214967; DOI=10.1002/prot.21909;
Gizak A., Maciaszczyk E., Dzugaj A., Eschrich K., Rakus D.;
"Evolutionary conserved N-terminal region of human muscle fructose
1,6-bisphosphatase regulates its activity and the interaction with
aldolase.";
Proteins 72:209-216(2008).
[13]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
PubMed=8989320; DOI=10.1038/nsb0197-36;
Blom N., Sygusch J.;
"Product binding and role of the C-terminal region in class I D-
fructose 1,6-bisphosphate aldolase.";
Nat. Struct. Biol. 4:36-39(1997).
[14]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 3-345 IN COMPLEX WITH
SUBSTRATE, SUBUNIT, AND MUTAGENESIS OF GLU-35; ARG-43; LYS-147 AND
ARG-304.
PubMed=10504235; DOI=10.1021/bi9828371;
Choi K.H., Mazurkie A.S., Morris A.J., Utheza D., Tolan D.R.,
Allen K.N.;
"Structure of a fructose-1,6-bis(phosphate) aldolase liganded to its
natural substrate in a cleavage-defective mutant at 2.3 A.";
Biochemistry 38:12655-12664(1999).
[15]
X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS), AND MUTAGENESIS OF GLU-188;
GLU-190 AND LYS-230.
PubMed=11779856; DOI=10.1074/jbc.M107600200;
Maurady A., Zdanov A., de Moissac D., Beaudry D., Sygusch J.;
"A conserved glutamate residue exhibits multifunctional catalytic
roles in D-fructose-1,6-bisphosphate aldolases.";
J. Biol. Chem. 277:9474-9483(2002).
[16]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH WAS, AND
FUNCTION.
PubMed=17329259; DOI=10.1074/jbc.M611505200;
St-Jean M., Izard T., Sygusch J.;
"A hydrophobic pocket in the active site of glycolytic aldolase
mediates interactions with Wiskott-Aldrich syndrome protein.";
J. Biol. Chem. 282:14309-14315(2007).
[17]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 5-344 OF MUTANT VAL-129, AND
SUBUNIT.
PubMed=18453690; DOI=10.1107/S0907444908004976;
Sherawat M., Tolan D.R., Allen K.N.;
"Structure of a rabbit muscle fructose-1,6-bisphosphate aldolase A
dimer variant.";
Acta Crystallogr. D 64:543-550(2008).
[18]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SNX9,
INTERACTION WITH SNX9, SUBUNIT, AND CATALYTIC ACTIVITY.
PubMed=20129922; DOI=10.1074/jbc.M109.092049;
Rangarajan E.S., Park H., Fortin E., Sygusch J., Izard T.;
"Mechanism of aldolase control of sorting nexin 9 function in
endocytosis.";
J. Biol. Chem. 285:11983-11990(2010).
-!- FUNCTION: Plays a key role in glycolysis and gluconeogenesis. In
addition, may also function as scaffolding protein.
{ECO:0000269|PubMed:17329259}.
-!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone
phosphate + D-glyceraldehyde 3-phosphate.
{ECO:0000269|PubMed:20129922}.
-!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
phosphate and glycerone phosphate from D-glucose: step 4/4.
-!- SUBUNIT: Homotetramer. Interacts with SNX9 and WAS. Interacts with
FBP2; the interaction blocks FBP2 inhibition by physiological
concentrations of AMP and reduces inhibition by Ca(2+).
{ECO:0000269|PubMed:10504235, ECO:0000269|PubMed:15757649,
ECO:0000269|PubMed:17329259, ECO:0000269|PubMed:18214967,
ECO:0000269|PubMed:18453690, ECO:0000269|PubMed:20129922}.
-!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, I band
{ECO:0000269|PubMed:15757649}. Cytoplasm, myofibril, sarcomere, M
line {ECO:0000269|PubMed:15757649}. 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+).
-!- PTM: Asn-361 in form alpha is deaminated to Asp in form beta.
-!- MISCELLANEOUS: In vertebrates, three forms of this ubiquitous
glycolytic enzyme are found, aldolase A in muscle, aldolase B in
liver and aldolase C in brain.
-!- MISCELLANEOUS: Alkylation of Arg-43 inactivates the enzyme.
-!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Worthington enzyme manual;
URL="http://www.worthington-biochem.com/ALD/";
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EMBL; K02300; AAA31156.1; -; mRNA.
