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Platelet-activating factor acetylhydrolase IB subunit alpha (Lissencephaly-1 protein) (LIS-1) (PAF acetylhydrolase 45 kDa subunit) (PAF-AH 45 kDa subunit) (PAF-AH alpha) (PAFAH alpha)

 Q5SW18_MOUSE            Unreviewed;       410 AA.
Q5SW18;
10-MAY-2005, integrated into UniProtKB/TrEMBL.
10-MAY-2005, sequence version 1.
28-MAR-2018, entry version 137.
RecName: Full=Platelet-activating factor acetylhydrolase IB subunit alpha {ECO:0000256|HAMAP-Rule:MF_03141};
AltName: Full=Lissencephaly-1 protein {ECO:0000256|HAMAP-Rule:MF_03141};
Short=LIS-1 {ECO:0000256|HAMAP-Rule:MF_03141};
AltName: Full=PAF acetylhydrolase 45 kDa subunit {ECO:0000256|HAMAP-Rule:MF_03141};
Short=PAF-AH 45 kDa subunit {ECO:0000256|HAMAP-Rule:MF_03141};
AltName: Full=PAF-AH alpha {ECO:0000256|HAMAP-Rule:MF_03141};
Short=PAFAH alpha {ECO:0000256|HAMAP-Rule:MF_03141};
Name=Pafah1b1 {ECO:0000313|MGI:MGI:109520};
Synonyms=LIS1 {ECO:0000256|HAMAP-Rule:MF_03141},
PAFAH1B1 {ECO:0000256|HAMAP-Rule:MF_03141};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000313|EMBL:BAE27977.1};
[1] {ECO:0000313|EMBL:BAE27977.1}
NUCLEOTIDE SEQUENCE.
STRAIN=C57BL/6 {ECO:0000313|EMBL:BAE27977.1}, and
C57BL/6J {ECO:0000313|EMBL:BAE27764.1};
TISSUE=Amnion {ECO:0000313|EMBL:BAE40742.1},
Brain {ECO:0000313|EMBL:BAE27977.1},
Mammary gland {ECO:0000313|EMBL:BAE26129.1},
Stomach {ECO:0000313|EMBL:BAE40766.1}, and
Whole body {ECO:0000313|EMBL:BAE27764.1};
PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
Carninci P., Hayashizaki Y.;
"High-efficiency full-length cDNA cloning.";
Methods Enzymol. 303:19-44(1999).
[2] {ECO:0000313|EMBL:BAE27977.1}
NUCLEOTIDE SEQUENCE.
STRAIN=C57BL/6 {ECO:0000313|EMBL:BAE27977.1}, and
C57BL/6J {ECO:0000313|EMBL:BAE27764.1};
TISSUE=Amnion {ECO:0000313|EMBL:BAE40742.1},
Brain {ECO:0000313|EMBL:BAE27977.1},
Mammary gland {ECO:0000313|EMBL:BAE26129.1},
Stomach {ECO:0000313|EMBL:BAE40766.1}, and
Whole body {ECO:0000313|EMBL:BAE27764.1};
PubMed=11042159; DOI=10.1101/gr.145100;
Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
"Normalization and subtraction of cap-trapper-selected cDNAs to
prepare full-length cDNA libraries for rapid discovery of new genes.";
Genome Res. 10:1617-1630(2000).
[3] {ECO:0000313|EMBL:BAE27977.1}
NUCLEOTIDE SEQUENCE.
STRAIN=C57BL/6 {ECO:0000313|EMBL:BAE27977.1}, and
C57BL/6J {ECO:0000313|EMBL:BAE27764.1};
TISSUE=Amnion {ECO:0000313|EMBL:BAE40742.1},
Brain {ECO:0000313|EMBL:BAE27977.1},
Mammary gland {ECO:0000313|EMBL:BAE26129.1},
Stomach {ECO:0000313|EMBL:BAE40766.1}, and
Whole body {ECO:0000313|EMBL:BAE27764.1};
PubMed=11076861; DOI=10.1101/gr.152600;
Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
"RIKEN integrated sequence analysis (RISA) system--384-format
sequencing pipeline with 384 multicapillary sequencer.";
Genome Res. 10:1757-1771(2000).
