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Arsenate reductase (EC 1.20.4.4) (Arsenical pump modifier) (Protein ArsC)

 ARSC_STAAU              Reviewed;         131 AA.
P0A006; P30330; Q6Y0M0; Q6Y0M4; Q6Y0N2; Q8GQH3;
15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
15-FEB-2005, sequence version 1.
27-SEP-2017, entry version 94.
RecName: Full=Arsenate reductase {ECO:0000255|HAMAP-Rule:MF_01624, ECO:0000303|PubMed:1409657};
EC=1.20.4.4 {ECO:0000269|PubMed:10606519, ECO:0000269|PubMed:11862551, ECO:0000269|PubMed:12072565, ECO:0000269|PubMed:12682056, ECO:0000269|PubMed:1409657, ECO:0000269|PubMed:16797027, ECO:0000269|PubMed:8003493};
AltName: Full=Arsenical pump modifier;
AltName: Full=Protein ArsC;
Name=arsC {ECO:0000255|HAMAP-Rule:MF_01624,
ECO:0000303|PubMed:1534328};
Staphylococcus aureus.
Plasmid pI258.
Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
Staphylococcus.
NCBI_TaxID=1280;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND DISRUPTION
PHENOTYPE.
PLASMID=pI258;
PubMed=1534328; DOI=10.1128/jb.174.11.3684-3694.1992;
Ji G., Silver S.;
"Regulation and expression of the arsenic resistance operon from
Staphylococcus aureus plasmid pI258.";
J. Bacteriol. 174:3684-3694(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=SW1, SW18, SW24, and SW4;
Tibor L., Cramton S.E., Goetz F., Hunt T.K.;
"Characterization of a collection of clinical Staphylococcus aureus
wound isolates.";
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
PLASMID=pI258;
PubMed=1409657; DOI=10.1073/pnas.89.20.9474;
Ji G., Silver S.;
"Reduction of arsenate to arsenite by the ArsC protein of the arsenic
resistance operon of Staphylococcus aureus plasmid pI258.";
Proc. Natl. Acad. Sci. U.S.A. 89:9474-9478(1992).
[4]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MASS
SPECTROMETRY.
PLASMID=pI258;
PubMed=8003493; DOI=10.1021/bi00189a034;
Ji G., Garber E.A.E., Armes L.G., Chen C.-M., Fuchs J.A., Silver S.;
"Arsenate reductase of Staphylococcus aureus plasmid pI258.";
Biochemistry 33:7294-7299(1994).
[5]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MASS
SPECTROMETRY, MUTAGENESIS OF CYS-10; CYS-15; CYS-82 AND CYS-89, AND
REACTION MECHANISM.
PLASMID=pI258;
PubMed=10606519; DOI=10.1021/bi9911841;
Messens J., Hayburn G., Desmyter A., Laus G., Wyns L.;
"The essential catalytic redox couple in arsenate reductase from
Staphylococcus aureus.";
Biochemistry 38:16857-16865(1999).
[6]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL
PROPERTIES, AND STRUCTURE BY NMR.
PLASMID=pI258;
PubMed=11862551; DOI=10.1007/s007750100282;
Messens J., Martins J.C., Brosens E., Van Belle K., Jacobs D.M.,
Willem R., Wyns L.;
"Kinetics and active site dynamics of Staphylococcus aureus arsenate
reductase.";
J. Biol. Inorg. Chem. 7:146-156(2002).
[7]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL
PROPERTIES, METAL-BINDING, AND MUTAGENESIS OF ASN-13; GLU-21; SER-36
AND ASP-65.
PubMed=12682056; DOI=10.1074/jbc.M303194200;
Lah N., Lah J., Zegers I., Wyns L., Messens J.;
"Specific potassium binding stabilizes pI258 arsenate reductase from
Staphylococcus aureus.";
J. Biol. Chem. 278:24673-24679(2003).
[8] {ECO:0000244|PDB:1JF8, ECO:0000244|PDB:1JFV}
X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF REDUCED AND OXIDIZED FORM OF
DOUBLE MUTANT SER-10/ALA-15 IN COMPLEX WITH POTASSIUM, FUNCTION AS A
PHOSPHATASE, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-10;
CYS-15 AND CYS-89, ACTIVE SITE, AND REACTION MECHANISM.
