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Endothelial PAS domain-containing protein 1 (EPAS-1) (HIF-1-alpha-like factor) (HLF) (mHLF) (HIF-related factor) (HRF) (Hypoxia-inducible factor 2-alpha) (HIF-2-alpha) (HIF2-alpha)

 EPAS1_MOUSE             Reviewed;         874 AA.
P97481; O08787; O55046;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 2.
20-JUN-2018, entry version 166.
RecName: Full=Endothelial PAS domain-containing protein 1;
Short=EPAS-1;
AltName: Full=HIF-1-alpha-like factor;
Short=HLF;
Short=mHLF;
AltName: Full=HIF-related factor;
Short=HRF;
AltName: Full=Hypoxia-inducible factor 2-alpha;
Short=HIF-2-alpha;
Short=HIF2-alpha;
Name=Epas1; Synonyms=Hif2a;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=9000051; DOI=10.1101/gad.11.1.72;
Tian H., McKnight S.L., Russell D.W.;
"Endothelial PAS domain protein 1 (EPAS1), a transcription factor
selectively expressed in endothelial cells.";
Genes Dev. 11:72-82(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Hypothalamus, and Skeletal muscle;
PubMed=9113979; DOI=10.1073/pnas.94.9.4273;
Ema M., Taya S., Yokotani N., Sogawa K., Matsuda Y.,
Fujii-Kuriyama Y.;
"A novel bHLH-PAS factor with close sequence similarity to hypoxia-
inducible factor 1alpha regulates the VEGF expression and is
potentially involved in lung and vascular development.";
Proc. Natl. Acad. Sci. U.S.A. 94:4273-4278(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain capillary;
PubMed=9178256; DOI=10.1016/S0925-4773(97)00674-6;
Flamme I., Froehlich T., von Reutern M., Kappel A., Damert A.,
Risau W.;
"HRF, a putative basic helix-loop-helix-PAS-domain transcription
factor is closely related to hypoxia-inducible factor-1 alpha and
developmentally expressed in blood vessels.";
Mech. Dev. 63:51-60(1997).
[4]
PROTEIN SEQUENCE OF 846-864, AND MUTAGENESIS OF PRO-530 AND ASN-851.
PubMed=12080085; DOI=10.1101/gad.991402;
Lando D., Peet D.J., Gorman J.J., Whelan D.A., Whitelaw M.L.,
Bruick R.K.;
"FIH-1 is an asparaginyl hydroxylase enzyme that regulates the
transcriptional activity of hypoxia-inducible factor.";
Genes Dev. 16:1466-1471(2002).
[5]
INTERACTION WITH CREBBP, PHOSPHORYLATION AT THR-844, AND MUTAGENESIS
OF THR-844.
PubMed=11983697; DOI=10.1074/jbc.M201307200;
Gradin K., Takasaki C., Fujii-Kuriyama Y., Sogawa K.;
"The transcriptional activation function of the HIF-like factor
requires phosphorylation at a conserved threonine.";
J. Biol. Chem. 277:23508-23514(2002).
[6]
HYDROXYLATION AT ASN-851.
PubMed=11823643; DOI=10.1126/science.1068592;
Lando D., Peet D.J., Whelan D.A., Gorman J.J., Whitelaw M.L.;
"Asparagine hydroxylation of the HIF transactivation domain a hypoxic
switch.";
Science 295:858-861(2002).
[7]
INTERACTION WITH HIF3A, AND SUBCELLULAR LOCATION.
PubMed=21546903; DOI=10.1038/cdd.2011.47;
Torii S., Goto Y., Ishizawa T., Hoshi H., Goryo K., Yasumoto K.,
Fukumura H., Sogawa K.;
"Pro-apoptotic activity of inhibitory PAS domain protein (IPAS), a
negative regulator of HIF-1, through binding to pro-survival Bcl-2
family proteins.";
Cell Death Differ. 18:1711-1725(2011).
[8] {ECO:0000244|PDB:4ZP4, ECO:0000244|PDB:4ZPH, ECO:0000244|PDB:4ZPK, ECO:0000244|PDB:4ZQD}
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 3-361 IN COMPLEXES WITH
ARNT; INHIBITOR AND DNA, MUTAGENESIS OF ALA-23; ARG-27; PHE-169;
ARG-171; ASN-184; LYS-186; VAL-192 AND HIS-194, REGION, FUNCTION, AND
INTERACTION WITH ARNT.