[4] {ECO:0000313|EMBL:BAE27977.1}
NUCLEOTIDE SEQUENCE.
STRAIN=C57BL/6 {ECO:0000313|EMBL:BAE27977.1}, and
C57BL/6J {ECO:0000313|EMBL:BAE27764.1};
TISSUE=Amnion {ECO:0000313|EMBL:BAE40742.1},
Brain {ECO:0000313|EMBL:BAE27977.1},
Mammary gland {ECO:0000313|EMBL:BAE26129.1},
Stomach {ECO:0000313|EMBL:BAE40766.1}, and
Whole body {ECO:0000313|EMBL:BAE27764.1};
PubMed=11217851; DOI=10.1038/35055500;
The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
"Functional annotation of a full-length mouse cDNA collection.";
Nature 409:685-690(2001).
[5] {ECO:0000313|EMBL:BAE27977.1}
NUCLEOTIDE SEQUENCE.
STRAIN=C57BL/6 {ECO:0000313|EMBL:BAE27977.1}, and
C57BL/6J {ECO:0000313|EMBL:BAE27764.1};
TISSUE=Amnion {ECO:0000313|EMBL:BAE40742.1},
Brain {ECO:0000313|EMBL:BAE27977.1},
Mammary gland {ECO:0000313|EMBL:BAE26129.1},
Stomach {ECO:0000313|EMBL:BAE40766.1}, and
Whole body {ECO:0000313|EMBL:BAE27764.1};
PubMed=12466851; DOI=10.1038/nature01266;
The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
"Analysis of the mouse transcriptome based on functional annotation of
60,770 full-length cDNAs.";
Nature 420:563-573(2002).
[6] {ECO:0000313|EMBL:BAE27977.1}
NUCLEOTIDE SEQUENCE.
STRAIN=C57BL/6 {ECO:0000313|EMBL:BAE27977.1}, and
C57BL/6J {ECO:0000313|EMBL:BAE27764.1};
TISSUE=Brain {ECO:0000313|EMBL:BAE27977.1},
Mammary gland {ECO:0000313|EMBL:BAE26129.1}, and
Whole body {ECO:0000313|EMBL:BAE27764.1};
Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
Muramatsu M., Hayashizaki Y.;
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[7] {ECO:0000313|EMBL:BAE37586.1}
NUCLEOTIDE SEQUENCE.
STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE37586.1};
TISSUE=Amnion {ECO:0000313|EMBL:BAE40742.1},
Stomach {ECO:0000313|EMBL:BAE40766.1}, and
Whole body {ECO:0000313|EMBL:BAE37586.1};
Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
Muramatsu M., Hayashizaki Y.;
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[8] {ECO:0000313|EMBL:BAE27977.1}
NUCLEOTIDE SEQUENCE.
STRAIN=C57BL/6 {ECO:0000313|EMBL:BAE27977.1}, and
C57BL/6J {ECO:0000313|EMBL:BAE27764.1};
TISSUE=Amnion {ECO:0000313|EMBL:BAE40742.1},
Brain {ECO:0000313|EMBL:BAE27977.1},
Mammary gland {ECO:0000313|EMBL:BAE26129.1},
Stomach {ECO:0000313|EMBL:BAE40766.1}, and
Whole body {ECO:0000313|EMBL:BAE27764.1};
The FANTOM Consortium;
Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
"The Transcriptional Landscape of the Mammalian Genome.";
Science 309:1559-1563(2005).
[9] {ECO:0000313|EMBL:BAE27977.1}
NUCLEOTIDE SEQUENCE.