PLASMID=pI258;
PubMed=11573087; DOI=10.1038/nsb1001-843;
Zegers I., Martins J.C., Willem R., Wyns L., Messens J.;
"Arsenate reductase from S. aureus plasmid pI258 is a phosphatase
drafted for redox duty.";
Nat. Struct. Biol. 8:843-847(2001).
[9] {ECO:0000244|PDB:1LJL, ECO:0000244|PDB:1LJU, ECO:0000244|PDB:1LK0}
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF WILD-TYPE AND OF MUTANTS
ALA-15 AND LEU-89 IN COMPLEXES WITH POTASSIUM, FUNCTION, CATALYTIC
ACTIVITY, MUTAGENESIS OF ARG-16; SER-17; CYS-89 AND ASP-105, STRUCTURE
BY NMR OF MUTANTS CYS-82 AND CYS-89, ACTIVE SITE, AND REACTION
MECHANISM.
PLASMID=pI258;
PubMed=12072565; DOI=10.1073/pnas.132142799;
Messens J., Martins J.C., Van Belle K., Brosens E., Desmyter A.,
De Gieter M., Wieruszeski J.-M., Willem R., Wyns L., Zegers I.;
"All intermediates of the arsenate reductase mechanism, including an
intramolecular dynamic disulfide cascade.";
Proc. Natl. Acad. Sci. U.S.A. 99:8506-8511(2002).
[10] {ECO:0000244|PDB:1RXE, ECO:0000244|PDB:1RXI}
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF TRIPLE MUTANT
SER-10/ALA-15/SER-82 IN COMPLEX WITH 5-THIO-2-NITROBENZOIC ACID AND
POTASSIUM.
PubMed=15159594; DOI=10.1107/S0907444904007334;
Messens J., Van Molle I., Vanhaesebrouck P., Van Belle K., Wahni K.,
Martins J.C., Wyns L., Loris R.;
"The structure of a triple mutant of pI258 arsenate reductase from
Staphylococcus aureus and its 5-thio-2-nitrobenzoic acid adduct.";
Acta Crystallogr. D 60:1180-1184(2004).
[11] {ECO:0000244|PDB:2CD7, ECO:0000244|PDB:2FXI}
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF MUTANT GLN-62 IN COMPLEX
WITH SODIUM AND OF DOUBLE MUTANT SER-10/ALA-15 IN COMPLEX WITH
POTASSIUM, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-62.
PubMed=16797027; DOI=10.1016/j.jmb.2006.05.054;
Roos G., Buts L., Van Belle K., Brosens E., Geerlings P., Loris R.,
Wyns L., Messens J.;
"Interplay between ion binding and catalysis in the thioredoxin-
coupled arsenate reductase family.";
J. Mol. Biol. 360:826-838(2006).
-!- FUNCTION: Catalyzes the reduction of arsenate [As(V)] to arsenite
[As(III)] (PubMed:1409657, PubMed:8003493, PubMed:10606519,
PubMed:11862551, PubMed:12072565, PubMed:12682056,
PubMed:16797027). In vitro, has also low phosphatase activity with
para-nitrophenyl phosphate (pNPP) as substrate (PubMed:11573087).
{ECO:0000269|PubMed:10606519, ECO:0000269|PubMed:11573087,
ECO:0000269|PubMed:11862551, ECO:0000269|PubMed:12072565,
ECO:0000269|PubMed:12682056, ECO:0000269|PubMed:1409657,
ECO:0000269|PubMed:16797027, ECO:0000269|PubMed:8003493}.
-!- CATALYTIC ACTIVITY: Arsenate + thioredoxin = arsenite +
thioredoxin disulfide + H(2)O. {ECO:0000255|HAMAP-Rule:MF_01624,
ECO:0000269|PubMed:10606519, ECO:0000269|PubMed:11862551,
ECO:0000269|PubMed:12072565, ECO:0000269|PubMed:12682056,
ECO:0000269|PubMed:1409657, ECO:0000269|PubMed:16797027,
ECO:0000269|PubMed:8003493}.