EMBL; V00876; CAA24245.1; -; mRNA.
EMBL; V00877; CAA24246.1; -; mRNA.
PIR; A92444; ADRBA.
RefSeq; NP_001075707.1; NM_001082238.1.
RefSeq; XP_008256151.1; XM_008257929.2.
RefSeq; XP_008256152.1; XM_008257930.2.
RefSeq; XP_017197924.1; XM_017342435.1.
UniGene; Ocu.864; -.
PDB; 1ADO; X-ray; 1.90 A; A/B/C/D=2-364.
PDB; 1EWD; X-ray; 2.46 A; A/B/C/D=2-364.
PDB; 1EWE; X-ray; 2.60 A; A/B/C/D=2-364.
PDB; 1EX5; X-ray; 2.20 A; A/B/C/D=2-364.
PDB; 1J4E; X-ray; 2.65 A; A/B/C/D=2-364.
PDB; 1ZAH; X-ray; 1.80 A; A/B/C/D=2-364.
PDB; 1ZAI; X-ray; 1.76 A; A/B/C/D=2-364.
PDB; 1ZAJ; X-ray; 1.89 A; A/B/C/D=2-364.
PDB; 1ZAL; X-ray; 1.89 A; A/B/C/D=2-364.
PDB; 2OT0; X-ray; 2.05 A; A/B/C/D=2-364.
PDB; 2OT1; X-ray; 2.05 A; A/B/C/D=2-364.
PDB; 2QUT; X-ray; 1.88 A; A/B/C/D=2-364.
PDB; 2QUU; X-ray; 1.98 A; A/B/C/D=2-364.
PDB; 2QUV; X-ray; 2.22 A; A/B/C/D=2-364.
PDB; 3B8D; X-ray; 2.00 A; A/B/C/D=2-364.
PDB; 3BV4; X-ray; 1.70 A; A=5-344.
PDB; 3DFN; X-ray; 1.86 A; A/B/C/D=2-364.
PDB; 3DFO; X-ray; 1.94 A; A/B/C/D=2-364.
PDB; 3DFP; X-ray; 2.05 A; A/B/C/D=2-364.
PDB; 3DFQ; X-ray; 1.82 A; A/B/C/D=2-364.
PDB; 3DFS; X-ray; 2.03 A; A/B/C/D=2-364.
PDB; 3DFT; X-ray; 1.94 A; A/B/C/D=2-364.
PDB; 3LGE; X-ray; 2.20 A; A/B/C/D=2-364.
PDB; 3TU9; X-ray; 2.09 A; A/B/C/D=2-364.
PDB; 5F4X; X-ray; 1.84 A; A/B/C/D=2-364.
PDB; 5VY5; EM; 2.60 A; A/B/C/D=2-364.
PDB; 6ALD; X-ray; 2.30 A; A/B/C/D=2-364.
PDBsum; 1ADO; -.
PDBsum; 1EWD; -.
PDBsum; 1EWE; -.
PDBsum; 1EX5; -.
PDBsum; 1J4E; -.
PDBsum; 1ZAH; -.
PDBsum; 1ZAI; -.
PDBsum; 1ZAJ; -.
PDBsum; 1ZAL; -.
PDBsum; 2OT0; -.
PDBsum; 2OT1; -.
PDBsum; 2QUT; -.
PDBsum; 2QUU; -.
PDBsum; 2QUV; -.
PDBsum; 3B8D; -.
PDBsum; 3BV4; -.
PDBsum; 3DFN; -.
PDBsum; 3DFO; -.
PDBsum; 3DFP; -.
PDBsum; 3DFQ; -.
PDBsum; 3DFS; -.
PDBsum; 3DFT; -.
PDBsum; 3LGE; -.
PDBsum; 3TU9; -.
PDBsum; 5F4X; -.
PDBsum; 5VY5; -.
PDBsum; 6ALD; -.
ProteinModelPortal; P00883; -.
SMR; P00883; -.
BioGrid; 1172078; 2.
IntAct; P00883; 1.
MINT; MINT-7995296; -.
STRING; 9986.ENSOCUP00000020204; -.
BindingDB; P00883; -.
ChEMBL; CHEMBL4695; -.
iPTMnet; P00883; -.
PRIDE; P00883; -.
Ensembl; ENSOCUT00000009869; ENSOCUP00000008499; ENSOCUG00000006329.
GeneID; 100009055; -.
KEGG; ocu:100009055; -.