STRAIN=C57BL/6 {ECO:0000313|EMBL:BAE27977.1}, and
C57BL/6J {ECO:0000313|EMBL:BAE27764.1};
TISSUE=Amnion {ECO:0000313|EMBL:BAE40742.1},
Brain {ECO:0000313|EMBL:BAE27977.1},
Mammary gland {ECO:0000313|EMBL:BAE26129.1},
Stomach {ECO:0000313|EMBL:BAE40766.1}, and
Whole body {ECO:0000313|EMBL:BAE27764.1};
PubMed=16141073; DOI=10.1126/science.1112009;
RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
"Antisense Transcription in the Mammalian Transcriptome.";
Science 309:1564-1566(2005).
-!- FUNCTION: Positively regulates the activity of the minus-end
directed microtubule motor protein dynein. May enhance dynein-
mediated microtubule sliding by targeting dynein to the
microtubule plus end. Required for several dynein- and
microtubule-dependent processes such as the maintenance of Golgi
integrity, the peripheral transport of microtubule fragments and
the coupling of the nucleus and centrosome. Required during brain
development for the proliferation of neuronal precursors and the
migration of newly formed neurons from the
ventricular/subventricular zone toward the cortical plate.
Neuronal migration involves a process called nucleokinesis,
whereby migrating cells extend an anterior process into which the
nucleus subsequently translocates. During nucleokinesis dynein at
the nuclear surface may translocate the nucleus towards the
centrosome by exerting force on centrosomal microtubules. Also
required for proper activation of Rho GTPases and actin
polymerization at the leading edge of locomoting cerebellar
neurons and postmigratory hippocampal neurons in response to
calcium influx triggered via NMDA receptors. May also play a role
in other forms of cell locomotion including the migration of
fibroblasts during wound healing. Non-catalytic subunit of an
acetylhydrolase complex which inactivates platelet-activating
factor (PAF) by removing the acetyl group at the SN-2 position.
{ECO:0000256|HAMAP-Rule:MF_03141}.
-!- SUBUNIT: Can self-associate. Interacts with DCX, dynein, dynactin,
IQGAP1, KATNB1, NDE1, NDEL1, NUDC and RSN. Interacts with DISC1,
and this interaction is enhanced by NDEL1. Interacts with DAB1
when DAB1 is phosphorylated in response to RELN/reelin signaling.
Component of cytosolic PAF-AH IB, which is composed of PAFAH1B1
(alpha), PAFAH1B2 (beta) and PAFAH1B3 (gamma) subunits. Trimer
formation is not essential for the catalytic activity of the
enzyme which is contributed solely by the PAFAH1B2 (beta) and
PAFAH1B3 (gamma) subunits. {ECO:0000256|HAMAP-Rule:MF_03141}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000256|HAMAP-
Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing
center, centrosome {ECO:0000256|HAMAP-Rule:MF_03141}. Cytoplasm,
cytoskeleton, spindle {ECO:0000256|HAMAP-Rule:MF_03141}. Nucleus
membrane {ECO:0000256|HAMAP-Rule:MF_03141}. Note=Localizes to the
plus end of microtubules and to the centrosome. May localize to
the nuclear membrane. Redistributes to axons during neuronal
development. Also localizes to the microtubules of the manchette
in elongating spermatids and to the meiotic spindle in
spermatocytes. {ECO:0000256|HAMAP-Rule:MF_03141}.
-!- DOMAIN: Dimerization mediated by the LisH domain may be required
to activate dynein. {ECO:0000256|HAMAP-Rule:MF_03141}.
-!- SIMILARITY: Belongs to the WD repeat LIS1/nudF family.
{ECO:0000256|HAMAP-Rule:MF_03141, ECO:0000256|SAAS:SAAS00638756}.
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EMBL; AK144908; BAE26129.1; -; mRNA.
EMBL; AK147207; BAE27764.1; -; mRNA.
EMBL; AK147237; BAE27787.1; -; mRNA.
EMBL; AK147507; BAE27961.1; -; mRNA.
EMBL; AK147533; BAE27977.1; -; mRNA.
EMBL; AK164008; BAE37586.1; -; mRNA.
EMBL; AK168929; BAE40742.1; -; mRNA.
EMBL; AK168960; BAE40766.1; -; mRNA.
RefSeq; NP_038653.1; NM_013625.4.