PubMed=26245371; DOI=10.1038/nature14883;
Wu D., Potluri N., Lu J., Kim Y., Rastinejad F.;
"Structural integration in hypoxia-inducible factors.";
Nature 524:303-308(2015).
-!- FUNCTION: Transcription factor involved in the induction of oxygen
regulated genes. Heterodimerizes with ARNT; heterodimer binds to
core DNA sequence 5'-TACGTG-3' within the hypoxia response element
(HRE) of target gene promoters (PubMed:26245371). Regulates the
vascular endothelial growth factor (VEGF) expression and seems to
be implicated in the development of blood vessels and the tubular
system of lung. May also play a role in the formation of the
endothelium that gives rise to the blood brain barrier. Potent
activator of the Tie-2 tyrosine kinase expression. Activation
requires recruitment of transcriptional coactivators such as
CREBBP and probably EP300. Interaction with redox regulatory
protein APEX seems to activate CTAD (By similarity). {ECO:0000250,
ECO:0000269|PubMed:26245371}.
-!- SUBUNIT: Interacts with HIF3A isoform 2 (PubMed:21546903).
Efficient DNA binding requires dimerization with another bHLH
protein. Heterodimerizes with ARNT; heterodimer binds to core DNA
sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of
target gene promoters (PubMed:26245371). Interacts with CREBBP
(PubMed:11983697). Interacts with EGLN1. Interacts with VHL (By
similarity). {ECO:0000250|UniProtKB:Q99814,
ECO:0000269|PubMed:11983697, ECO:0000269|PubMed:21546903,
ECO:0000269|PubMed:26245371}.
-!- INTERACTION:
P53762:Arnt; NbExp=5; IntAct=EBI-15704570, EBI-78852;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00981, ECO:0000269|PubMed:21546903}. Nucleus speckle
{ECO:0000269|PubMed:21546903}. Note=Colocalizes with HIF3A isoform
2 in the nucleus and speckles. {ECO:0000269|PubMed:21546903}.
-!- TISSUE SPECIFICITY: Expressed in most tissues, with highest levels
in lung, followed by heart, kidney, brain and liver. Predominantly
expressed in endothelial cells. Also found in smooth muscle cells
of the uterus, neurons, and brown adipose tissue. High expression
in embryonic choroid plexus and kidney glomeruli.
-!- DEVELOPMENTAL STAGE: In day 11 embryo, expression is almost
exclusively seen in endothelial cells of the intersegmental blood
vessels separating the somites, the atrial and ventricular
chambers of the heart, and the dorsal aorta. High expression also
occurs in extraembryonic membranes. In the developing brain of day
13 embryo, endothelial cells of the highly vascularized choroid
plexus contain high levels of EPAS1.
-!- PTM: In normoxia, is probably hydroxylated on Pro-405 and Pro-530
by EGLN1/PHD1, EGLN2/PHD2 and/or EGLN3/PHD3. The hydroxylated
prolines promote interaction with VHL, initiating rapid
ubiquitination and subsequent proteasomal degradation. Under
hypoxia, proline hydroxylation is impaired and ubiquitination is
attenuated, resulting in stabilization (By similarity).
{ECO:0000250}.
-!- PTM: In normoxia, is hydroxylated on Asn-851 by HIF1AN thus
probably abrogating interaction with CREBBP and EP300 and
preventing transcriptional activation.
{ECO:0000269|PubMed:11823643}.
-!- PTM: Phosphorylated on multiple sites in the CTAD.
{ECO:0000269|PubMed:11983697}.
-!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
asparagine is (S) stereospecific within HIF CTAD domains.
{ECO:0000269|PubMed:11823643}.
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EMBL; U81983; AAB41496.1; -; mRNA.
EMBL; D89787; BAA20130.1; -; mRNA.
EMBL; AF045160; AAC12871.1; -; mRNA.
CCDS; CCDS37713.1; -.
RefSeq; NP_034267.3; NM_010137.3.
UniGene; Mm.1415; -.