CTD; 226; -.
eggNOG; KOG1557; Eukaryota.
eggNOG; COG3588; LUCA.
GeneTree; ENSGT00390000010235; -.
HOGENOM; HOG000220876; -.
HOVERGEN; HBG002386; -.
InParanoid; P00883; -.
KO; K01623; -.
OMA; MILKPNM; -.
OrthoDB; EOG091G0A9T; -.
BRENDA; 4.1.2.13; 1749.
SABIO-RK; P00883; -.
UniPathway; UPA00109; UER00183.
EvolutionaryTrace; P00883; -.
PRO; PR:P00883; -.
Proteomes; UP000001811; Chromosome 6.
Bgee; ENSOCUG00000006329; -.
GO; GO:0031674; C:I band; IEA:UniProtKB-SubCell.
GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:UniProtKB.
GO; GO:0006096; P:glycolytic process; IDA:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; IPI:UniProtKB.
Gene3D; 3.20.20.70; -; 1.
InterPro; IPR029768; Aldolase_I_AS.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR000741; FBA_I.
Pfam; PF00274; Glycolytic; 1.
PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Glycolysis; Isopeptide bond; Lyase;
Phosphoprotein; Reference proteome; Schiff base; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1122141,
ECO:0000269|PubMed:4812352}.
CHAIN 2 364 Fructose-bisphosphate aldolase A.
/FTId=PRO_0000216938.
REGION 272 274 Substrate binding. {ECO:0000244|PDB:6ALD,
ECO:0000269|PubMed:10504235}.
ACT_SITE 188 188 Proton acceptor.
{ECO:0000269|PubMed:11779856}.
ACT_SITE 230 230 Schiff-base intermediate with
dihydroxyacetone-P.
{ECO:0000269|PubMed:11779856}.
BINDING 43 43 Substrate. {ECO:0000244|PDB:6ALD,
ECO:0000269|PubMed:10504235}.
BINDING 304 304 Substrate. {ECO:0000244|PDB:6ALD,
ECO:0000269|PubMed:10504235}.
SITE 73 73 Essential for substrate cleavage.
SITE 108 108 Essential for substrate cleavage.
SITE 147 147 Alkylation inactivates the enzyme.
SITE 362 362 Alkylation inactivates the enzyme;
essential for the subsequent hydrolysis
of the dihydroxyacetone Schiff base.
SITE 364 364 Necessary for preference for fructose
1,6-bisphosphate over fructose 1-
phosphate.
MOD_RES 9 9 Phosphothreonine.
{ECO:0000250|UniProtKB:P04075}.
MOD_RES 36 36 Phosphoserine.
{ECO:0000250|UniProtKB:P04075}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000250|UniProtKB:P04075}.
MOD_RES 42 42 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P04075}.
MOD_RES 46 46 Phosphoserine.
{ECO:0000250|UniProtKB:P04075}.
MOD_RES 108 108 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04075}.
MOD_RES 111 111 N6-malonyllysine. {ECO:0000250}.
MOD_RES 132 132 Phosphoserine.
{ECO:0000250|UniProtKB:P05065}.
MOD_RES 272 272 Phosphoserine.
{ECO:0000250|UniProtKB:P04075}.
MOD_RES 312 312 N6-malonyllysine. {ECO:0000250}.
MOD_RES 330 330 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04075}.
MOD_RES 361 361 Deamidated asparagine; in form beta.
{ECO:0000269|PubMed:4857186}.
CROSSLNK 42 42 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P04075}.
CROSSLNK 42 42 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P04075}.
MUTAGEN 35 35 E->A: Reduces activity 14-fold.
{ECO:0000269|PubMed:10504235}.
MUTAGEN 43 43 R->A: Reduces activity 14-fold.
{ECO:0000269|PubMed:10504235}.
MUTAGEN 129 129 D->V: Alters protein-protein
interactions, leading to a dimeric
protein.
MUTAGEN 147 147 K->A: Loss of activity.
{ECO:0000269|PubMed:10504235}.
MUTAGEN 188 188 E->A: Reduces activity over 100-fold.
{ECO:0000269|PubMed:11779856}.
MUTAGEN 188 188 E->Q: Reduces activity over 1000-fold.
{ECO:0000269|PubMed:11779856}.
MUTAGEN 190 190 E->Q: Reduces activity 20-fold.
{ECO:0000269|PubMed:11779856}.
