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Delta(12)-fatty-acid desaturase (EC 1.14.19.22) (EC 1.14.19.6) (Omega-6 fatty acid desaturase, endoplasmic reticulum)

 FAD6E_ARATH             Reviewed;         383 AA.
P46313;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
25-APR-2018, entry version 144.
RecName: Full=Delta(12)-fatty-acid desaturase {ECO:0000303|PubMed:7907506};
EC=1.14.19.22 {ECO:0000269|PubMed:1730697};
EC=1.14.19.6 {ECO:0000269|PubMed:8685264};
AltName: Full=Omega-6 fatty acid desaturase, endoplasmic reticulum {ECO:0000303|PubMed:7907506};
Name=FAD2 {ECO:0000303|PubMed:7907506};
OrderedLocusNames=At3g12120 {ECO:0000312|Araport:AT3G12120};
ORFNames=T21B14.6 {ECO:0000312|EMBL:AAG51042.1}, T21B14_107,
T23B7.6 {ECO:0000312|EMBL:BAB01960.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION BY COLD, AND TISSUE
SPECIFICITY.
PubMed=7907506; DOI=10.1105/tpc.6.1.147;
Okuley J., Lightner J., Feldmann K.A., Yadav N., Lark E., Browse J.;
"Arabidopsis FAD2 gene encodes the enzyme that is essential for
polyunsaturated lipid synthesis.";
Plant Cell 6:147-158(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10907853; DOI=10.1093/dnares/7.3.217;
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 3. II.
Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC
and BAC clones.";
DNA Res. 7:217-221(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=1730697;
Miquel M., Browse J.;
"Arabidopsis mutants deficient in polyunsaturated fatty acid
synthesis. Biochemical and genetic characterization of a plant oleoyl-
phosphatidylcholine desaturase.";
J. Biol. Chem. 267:1502-1509(1992).
[7]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=8685264; DOI=10.1104/pp.111.1.223;
Covello P.S., Reed D.W.;
"Functional expression of the extraplastidial Arabidopsis thaliana
oleate desaturase gene (FAD2) in Saccharomyces cerevisiae.";
Plant Physiol. 111:223-226(1996).
[8]
FUNCTION, AND MUTAGENESIS OF ALA-63; ALA-104; THR-148; TYR-217;
ALA-295; SER-322 AND MET-324.
PubMed=9812895; DOI=10.1126/science.282.5392.1315;
Broun P., Shanklin J., Whittle E., Somerville C.;
"Catalytic plasticity of fatty acid modification enzymes underlying
chemical diversity of plant lipids.";
Science 282:1315-1317(1998).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11104757; DOI=10.1074/jbc.M006231200;
Caiveau O., Fortune D., Cantrel C., Zachowski A., Moreau F.;
"Consequences of omega -6-oleate desaturase deficiency on lipid
dynamics and functional properties of mitochondrial membranes of
Arabidopsis thaliana.";
J. Biol. Chem. 276:5788-5794(2001).
[10]
FUNCTION, AND MUTAGENESIS OF ALA-104; THR-148; SER-322 AND MET-324.
PubMed=11864983; DOI=10.1074/jbc.M200231200;
Broadwater J.A., Whittle E., Shanklin J.;
"Desaturation and hydroxylation. Residues 148 and 324 of Arabidopsis
FAD2, in addition to substrate chain length, exert a major influence
in partitioning of catalytic specificity.";
J. Biol. Chem. 277:15613-15620(2002).
[11]
SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=14690501; DOI=10.1111/j.1365-313X.2004.01949.x;
McCartney A.W., Dyer J.M., Dhanoa P.K., Kim P.K., Andrews D.W.,
McNew J.A., Mullen R.T.;
"Membrane-bound fatty acid desaturases are inserted co-translationally
into the ER and contain different ER retrieval motifs at their carboxy
termini.";
Plant J. 37:156-173(2004).
[12]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17507388; DOI=10.1093/pcp/pcm061;
Matos A.R., Hourton-Cabassa C., Cicek D., Reze N., Arrabaca J.D.,
Zachowski A., Moreau F.;
"Alternative oxidase involvement in cold stress response of
Arabidopsis thaliana fad2 and FAD3+ cell suspensions altered in
membrane lipid composition.";
Plant Cell Physiol. 48:856-865(2007).