PDB; 4ZP4; X-ray; 2.35 A; B/D=3-361.
PDB; 4ZPH; X-ray; 2.80 A; B/D=3-361.
PDB; 4ZPK; X-ray; 3.60 A; B=3-361.
PDB; 4ZQD; X-ray; 2.87 A; B/D=3-361.
PDBsum; 4ZP4; -.
PDBsum; 4ZPH; -.
PDBsum; 4ZPK; -.
PDBsum; 4ZQD; -.
ProteinModelPortal; P97481; -.
SMR; P97481; -.
BioGrid; 199458; 3.
DIP; DIP-46109N; -.
IntAct; P97481; 4.
STRING; 10090.ENSMUSP00000024954; -.
iPTMnet; P97481; -.
PhosphoSitePlus; P97481; -.
MaxQB; P97481; -.
PaxDb; P97481; -.
PRIDE; P97481; -.
Ensembl; ENSMUST00000024954; ENSMUSP00000024954; ENSMUSG00000024140.
GeneID; 13819; -.
KEGG; mmu:13819; -.
UCSC; uc008duj.2; mouse.
CTD; 2034; -.
MGI; MGI:109169; Epas1.
eggNOG; KOG3558; Eukaryota.
eggNOG; ENOG410YK57; LUCA.
GeneTree; ENSGT00760000118788; -.
HOGENOM; HOG000234306; -.
HOVERGEN; HBG060456; -.
InParanoid; P97481; -.
KO; K09095; -.
OMA; DFQLSPI; -.
OrthoDB; EOG091G0486; -.
PhylomeDB; P97481; -.
TreeFam; TF317772; -.
Reactome; R-MMU-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
Reactome; R-MMU-1234162; Oxygen-dependent asparagine hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-MMU-8951664; Neddylation.
ChiTaRS; Epas1; mouse.
PRO; PR:P97481; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000024140; -.
CleanEx; MM_EPAS1; -.
Genevisible; P97481; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IDA:MGI.
GO; GO:0050897; F:cobalt ion binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0003700; F:DNA binding transcription factor activity; IDA:MGI.
GO; GO:0035035; F:histone acetyltransferase binding; ISS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0001525; P:angiogenesis; IMP:MGI.
GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
GO; GO:0030154; P:cell differentiation; IGI:MGI.
GO; GO:0048469; P:cell maturation; IMP:MGI.
GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
GO; GO:0001892; P:embryonic placenta development; IGI:MGI.
GO; GO:0030218; P:erythrocyte differentiation; IMP:MGI.
GO; GO:0030097; P:hemopoiesis; IMP:MGI.
GO; GO:0055072; P:iron ion homeostasis; IGI:MGI.
GO; GO:0030324; P:lung development; IMP:MGI.
GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
GO; GO:0048625; P:myoblast fate commitment; IMP:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0042421; P:norepinephrine biosynthetic process; ISO:MGI.
GO; GO:0042415; P:norepinephrine metabolic process; IMP:MGI.
GO; GO:1903181; P:positive regulation of dopamine biosynthetic process; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0002027; P:regulation of heart rate; IMP:MGI.
GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IDA:MGI.
GO; GO:0001666; P:response to hypoxia; IMP:MGI.
GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
GO; GO:0043129; P:surfactant homeostasis; IMP:MGI.
GO; GO:0007601; P:visual perception; IMP:MGI.
CDD; cd00083; HLH; 1.
CDD; cd00130; PAS; 2.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR014887; HIF-1_TAD_C.
InterPro; IPR021537; HIF_alpha_subunit.
InterPro; IPR036638; HLH_DNA-bd_sf.
InterPro; IPR001067; Nuc_translocat.
InterPro; IPR001610; PAC.
InterPro; IPR000014; PAS.
InterPro; IPR035965; PAS-like_dom_sf.
InterPro; IPR013767; PAS_fold.
InterPro; IPR013655; PAS_fold_3.
Pfam; PF11413; HIF-1; 1.
Pfam; PF08778; HIF-1a_CTAD; 1.
Pfam; PF00989; PAS; 1.
Pfam; PF08447; PAS_3; 1.
PRINTS; PR00785; NCTRNSLOCATR.