UniGene; Mm.397111; -.
GeneID; 18472; -.
KEGG; mmu:18472; -.
CTD; 5048; -.
MGI; MGI:109520; Pafah1b1.
eggNOG; KOG0295; Eukaryota.
eggNOG; ENOG410XP3K; LUCA.
HOVERGEN; HBG006271; -.
KO; K16794; -.
OMA; DAHGHFV; -.
OrthoDB; EOG091G07Q1; -.
ChiTaRS; Pafah1b1; mouse.
Bgee; ENSMUSG00000020745; -.
GO; GO:0000235; C:astral microtubule; IEA:Ensembl.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0005938; C:cell cortex; IEA:Ensembl.
GO; GO:0090724; C:central region of growth cone; IEA:Ensembl.
GO; GO:0005813; C:centrosome; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005871; C:kinesin complex; IEA:Ensembl.
GO; GO:0000776; C:kinetochore; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0031982; C:vesicle; IEA:Ensembl.
GO; GO:0070840; F:dynein complex binding; IEA:UniProtKB-UniRule.
GO; GO:0045505; F:dynein intermediate chain binding; IEA:Ensembl.
GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
GO; GO:0048854; P:brain morphogenesis; IEA:Ensembl.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0021895; P:cerebral cortex neuron differentiation; IEA:Ensembl.
GO; GO:0021540; P:corpus callosum morphogenesis; IEA:Ensembl.
GO; GO:0051660; P:establishment of centrosome localization; IEA:Ensembl.
GO; GO:0000132; P:establishment of mitotic spindle orientation; IEA:UniProtKB-UniRule.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0031023; P:microtubule organizing center organization; IEA:Ensembl.
GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
GO; GO:0001764; P:neuron migration; IEA:Ensembl.
GO; GO:0007097; P:nuclear migration; IEA:Ensembl.
GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:Ensembl.
GO; GO:0017145; P:stem cell division; IEA:Ensembl.
Gene3D; 2.130.10.10; -; 1.
HAMAP; MF_03141; lis1; 1.
InterPro; IPR017252; Dynein_regulator_LIS1.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR037190; LIS1_N.
InterPro; IPR006594; LisH.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF08513; LisH; 1.
Pfam; PF00400; WD40; 7.
PIRSF; PIRSF037647; Dynein_regulator_Lis1; 1.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00667; LisH; 1.
SMART; SM00320; WD40; 7.
SUPFAM; SSF109925; SSF109925; 1.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS50896; LISH; 1.
PROSITE; PS00678; WD_REPEATS_1; 4.
PROSITE; PS50082; WD_REPEATS_2; 7.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
2: Evidence at transcript level;
Cell cycle {ECO:0000256|HAMAP-Rule:MF_03141,
ECO:0000256|SAAS:SAAS00638754};
Cell division {ECO:0000256|HAMAP-Rule:MF_03141,
ECO:0000256|SAAS:SAAS00638754};
Coiled coil {ECO:0000256|HAMAP-Rule:MF_03141,
ECO:0000256|SAAS:SAAS00638762, ECO:0000256|SAM:Coils};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03141,
ECO:0000256|SAAS:SAAS00638741};
Cytoskeleton {ECO:0000256|HAMAP-Rule:MF_03141,
ECO:0000256|SAAS:SAAS00638741};
Developmental protein {ECO:0000256|HAMAP-Rule:MF_03141};
Differentiation {ECO:0000256|HAMAP-Rule:MF_03141};
Lipid degradation {ECO:0000256|HAMAP-Rule:MF_03141};
Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03141};
Membrane {ECO:0000256|HAMAP-Rule:MF_03141};
Microtubule {ECO:0000256|HAMAP-Rule:MF_03141,
ECO:0000256|SAAS:SAAS00638742};
Mitosis {ECO:0000256|HAMAP-Rule:MF_03141,
ECO:0000256|SAAS:SAAS00638754};
Neurogenesis {ECO:0000256|HAMAP-Rule:MF_03141};
Nucleus {ECO:0000256|HAMAP-Rule:MF_03141};
Repeat {ECO:0000256|SAAS:SAAS00998418};
Transport {ECO:0000256|HAMAP-Rule:MF_03141,
ECO:0000256|SAAS:SAAS00638761};
WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221,
ECO:0000256|SAAS:SAAS00998547}.