[13]
MUTAGENESIS OF ALA-335.
PubMed=20345604; DOI=10.1111/j.1365-313X.2010.04212.x;
Song W., Maeda H., DellaPenna D.;
"Mutations of the ER to plastid lipid transporters TGD1, 2, 3 and 4
and the ER oleate desaturase FAD2 suppress the low temperature-induced
phenotype of Arabidopsis tocopherol-deficient mutant vte2.";
Plant J. 62:1004-1018(2010).
[14]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INDUCTION BY
OSMOTIC STRESS, AND MUTAGENESIS OF ALA-104.
PubMed=22279586; DOI=10.1371/journal.pone.0030355;
Zhang J., Liu H., Sun J., Li B., Zhu Q., Chen S., Zhang H.;
"Arabidopsis fatty acid desaturase FAD2 is required for salt tolerance
during seed germination and early seedling growth.";
PLoS ONE 7:E30355-E30355(2012).
[15]
SUBUNIT, AND INTERACTION WITH FAD3.
PubMed=24811169; DOI=10.1074/jbc.M114.572883;
Lou Y., Schwender J., Shanklin J.;
"FAD2 and FAD3 desaturases form heterodimers that facilitate metabolic
channeling in vivo.";
J. Biol. Chem. 289:17996-18007(2014).
-!- FUNCTION: ER (microsomal) omega-6 fatty acid desaturase introduces
the second double bond in the biosynthesis of 18:3 fatty acids,
important constituents of plant membranes (PubMed:14593172,
PubMed:7907506). Delta(12)-desaturase with regioselectivity
determined by the double bond (delta(9) position) and carboxyl
group of the substrate. Can use both 16:1 and 18:1 fatty acids as
substrates (PubMed:8685264). It is thought to use cytochrome b5 as
an electron donor and to act on fatty acids esterified to
phosphatidylcholine (PC) and, possibly, other phospholipids
(PubMed:14593172, PubMed:7907506, PubMed:1730697). Very low
constitutive hydroxylation activity (PubMed:11864983). Required
for desaturation of fatty acids present in extraplastidial
membranes, including mitochondria (PubMed:11104757,
PubMed:17507388). Required for salt tolerance during seed
germination and early seedling growth (PubMed:22279586).
{ECO:0000269|PubMed:11104757, ECO:0000269|PubMed:11864983,
ECO:0000269|PubMed:14593172, ECO:0000269|PubMed:1730697,
ECO:0000269|PubMed:17507388, ECO:0000269|PubMed:22279586,
ECO:0000269|PubMed:7907506, ECO:0000269|PubMed:8685264}.
-!- CATALYTIC ACTIVITY: Oleoyl-CoA + 2 ferrocytochrome b5 + O(2) + 2
H(+) = linoleoyl-CoA + 2 ferricytochrome b5 + 2 H(2)O.
{ECO:0000269|PubMed:8685264}.
-!- CATALYTIC ACTIVITY: Palmitoleoyl-CoA + 2 ferrocytochrome b5 + O(2)
+ 2 H(+) = (9Z,12Z)-hexadeca-9,12-dienoyl-CoA + 2 ferricytochrome
b5 + 2 H(2)O. {ECO:0000269|PubMed:8685264}.
-!- CATALYTIC ACTIVITY: An oleoyl-[glycerolipid] + 2 ferrocytochrome
b5 + O(2) + 2 H(+) = a linoleoyl-[glycerolipid] + 2
ferricytochrome b5 + 2 H(2)O. {ECO:0000269|PubMed:1730697}.
-!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid
biosynthesis.
-!- SUBUNIT: Homo- and heterodimer (PubMed:24811169). Interacts with
FAD3 but not with FAD6 (PubMed:24811169). FAD2-FAD3 heterodimers
can form a metabolic channel in which 18:1-PC is converted to
18:3-PC without releasing a free 18:2-PC intermediate
(PubMed:24811169). {ECO:0000269|PubMed:24811169}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:14690501, ECO:0000305|PubMed:7907506}; Multi-
pass membrane protein {ECO:0000255}. Microsome membrane
{ECO:0000269|PubMed:1730697}; Multi-pass membrane protein
{ECO:0000255}.