-!- ENZYME REGULATION: Potassium binding stabilizes the enzyme and
increases its specific activity (PubMed:12682056,
PubMed:16797027). Activity is also stimulated by sulfate
(PubMed:16797027). Inhibited by arsenite (mixed inhibitor)
(PubMed:11862551). {ECO:0000269|PubMed:11862551,
ECO:0000269|PubMed:12682056, ECO:0000269|PubMed:16797027}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.8 uM for arsenate (below 1 mM arsenate)
{ECO:0000269|PubMed:8003493};
KM=2 mM for arsenate (above 1 mM arsenate)
{ECO:0000269|PubMed:8003493};
KM=0.066 uM for arsenate {ECO:0000269|PubMed:10606519};
KM=68 uM for arsenate {ECO:0000269|PubMed:11862551};
KM=9 uM for arsenate (in the presence of KCl)
{ECO:0000269|PubMed:12682056, ECO:0000269|PubMed:16797027};
KM=22 uM for arsenate (in the presence of NaCl)
{ECO:0000269|PubMed:12682056, ECO:0000269|PubMed:16797027};
KM=61 uM for arsenate (in the presence of Na(2)SO(4))
{ECO:0000269|PubMed:16797027};
KM=81 uM for arsenate (in the presence of K(2)SO(4))
{ECO:0000269|PubMed:16797027};
KM=146 mM for para-nitrophenyl phosphate (reduced form only)
{ECO:0000269|PubMed:11573087};
Vmax=200 nmol/min/mg enzyme (below 1 mM arsenate)
{ECO:0000269|PubMed:8003493};
Vmax=450 nmol/min/mg enzyme (above 1 mM arsenate)
{ECO:0000269|PubMed:8003493};
Note=kcat is 4.5 min(-1) with arsenate as substrate (at 2 uM
arsenate) and kcat is 9.9 min(-1) with arsenate as substrate (at
10 mM arsenate) (PubMed:10606519). kcat is 54 min(-1) in the
presence of KCl (PubMed:12682056, PubMed:16797027). kcat is 35
min(-1) in the presence of NaCl (PubMed:12682056,
PubMed:16797027). kcat is 172 min(-1) in the presence of
Na(2)SO(4) (PubMed:16797027). kcat is 219 min(-1) in the
presence of K(2)SO(4) (PubMed:16797027). kcat is 0.53 min(-1)
for the phosphatase activity with para-nitrophenyl phosphate as
substrate (PubMed:11573087). {ECO:0000269|PubMed:10606519,
ECO:0000269|PubMed:11573087, ECO:0000269|PubMed:12682056,
ECO:0000269|PubMed:16797027};
pH dependence:
Optimum pH is 8. {ECO:0000269|PubMed:11862551};
-!- SUBUNIT: Monomer.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01624,
ECO:0000269|PubMed:1409657}.
-!- INDUCTION: Induced by arsenate [As(V)], arsenite [As(III)], and
antimonite [Sb(III)]. {ECO:0000269|PubMed:1534328}.
-!- PTM: Cys-89 performs a nucleophilic attack on a Cys-10-Cys-82
intermediate, forming another disulfide intermediate with Cys-82.
{ECO:0000305|PubMed:11573087, ECO:0000305|PubMed:12072565}.
-!- MASS SPECTROMETRY: Mass=14810.5; Method=Electrospray; Range=1-131;
Evidence={ECO:0000269|PubMed:8003493};
-!- MASS SPECTROMETRY: Mass=14812; Method=Electrospray; Range=1-131;
Evidence={ECO:0000269|PubMed:10606519};
-!- DISRUPTION PHENOTYPE: Deletion of the gene leads to a complete
loss of arsenate resistance, but does not affect arsenite or
antimony resistance. {ECO:0000269|PubMed:1534328}.
-!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine
protein phosphatase family. Thioredoxin-coupled ArsC subfamily.
{ECO:0000255|HAMAP-Rule:MF_01624, ECO:0000305}.
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EMBL; M86824; AAA25638.1; -; Genomic_DNA.
EMBL; AY194061; AAP32334.1; -; Genomic_DNA.
EMBL; AY194062; AAP32338.1; -; Genomic_DNA.
EMBL; AY194064; AAP32346.1; -; Genomic_DNA.
EMBL; AY194065; AAP32350.1; -; Genomic_DNA.
PIR; A53641; A53641.
PIR; D41903; D41903.
RefSeq; WP_000163242.1; NZ_NAJH01000080.1.