INIT_MET 1 1 Removed. {ECO:0000256|HAMAP-
Rule:MF_03141}.
DOMAIN 7 39 LisH. {ECO:0000259|PROSITE:PS50896}.
DOMAIN 104 410 WD_REPEATS_REGION.
{ECO:0000259|PROSITE:PS50294}.
REPEAT 104 145 WD. {ECO:0000256|PROSITE-
ProRule:PRU00221}.
REPEAT 146 187 WD. {ECO:0000256|PROSITE-
ProRule:PRU00221}.
REPEAT 188 229 WD. {ECO:0000256|PROSITE-
ProRule:PRU00221}.
REPEAT 230 271 WD. {ECO:0000256|PROSITE-
ProRule:PRU00221}.
REPEAT 308 333 WD. {ECO:0000256|PROSITE-
ProRule:PRU00221}.
REPEAT 334 375 WD. {ECO:0000256|PROSITE-
ProRule:PRU00221}.
REPEAT 376 410 WD. {ECO:0000256|PROSITE-
ProRule:PRU00221}.
REGION 1 102 Interaction with NDEL1.
{ECO:0000256|HAMAP-Rule:MF_03141}.
REGION 1 66 Interaction with NDE1.
{ECO:0000256|HAMAP-Rule:MF_03141}.
REGION 1 38 Required for self-association and
interaction with PAFAH1B2 and PAFAH1B3.
{ECO:0000256|HAMAP-Rule:MF_03141}.
REGION 83 410 Interaction with dynein and dynactin.
{ECO:0000256|HAMAP-Rule:MF_03141}.
REGION 388 410 Interaction with NDEL1.
{ECO:0000256|HAMAP-Rule:MF_03141}.
COILED 58 78 {ECO:0000256|SAM:Coils}.
SEQUENCE 410 AA; 46670 MW; 4DBF6A24A6B131CD CRC64;
MVLSQRQRDE LNRAIADYLR SNGYEEAYSV FKKEAELDMN EELDKKYAGL LEKKWTSVIR
LQKKVMELES KLNEAKEEFT SGGPLGQKRD PKEWIPRPPE KYALSGHRSP VTRVIFHPVF
SVMVSASEDA TIKVWDYETG DFERTLKGHT DSVQDISFDH SGKLLASCSA DMTIKLWDFQ
GFECIRTMHG HDHNVSSVAI MPNGDHIVSA SRDKTIKMWE VQTGYCVKTF TGHREWVRMV
RPNQDGTLIA SCSNDQTVRV WVVATKECKA ELREHEHVVE CISWAPESSY SSISEATGSE
TKKSGKPGPF LLSGSRDKTI KMWDVSTGMC LMTLVGHDNW VRGVLFHSGG KFILSCADDK
TLRVWDYKNK RCMKTLNAHE HFVTSLDFHK TAPYVVTGSV DQTVKVWECR


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E0526m ELISA kit Lis1,LIS-1,Lis-1,Lissencephaly-1 protein,Mouse,Mus musculus,PAF acetylhydrolase 45 kDa subunit,PAF-AH 45 kDa subunit,PAFAH alpha,PAF-AH alpha,Pafah1b1,Pafaha,Platelet-activating factor acet 96T
E0526m ELISA Lis1,LIS-1,Lis-1,Lissencephaly-1 protein,Mouse,Mus musculus,PAF acetylhydrolase 45 kDa subunit,PAF-AH 45 kDa subunit,PAFAH alpha,PAF-AH alpha,Pafah1b1,Pafaha,Platelet-activating factor acetylhyd 96T
E0526h ELISA kit Homo sapiens,Human,LIS1,LIS-1,Lissencephaly-1 protein,MDCR,MDS,PAF acetylhydrolase 45 kDa subunit,PAF-AH 45 kDa subunit,PAFAH alpha,PAF-AH alpha,PAFAH1B1,PAFAHA,Platelet-activating factor a 96T
E0526h ELISA Homo sapiens,Human,LIS1,LIS-1,Lissencephaly-1 protein,MDCR,MDS,PAF acetylhydrolase 45 kDa subunit,PAF-AH 45 kDa subunit,PAFAH alpha,PAF-AH alpha,PAFAH1B1,PAFAHA,Platelet-activating factor acetyl 96T