-!- TISSUE SPECIFICITY: Expressed in shoots and roots (PubMed:7907506,
PubMed:22279586). Expressed in leaves, stems, flowers and siliques
(PubMed:22279586). {ECO:0000269|PubMed:22279586,
ECO:0000269|PubMed:7907506}.
-!- INDUCTION: Up-regulated by osmotic stress (PubMed:22279586). Not
regulated by cold stress (PubMed:7907506).
{ECO:0000269|PubMed:22279586, ECO:0000269|PubMed:7907506}.
-!- DOMAIN: The histidine box domains may contain the active site
and/or be involved in metal ion binding (Probable). The C-terminal
sequence (-YNNKL) is necessary and sufficient for maintaining
localization in the endoplasmic reticulum (PubMed:14690501).
{ECO:0000269|PubMed:14690501, ECO:0000305|PubMed:7907506}.
-!- DISRUPTION PHENOTYPE: Enhancement of both microviscosity and
lipid/protein ratio of mitochondrial membranes, which in turn were
responsible for the change in lateral mobility of lipids and for
bioenergetic parameter modifications (PubMed:11104757). Increased
membrane rigidity and cold sensitivity (PubMed:17507388).
Hypersensitivity to salt or osmotic stress (PubMed:22279586).
{ECO:0000269|PubMed:11104757, ECO:0000269|PubMed:17507388,
ECO:0000269|PubMed:22279586}.
-!- MISCELLANEOUS: Introduction of Ile at position 146 or 324 has a
dominant role in specifying hydroxylation activity.
{ECO:0000269|PubMed:11864983}.
-!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
{ECO:0000305}.
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EMBL; L26296; AAA32782.1; -; mRNA.
EMBL; AP002063; BAB01960.1; -; Genomic_DNA.
EMBL; AC069473; AAG51042.1; -; Genomic_DNA.
EMBL; CP002686; AEE75152.1; -; Genomic_DNA.
EMBL; CP002686; AEE75153.1; -; Genomic_DNA.
EMBL; AY039572; AAK62627.1; -; mRNA.
EMBL; AY142057; AAM98321.1; -; mRNA.
RefSeq; NP_001319529.1; NM_001337975.1.
RefSeq; NP_187819.1; NM_112047.4.
UniGene; At.23898; -.
UniGene; At.50826; -.
UniGene; At.66993; -.
ProteinModelPortal; P46313; -.
BioGrid; 5721; 2.
STRING; 3702.AT3G12120.1; -.
SwissLipids; SLP:000000808; -.
PaxDb; P46313; -.
EnsemblPlants; AT3G12120.1; AT3G12120.1; AT3G12120.
EnsemblPlants; AT3G12120.2; AT3G12120.2; AT3G12120.
GeneID; 820387; -.
Gramene; AT3G12120.1; AT3G12120.1; AT3G12120.
Gramene; AT3G12120.2; AT3G12120.2; AT3G12120.
KEGG; ath:AT3G12120; -.
Araport; AT3G12120; -.
TAIR; locus:2099297; AT3G12120.
eggNOG; ENOG410IFN9; Eukaryota.
eggNOG; COG3239; LUCA.
HOGENOM; HOG000201905; -.
InParanoid; P46313; -.
KO; K10256; -.
OMA; HWLVFIT; -.
OrthoDB; EOG09360ANT; -.
PhylomeDB; P46313; -.
BioCyc; MetaCyc:AT3G12120-MONOMER; -.
UniPathway; UPA00658; -.
PRO; PR:P46313; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; P46313; baseline and differential.
Genevisible; P46313; AT.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0102985; F:Delta12-fatty-acid desaturase activity; IEA:UniProtKB-EC.
GO; GO:0045485; F:omega-6 fatty acid desaturase activity; IDA:TAIR.
GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
InterPro; IPR005804; FA_desaturase_dom.
InterPro; IPR021863; FAS_N.
Pfam; PF11960; DUF3474; 1.
Pfam; PF00487; FA_desaturase; 1.
1: Evidence at protein level;
Complete proteome; Endoplasmic reticulum; Fatty acid biosynthesis;
Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Membrane;
Microsome; Oxidoreductase; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 383 Delta(12)-fatty-acid desaturase.
/FTId=PRO_0000185418.
TRANSMEM 56 76 Helical. {ECO:0000255}.
TRANSMEM 117 137 Helical. {ECO:0000255}.
TRANSMEM 179 199 Helical. {ECO:0000255}.
TRANSMEM 225 245 Helical. {ECO:0000255}.
TRANSMEM 252 272 Helical. {ECO:0000255}.
MOTIF 105 109 Histidine box-1. {ECO:0000305}.
MOTIF 141 145 Histidine box-2. {ECO:0000305}.
MOTIF 315 319 Histidine box-3. {ECO:0000305}.
MUTAGEN 63 63 A->V: In m7FAD2/L7M; Converted from a
desaturase to a bifunctional
desaturase/hydroxylase; when associated
with G-104; N-148; F-217; V-295; A-322
and I-324. {ECO:0000269|PubMed:9812895}.
MUTAGEN 104 104 A->G: Produces less than 1% hydroxy fatty
acid. In m7FAD2/L7M; Converted from a
desaturase to a bifunctional
desaturase/hydroxylase; when associated
with V-63; N-148; F-217; V-295; A-322 and
I-324. In C4M; Converted from a
desaturase to a bifunctional
desaturase/hydroxylase with a high
hydroxylase activity; when associated
with I-148; A-322 and V-324.
{ECO:0000269|PubMed:11864983,
ECO:0000269|PubMed:9812895}.
MUTAGEN 104 104 A->T: Increased monounsaturated and
decreased polyunsaturated fatty acid
levels. {ECO:0000269|PubMed:22279586}.
MUTAGEN 148 148 T->I: Produces up to 4.2% hydroxy fatty
acid. In C4M; Converted from a desaturase
to a bifunctional desaturase/hydroxylase
with a high hydroxylase activity; when
associated with G-104; A-322 and V-324.
{ECO:0000269|PubMed:11864983}.
MUTAGEN 148 148 T->N: Produces less than 1% hydroxy fatty
acid. In m7FAD2/L7M; Converted from a
desaturase to a bifunctional
desaturase/hydroxylase; when associated
with V-63; G-104; F-217; V-295; A-322 and
I-324. In m4FAD2/L4M; Converted from a
desaturase to a bifunctional
desaturase/hydroxylase; when associated
with V-295; A-322 and I-324.
{ECO:0000269|PubMed:11864983,
ECO:0000269|PubMed:9812895}.
MUTAGEN 217 217 Y->F: In m7FAD2/L7M; Converted from a
desaturase to a bifunctional
desaturase/hydroxylase; when associated
with V-63; G-104; N-148; V-295; A-322 and
I-324. {ECO:0000269|PubMed:9812895}.
MUTAGEN 295 295 A->V: In m7FAD2/L7M; Converted from a
desaturase to a bifunctional
desaturase/hydroxylase; when associated
with V-63; G-104; N-148; F-217; A-322 and
I-324. In m4FAD2/L4M; Converted from a
desaturase to a bifunctional
desaturase/hydroxylase; when associated
with N-148; A-322 and I-324.
{ECO:0000269|PubMed:9812895}.
MUTAGEN 322 322 S->A: Produces less than 1% hydroxy fatty
acid. In m7FAD2/L7M; Converted from a
desaturase to a bifunctional
desaturase/hydroxylase; when associated
with V-63; G-104; N-148; F-217; V-295 and
I-324. In m4FAD2/L4M; Converted from a
desaturase to a bifunctional
desaturase/hydroxylase; when associated
with N-148; V-295 and I-324. In C4M;
Converted from a desaturase to a
bifunctional desaturase/hydroxylase with
a high hydroxylase activity; when
associated with G-104; I-148 and V-324.