MUTAGEN 230 230 K->M: Loss of activity.
{ECO:0000269|PubMed:11779856}.
MUTAGEN 304 304 R->A: Reduces activity 400-fold.
{ECO:0000269|PubMed:10504235}.
CONFLICT 35 35 E -> Q (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 274 276 GQS -> SQE (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 276 276 S -> E (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 294 296 KPW -> WPK (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 354 354 S -> R (in Ref. 7; CAA24246).
{ECO:0000305}.
HELIX 10 23 {ECO:0000244|PDB:3BV4}.
STRAND 29 33 {ECO:0000244|PDB:3BV4}.
HELIX 37 45 {ECO:0000244|PDB:3BV4}.
TURN 46 48 {ECO:0000244|PDB:3BV4}.
HELIX 53 64 {ECO:0000244|PDB:3BV4}.
HELIX 68 70 {ECO:0000244|PDB:3BV4}.
TURN 71 73 {ECO:0000244|PDB:3BV4}.
STRAND 74 79 {ECO:0000244|PDB:3BV4}.
HELIX 81 84 {ECO:0000244|PDB:3BV4}.
TURN 89 91 {ECO:0000244|PDB:1EWE}.
HELIX 94 99 {ECO:0000244|PDB:3BV4}.
TURN 100 102 {ECO:0000244|PDB:3BV4}.
STRAND 104 108 {ECO:0000244|PDB:3BV4}.
STRAND 113 115 {ECO:0000244|PDB:3BV4}.
STRAND 119 121 {ECO:0000244|PDB:3BV4}.
STRAND 123 125 {ECO:0000244|PDB:3BV4}.
HELIX 131 140 {ECO:0000244|PDB:3BV4}.
STRAND 145 152 {ECO:0000244|PDB:3BV4}.
STRAND 155 157 {ECO:0000244|PDB:1ZAI}.
HELIX 161 180 {ECO:0000244|PDB:3BV4}.
STRAND 184 191 {ECO:0000244|PDB:3BV4}.
HELIX 199 219 {ECO:0000244|PDB:3BV4}.
HELIX 224 226 {ECO:0000244|PDB:3BV4}.
HELIX 246 258 {ECO:0000244|PDB:3BV4}.
STRAND 267 270 {ECO:0000244|PDB:3BV4}.
HELIX 277 289 {ECO:0000244|PDB:3BV4}.
STRAND 290 292 {ECO:0000244|PDB:2QUV}.
STRAND 296 303 {ECO:0000244|PDB:3BV4}.
HELIX 304 314 {ECO:0000244|PDB:3BV4}.
HELIX 318 320 {ECO:0000244|PDB:3BV4}.
HELIX 321 338 {ECO:0000244|PDB:3BV4}.
TURN 339 341 {ECO:0000244|PDB:3BV4}.
STRAND 345 347 {ECO:0000244|PDB:1ZAI}.
HELIX 351 354 {ECO:0000244|PDB:3DFQ}.
STRAND 358 360 {ECO:0000244|PDB:1ADO}.
HELIX 361 363 {ECO:0000244|PDB:1ZAI}.
SEQUENCE 364 AA; 39343 MW; E61BCBC60F668324 CRC64;
MPHSHPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE NTEENRRFYR
QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS KGGVVGIKVD KGVVPLAGTN
GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKIGEHTPS ALAIMENANV LARYASICQQ
NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HIYLEGTLLK PNMVTPGHAC
TQKYSHEEIA MATVTALRRT VPPAVTGVTF LSGGQSEEEA SINLNAINKC PLLKPWALTF
SYGRALQASA LKAWGGKKEN LKAAQEEYVK RALANSLACQ GKYTPSGQAG AAASESLFIS
NHAY


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25-695 Fructose-1,6-bisphosphate aldolase (EC 4.1.2.13) is a tetrameric glycolytic enzyme that catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacet 0.05 mg
CSB-EL001586RA Rat aldolase B, fructose-bisphosphate (ALDOB) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL001583RA Rat aldolase A, fructose-bisphosphate (ALDOA) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL001587RA Rat aldolase C, fructose-bisphosphate (ALDOC) ELISA kit, Species Rat, Sample Type serum, plasma 96T
20312313-1 ALD | fructose-1,6 bisphosphate aldolase 100 uL
E02F0213 Rat Fructose-1,6-bisphosphate aldolase 96 Tests/kit


 

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