SMART; SM00353; HLH; 1.
SMART; SM00086; PAC; 1.
SMART; SM00091; PAS; 2.
SUPFAM; SSF47459; SSF47459; 1.
SUPFAM; SSF55785; SSF55785; 2.
TIGRFAMs; TIGR00229; sensory_box; 2.
PROSITE; PS50888; BHLH; 1.
PROSITE; PS50112; PAS; 2.
1: Evidence at protein level;
3D-structure; Activator; Angiogenesis; Complete proteome;
Developmental protein; Differentiation; Direct protein sequencing;
DNA-binding; Hydroxylation; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 874 Endothelial PAS domain-containing protein
1.
/FTId=PRO_0000127420.
DOMAIN 14 67 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
DOMAIN 84 154 PAS 1. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 230 300 PAS 2. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 304 347 PAC.
REGION 26 53 DNA-binding.
{ECO:0000269|PubMed:26245371}.
REGION 171 192 Required for heterodimer formation with
ARNT. {ECO:0000269|PubMed:26245371}.
REGION 495 541 NTAD.
REGION 834 874 CTAD.
COMPBIAS 471 479 Poly-Ser.
MOD_RES 405 405 4-hydroxyproline. {ECO:0000250}.
MOD_RES 530 530 4-hydroxyproline. {ECO:0000250}.
MOD_RES 844 844 Phosphothreonine.
{ECO:0000269|PubMed:11983697}.
MOD_RES 851 851 (3S)-3-hydroxyasparagine.
{ECO:0000269|PubMed:11823643}.
MUTAGEN 23 23 A->D: Decreases HRE DNA binding.
{ECO:0000269|PubMed:26245371}.
MUTAGEN 27 27 R->A: Decreases HRE DNA binding.
{ECO:0000269|PubMed:26245371}.
MUTAGEN 169 169 F->D: Decreases heterodimer formation
with ARNT. {ECO:0000269|PubMed:26245371}.
MUTAGEN 171 171 R->A: Markedly decreases heterodimer
formation with ARNT. Impairs heterodimer
formation with ARNT; when associated with
D-192. {ECO:0000269|PubMed:26245371}.
MUTAGEN 184 184 N->D: Decreases HRE DNA binding; when
associated with D-186.
{ECO:0000269|PubMed:26245371}.
MUTAGEN 186 186 K->D: Decreases HRE DNA binding; when
associated with D-184.
{ECO:0000269|PubMed:26245371}.
MUTAGEN 192 192 V->D: Markedly decreases heterodimer
formation with ARNT. Impairs heterodimer
formation with ARNT; when associated with
A-171. {ECO:0000269|PubMed:26245371}.
MUTAGEN 194 194 H->A: Decreases heterodimer formation
with ARNT. {ECO:0000269|PubMed:26245371}.
MUTAGEN 530 530 P->A: Confers transcriptional activity at
normoxia; when associated with A-851.
{ECO:0000269|PubMed:12080085}.
MUTAGEN 844 844 T->A: Decreases interaction with CREBBP.
{ECO:0000269|PubMed:11983697}.
MUTAGEN 851 851 N->A: Confers transcriptional activity at
normoxia; when associated with A-530.
{ECO:0000269|PubMed:12080085}.
CONFLICT 25 25 C -> S (in Ref. 2; BAA20130).
{ECO:0000305}.
CONFLICT 191 191 K -> KS (in Ref. 1; AAB41496).
{ECO:0000305}.
CONFLICT 439 440 VS -> AA (in Ref. 3; AAC12871).
{ECO:0000305}.
CONFLICT 463 463 D -> G (in Ref. 3; AAC12871).
{ECO:0000305}.
CONFLICT 654 654 G -> V (in Ref. 2; BAA20130).
{ECO:0000305}.
CONFLICT 663 663 A -> P (in Ref. 2; BAA20130).
{ECO:0000305}.
CONFLICT 669 669 S -> W (in Ref. 1; AAB41496).
{ECO:0000305}.
CONFLICT 673 673 P -> L (in Ref. 1; AAB41496).
{ECO:0000305}.
CONFLICT 678 678 P -> L (in Ref. 1; AAB41496).
{ECO:0000305}.