U0526h CLIA Homo sapiens,Human,LIS1,LIS-1,Lissencephaly-1 protein,MDCR,MDS,PAF acetylhydrolase 45 kDa subunit,PAF-AH 45 kDa subunit,PAFAH alpha,PAF-AH alpha,PAFAH1B1,PAFAHA,Platelet-activating factor acetylh 96T
EIAAB29615 PAF acetylhydrolase 30 kDa subunit,PAF-AH 30 kDa subunit,PAF-AH alpha 2,PAFAH subunit beta,PAF-AH subunit beta,Pafah1b2,Pafahb,Platelet-activating factor acetylhydrolase alpha 2 subunit,Platelet-activ
EIAAB29616 PAF acetylhydrolase 29 kDa subunit,PAF-AH 29 kDa subunit,PAF-AH alpha 1,PAFAH subunit gamma,PAF-AH subunit gamma,Pafah1b3,Pafahg,Platelet-activating factor acetylhydrolase alpha 1 subunit,Platelet-act
EIAAB29619 Homo sapiens,Human,PAF acetylhydrolase 29 kDa subunit,PAF-AH 29 kDa subunit,PAFAH subunit gamma,PAF-AH subunit gamma,PAFAH1B3,PAFAHG,Platelet-activating factor acetylhydrolase IB subunit gamma
EIAAB29611 Homo sapiens,Human,PAF acetylhydrolase 30 kDa subunit,PAF-AH 30 kDa subunit,PAFAH subunit beta,PAF-AH subunit beta,PAFAH1B2,PAFAHB,Platelet-activating factor acetylhydrolase IB subunit beta
EIAAB29617 Bos taurus,Bovine,PAF acetylhydrolase 29 kDa subunit,PAF-AH 29 kDa subunit,PAFAH subunit gamma,PAF-AH subunit gamma,PAFAH1B3,PAFAHG,Platelet-activating factor acetylhydrolase IB subunit gamma
EIAAB29612 Mouse,Mus musculus,PAF acetylhydrolase 30 kDa subunit,PAF-AH 30 kDa subunit,PAFAH subunit beta,PAF-AH subunit beta,Pafah1b2,Pafahb,Platelet-activating factor acetylhydrolase IB subunit beta
EIAAB29614 Bos taurus,Bovine,PAF acetylhydrolase 30 kDa subunit,PAF-AH 30 kDa subunit,PAFAH subunit beta,PAF-AH subunit beta,PAFAH1B2,PAFAHB,Platelet-activating factor acetylhydrolase IB subunit beta
EIAAB29618 Mouse,Mus musculus,PAF acetylhydrolase 29 kDa subunit,PAF-AH 29 kDa subunit,PAFAH subunit gamma,PAF-AH subunit gamma,Pafah1b3,Pafahg,Platelet-activating factor acetylhydrolase IB subunit gamma
EIAAB29613 Chicken,Gallus gallus,PAF acetylhydrolase 30 kDa subunit,PAF-AH 30 kDa subunit,PAFAH subunit beta,PAF-AH subunit beta,PAFAH1B2,PAFAHB,Platelet-activating factor acetylhydrolase IB subunit beta,RCJMB04
15-288-22423F Platelet-activating factor acetylhydrolase IB subunit beta - EC 3.1.1.47; PAF acetylhydrolase 30 kDa subunit; PAF-AH 30 kDa subunit; PAF-AH subunit beta; PAFAH subunit beta Polyclonal 0.1 mg


 

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