RefSeq; WP_000358995.1; NZ_NAJD01000043.1.
RefSeq; YP_001573918.1; NC_010077.1.
RefSeq; YP_001715971.1; NC_010419.1.
RefSeq; YP_006937217.1; NC_013292.1.
RefSeq; YP_006937607.1; NC_013319.1.
RefSeq; YP_006937727.1; NC_013322.1.
RefSeq; YP_006937753.1; NC_013323.1.
RefSeq; YP_006938161.1; NC_013333.1.
RefSeq; YP_006938435.1; NC_013340.1.
RefSeq; YP_006938641.1; NC_013347.1.
RefSeq; YP_006938712.1; NC_013349.1.
RefSeq; YP_006938775.1; NC_013352.1.
RefSeq; YP_006939395.1; NC_018965.1.
RefSeq; YP_006940871.1; NC_019009.1.
RefSeq; YP_536862.1; NC_007931.1.
PDB; 1JF8; X-ray; 1.12 A; A=1-131.
PDB; 1JFV; X-ray; 2.00 A; A=1-131.
PDB; 1LJL; X-ray; 2.01 A; A=1-131.
PDB; 1LJU; X-ray; 1.40 A; A=1-131.
PDB; 1LK0; X-ray; 1.60 A; A/B=1-131.
PDB; 1RXE; X-ray; 1.70 A; A=1-131.
PDB; 1RXI; X-ray; 1.50 A; A=1-131.
PDB; 2CD7; X-ray; 1.50 A; A=1-131.
PDB; 2FXI; X-ray; 1.80 A; A=1-131.
PDBsum; 1JF8; -.
PDBsum; 1JFV; -.
PDBsum; 1LJL; -.
PDBsum; 1LJU; -.
PDBsum; 1LK0; -.
PDBsum; 1RXE; -.
PDBsum; 1RXI; -.
PDBsum; 2CD7; -.
PDBsum; 2FXI; -.
ProteinModelPortal; P0A006; -.
SMR; P0A006; -.
DrugBank; DB02763; 5-Mercapto-2-Nitro-Benzoic Acid.
DrugBank; DB03138; Perchlorate Ion.
DrugBank; DB03352; S-Arsonocysteine.
GeneID; 13874340; -.
GeneID; 13874755; -.
GeneID; 13874878; -.
GeneID; 13874905; -.
GeneID; 13875324; -.
GeneID; 13875605; -.
GeneID; 13875818; -.
GeneID; 13875891; -.
GeneID; 13875956; -.
GeneID; 13876308; -.
GeneID; 13877846; -.
GeneID; 3978621; -.
GeneID; 5759819; -.
GeneID; 6155824; -.
BioCyc; MetaCyc:MONOMER-10862; -.
BRENDA; 1.20.4.1; 3352.
BRENDA; 1.20.4.B2; 3352.
SABIO-RK; P0A006; -.
EvolutionaryTrace; P0A006; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0030612; F:arsenate reductase (thioredoxin) activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
GO; GO:0046685; P:response to arsenic-containing substance; IEA:UniProtKB-KW.
HAMAP; MF_01624; Arsenate_reduct; 1.
InterPro; IPR014064; Arsenate_reductase_ArsC.
InterPro; IPR023485; Ptyr_pPase_SF.
Pfam; PF01451; LMWPc; 1.
SMART; SM00226; LMWPc; 1.
SUPFAM; SSF52788; SSF52788; 1.
TIGRFAMs; TIGR02691; arsC_pI258_fam; 1.
1: Evidence at protein level;
3D-structure; Arsenical resistance; Cytoplasm; Disulfide bond;
Metal-binding; Oxidoreductase; Plasmid; Potassium;
Redox-active center.
CHAIN 1 131 Arsenate reductase.
/FTId=PRO_0000162523.
ACT_SITE 10 10 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_01624,
ECO:0000305|PubMed:11573087,
ECO:0000305|PubMed:12072565}.
ACT_SITE 82 82 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_01624,
ECO:0000305|PubMed:11573087,
ECO:0000305|PubMed:12072565}.
ACT_SITE 89 89 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_01624,
ECO:0000305|PubMed:11573087,
ECO:0000305|PubMed:12072565}.