{ECO:0000269|PubMed:11864983,
ECO:0000269|PubMed:9812895}.
MUTAGEN 324 324 M->I: Produces up to 5.4% hydroxy fatty
acid. In m7FAD2/L7M; Converted from a
desaturase to a bifunctional
desaturase/hydroxylase; when associated
with V-63; G-104; N-148; F-217; V-295 and
A-322. In m4FAD2/L4M; Converted from a
desaturase to a bifunctional
desaturase/hydroxylase; when associated
with N-148; V-295 and A-322.
{ECO:0000269|PubMed:11864983,
ECO:0000269|PubMed:9812895}.
MUTAGEN 324 324 M->V: In C4M; Converted from a desaturase
to a bifunctional desaturase/hydroxylase
with a high hydroxylase activity; when
associated with G-104; I-148 and A-322.
{ECO:0000269|PubMed:11864983}.
MUTAGEN 335 335 A->T: In sve1; Altered fatty acid
composition and suppresses the low
temperature-induced phenotype of
tocopherol-deficient mutant.
{ECO:0000269|PubMed:20345604}.
SEQUENCE 383 AA; 44048 MW; 8815ADD2D3BBC982 CRC64;
MGAGGRMPVP TSSKKSETDT TKRVPCEKPP FSVGDLKKAI PPHCFKRSIP RSFSYLISDI
IIASCFYYVA TNYFSLLPQP LSYLAWPLYW ACQGCVLTGI WVIAHECGHH AFSDYQWLDD
TVGLIFHSFL LVPYFSWKYS HRRHHSNTGS LERDEVFVPK QKSAIKWYGK YLNNPLGRIM
MLTVQFVLGW PLYLAFNVSG RPYDGFACHF FPNAPIYNDR ERLQIYLSDA GILAVCFGLY
RYAAAQGMAS MICLYGVPLL IVNAFLVLIT YLQHTHPSLP HYDSSEWDWL RGALATVDRD
YGILNKVFHN ITDTHVAHHL FSTMPHYNAM EATKAIKPIL GDYYQFDGTP WYVAMYREAK
ECIYVEPDRE GDKKGVYWYN NKL


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20-272-191926 SCD - Mouse monoclonal [CD.E10] to SCD; EC 1.14.19.1; Stearoyl-CoA desaturase; Fatty acid desaturase; Delta(9)-desaturase Monoclonal 0.1 mg
FADS21-A Anti-Mouse Fatty acid desaturase 2 (FADS2 delta-6 desaturase) IgG aff pure 100 ug
FADS21-P Mouse Fatty acid desaturase 2 (FADS2 delta-6 desaturase) Control blocking peptide 100 ug
27-711 Stearoyl-CoA desaturase ( fatty acid desaturase, SCD) is expressed at high levels in several human tissues and is required for the biosynthesis of oleate (18 1) and palmitoleate (16 1). These monounsa 0.1 mg
FADS21-A Anti-Mouse Fatty acid desaturase 2 (FADS2_delta-6 desaturase) IgG aff pure Species Reactivity: Mouse 100 ug Product tipe: Antibodies
FADS21-P Mouse Fatty acid desaturase 2 (FADS2_delta-6 desaturase) Control_blocking peptide Species Reactivity: Mouse 100 ug Product tipe: Peptide
26-055 DEGS1 is a member of the membrane fatty acid desaturase family which is responsible for inserting double bonds into specific positions in fatty acids. This protein contains three His-containing consen 0.05 mg
FADS21-A Fatty acid desaturase 2 0.1 mg
FADS22-A Fatty acid desaturase 2 0.1 mg
FADS32-A Fatty acid desaturase 3 0.1 mg
FADS12-A Fatty acid desaturase 1 (FADS1) 0.1 mg
EB07568 Fatty acid desaturase 1 (FADS1) 0.1 mg
ARP42383_P050 Fatty acid desaturase 1 (FADS1) 50 µg
FADS12-A Fatty acid desaturase 1 (FADS1) 0.1 mg
EH885 Fatty acid desaturase 2 Elisa Kit 96T


 

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