METAL 13 13 Potassium. {ECO:0000269|PubMed:11573087,
ECO:0000269|PubMed:12072565,
ECO:0000269|PubMed:12682056,
ECO:0000269|PubMed:15159594,
ECO:0000269|PubMed:16797027}.
METAL 36 36 Potassium. {ECO:0000269|PubMed:11573087,
ECO:0000269|PubMed:12072565,
ECO:0000269|PubMed:12682056,
ECO:0000269|PubMed:15159594,
ECO:0000269|PubMed:16797027}.
METAL 63 63 Potassium. {ECO:0000269|PubMed:11573087,
ECO:0000269|PubMed:12072565,
ECO:0000269|PubMed:12682056,
ECO:0000269|PubMed:15159594,
ECO:0000269|PubMed:16797027}.
METAL 65 65 Potassium. {ECO:0000269|PubMed:11573087,
ECO:0000269|PubMed:12072565,
ECO:0000269|PubMed:12682056,
ECO:0000269|PubMed:15159594,
ECO:0000269|PubMed:16797027}.
DISULFID 10 82 Redox-active; alternate.
{ECO:0000244|PDB:1LK0, ECO:0000255|HAMAP-
Rule:MF_01624,
ECO:0000305|PubMed:11573087,
ECO:0000305|PubMed:12072565}.
DISULFID 82 89 Redox-active; alternate.
{ECO:0000244|PDB:1JFV,
ECO:0000244|PDB:1LJU, ECO:0000255|HAMAP-
Rule:MF_01624,
ECO:0000305|PubMed:10606519,
ECO:0000305|PubMed:11573087,
ECO:0000305|PubMed:12072565}.
VARIANT 2 2 D -> T (in strain: SW18, SW4, SW24 and
SW1).
VARIANT 24 33 GKEILGEGWN -> AKQILAKDWD (in strain:
SW18).
VARIANT 24 31 GKEILGEG -> AKQILADD (in strain: SW24 and
SW1).
VARIANT 24 31 GKEILGEG -> AKQILAED (in strain: SW4).
VARIANT 56 56 D -> G (in strain: SW18, SW4, SW24 and
SW1).
VARIANT 65 65 D -> N (in strain: SW24 and SW1).
VARIANT 70 76 DILKQSD -> NIIKNSN (in strain: SW18, SW4,
SW24 and SW1).
VARIANT 87 87 N -> V (in strain: SW18, SW4, SW24 and
SW1).
VARIANT 91 91 I -> S (in strain: SW4, SW24 and SW1).
VARIANT 91 91 I -> T (in strain: SW18).
VARIANT 94 94 P -> T (in strain: SW18, SW4, SW24 and
SW1).
VARIANT 110 110 E -> P (in strain: SW18, SW4, SW24 and
SW1).
VARIANT 123 123 L -> I (in strain: SW4, SW24 and SW1).
VARIANT 123 123 L -> V (in strain: SW18).
VARIANT 127 127 K -> N (in strain: SW18, SW4, SW24 and
SW1).
VARIANT 130 130 L -> S (in strain: SW18, SW4, SW24 and
SW1).
MUTAGEN 10 10 C->A: Loss of activity.
{ECO:0000269|PubMed:10606519}.
MUTAGEN 10 10 C->S: Loss of activity; when associated
with A-15. {ECO:0000269|PubMed:10606519,
ECO:0000269|PubMed:11573087}.
MUTAGEN 13 13 N->A: Loss of K(+) stabilization over
Na(+). {ECO:0000269|PubMed:12682056}.
MUTAGEN 15 15 C->A: 2-fold decrease in affinity for
arsenate. Does not affect affinity for
pNPP. Loss of activity; when associated
with S-10. {ECO:0000269|PubMed:10606519,
ECO:0000269|PubMed:11573087}.
MUTAGEN 16 16 R->K: Loss of activity.
{ECO:0000269|PubMed:12072565}.
MUTAGEN 17 17 S->A: 5-fold decrease in catalytic
efficiency.
{ECO:0000269|PubMed:12072565}.
MUTAGEN 21 21 E->A: Decreases the thermal stabilization
effect of K(+).
{ECO:0000269|PubMed:12682056}.
MUTAGEN 36 36 S->A: Strong impact on thermal
stabilization.
{ECO:0000269|PubMed:12682056}.
MUTAGEN 62 62 H->Q: Uncouples the sulfate effect from
the potassium effect on the kinetics.
{ECO:0000269|PubMed:16797027}.
MUTAGEN 65 65 D->A: Loss of K(+) stabilization over
Na(+). {ECO:0000269|PubMed:12682056}.
MUTAGEN 82 82 C->S: Loss of activity.
{ECO:0000269|PubMed:10606519}.
MUTAGEN 89 89 C->A: Loss of activity.
{ECO:0000269|PubMed:10606519}.
MUTAGEN 89 89 C->L: Leads to a reductase locked in the
C-10/C-82 intermediate form. Decrease in
affinity for pNPP.
{ECO:0000269|PubMed:11573087,
ECO:0000269|PubMed:12072565}.
MUTAGEN 105 105 D->A: 4-fold decrease in catalytic
efficiency.
{ECO:0000269|PubMed:12072565}.
STRAND 4 15 {ECO:0000244|PDB:1JF8}.
HELIX 16 27 {ECO:0000244|PDB:1JF8}.
TURN 29 31 {ECO:0000244|PDB:1JF8}.
STRAND 32 40 {ECO:0000244|PDB:1JF8}.
HELIX 46 54 {ECO:0000244|PDB:1JF8}.
HELIX 69 74 {ECO:0000244|PDB:1JF8}.
STRAND 76 80 {ECO:0000244|PDB:1JF8}.
HELIX 83 88 {ECO:0000244|PDB:1JF8}.
STRAND 96 100 {ECO:0000244|PDB:1JF8}.
HELIX 111 129 {ECO:0000244|PDB:1JF8}.
SEQUENCE 131 AA; 14813 MW; 03871148DC433A18 CRC64;
MDKKTIYFIC TGNSCRSQMA EGWGKEILGE GWNVYSAGIE THGVNPKAIE AMKEVDIDIS
NHTSDLIDND ILKQSDLVVT LCSDADNNCP ILPPNVKKEH WGFDDPAGKE WSEFQRVRDE
IKLAIEKFKL R


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ASNA1-101AP Arsenical Pump driving ATPase Antigenic peptide: P-ASNA1 Host: Rabbit Affinity purifed 100ul
ASNA1-101AP PC-ASNA1 (WB control) Arsenical Pump driving ATPase Immunogen: peptide (22mer) Host: Rabbit 100-150ul
ASNA1-101AP P-ASNA1 (Antigenic peptide) Arsenical Pump driving ATPase Immunogen: peptide (22mer) Host: Rabbit 100ul
ASNA1-101AP Arsenical Pump driving ATPase Biotin Conjugates: ASNA1-Biotin Host: Rabbit Affinity purifed 200ul
ASNA1-101AP Arsenical Pump driving ATPase FITC-conjugates: ASNA1-FITC Host: Rabbit Affinity purifed 200ul
ASNA1-101AP ASNA1-Biotin (Biotin Conjugates) Arsenical Pump driving ATPase Immunogen: peptide (22mer) Host: Rabbit 200ul
ASNA1-101AP ASNA1-FITC (FITC-conjugates) Arsenical Pump driving ATPase Immunogen: peptide (22mer) Host: Rabbit 200ul
F-04000 FERRIC ARSENATE (Iron(III) Arsenate) CAS: 10102-49-5 100 gm
F-04000 FERRIC ARSENATE (Iron(III) Arsenate) CAS: 10102-49-5 500 gm
S-08495 STANNOUS ARSENATE (Tin (II) Arsenate) CAS: 15476-59-2 100 gm
S-08495 STANNOUS ARSENATE (Tin (II) Arsenate) CAS: 15476-59-2 250 gm
EIAAB10691 Carbonyl reductase II,DCXR,Dicarbonyl_L-xylulose reductase,Homo sapiens,Human,kiDCR,Kidney dicarbonyl reductase,L-xylulose reductase,Sperm surface protein P34H,XR
EIAAB13217 ANG1,Another new gene 1 protein,C-14 sterol reductase,Delta(14)-sterol reductase,Delta-14-SR,Homo sapiens,Human,Putative sterol reductase SR-1,Sterol C14-reductase,TM7SF2,Transmembrane 7 superfamily m
10048-95-0 Sodium arsenate-dibasic Sodium arsenate-dibasi 1g


 

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