CONFLICT 725 725 D -> E (in Ref. 3; AAC12871).
{ECO:0000305}.
CONFLICT 731 731 P -> L (in Ref. 3; AAC12871).
{ECO:0000305}.
CONFLICT 762 762 A -> G (in Ref. 3; AAC12871).
{ECO:0000305}.
CONFLICT 786 786 P -> L (in Ref. 3; AAC12871).
{ECO:0000305}.
CONFLICT 791 791 S -> F (in Ref. 3; AAC12871).
{ECO:0000305}.
CONFLICT 794 794 S -> N (in Ref. 3; AAC12871).
{ECO:0000305}.
HELIX 27 39 {ECO:0000244|PDB:4ZP4}.
STRAND 41 43 {ECO:0000244|PDB:4ZP4}.
HELIX 45 48 {ECO:0000244|PDB:4ZP4}.
HELIX 53 74 {ECO:0000244|PDB:4ZP4}.
HELIX 88 94 {ECO:0000244|PDB:4ZP4}.
STRAND 96 103 {ECO:0000244|PDB:4ZP4}.
STRAND 107 111 {ECO:0000244|PDB:4ZP4}.
HELIX 115 119 {ECO:0000244|PDB:4ZP4}.
HELIX 123 126 {ECO:0000244|PDB:4ZP4}.
HELIX 131 134 {ECO:0000244|PDB:4ZP4}.
HELIX 137 147 {ECO:0000244|PDB:4ZP4}.
STRAND 165 174 {ECO:0000244|PDB:4ZP4}.
HELIX 185 187 {ECO:0000244|PDB:4ZP4}.
STRAND 189 200 {ECO:0000244|PDB:4ZP4}.
STRAND 221 228 {ECO:0000244|PDB:4ZP4}.
STRAND 243 248 {ECO:0000244|PDB:4ZP4}.
STRAND 253 257 {ECO:0000244|PDB:4ZP4}.
HELIX 260 265 {ECO:0000244|PDB:4ZP4}.
HELIX 269 272 {ECO:0000244|PDB:4ZP4}.
HELIX 277 280 {ECO:0000244|PDB:4ZP4}.
HELIX 283 299 {ECO:0000244|PDB:4ZP4}.
STRAND 300 303 {ECO:0000244|PDB:4ZP4}.
STRAND 307 310 {ECO:0000244|PDB:4ZP4}.
STRAND 314 327 {ECO:0000244|PDB:4ZP4}.
TURN 329 331 {ECO:0000244|PDB:4ZP4}.
STRAND 334 343 {ECO:0000244|PDB:4ZP4}.
HELIX 356 359 {ECO:0000244|PDB:4ZP4}.
SEQUENCE 874 AA; 96712 MW; A6FFA490AE43640C CRC64;
MTADKEKKRS SSELRKEKSR DAARCRRSKE TEVFYELAHE LPLPHSVSSH LDKASIMRLA
ISFLRTHKLL SSVCSENESE AEADQQMDNL YLKALEGFIA VVTQDGDMIF LSENISKFMG
LTQVELTGHS IFDFTHPCDH EEIRENLTLK NGSGFGKKSK DVSTERDFFM RMKCTVTNRG
RTVNLKSATW KVLHCTGQVR VYNNCPPHSS LCGSKEPLLS CLIIMCEPIQ HPSHMDIPLD
SKTFLSRHSM DMKFTYCDDR ILELIGYHPE ELLGRSAYEF YHALDSENMT KSHQNLCTKG
QVVSGQYRML AKHGGYVWLE TQGTVIYNPR NLQPQCIMCV NYVLSEIEKN DVVFSMDQTE
SLFKPHLMAM NSIFDSSDDV AVTEKSNYLF TKLKEEPEEL AQLAPTPGDA IISLDFGSQN
FDEPSAYGKA ILPPGQPWVS GLRSHSAQSE SGSLPAFTVP QADTPGNTTP SASSSSSCST
PSSPEDYYSS LENPLKIEVI EKLFAMDTEP RDPGSTQTDF SELDLETLAP YIPMDGEDFQ
LSPICPEEPL MPESPQPTPQ HCFSTMTSIF QPLTPGATHG PFFLDKYPQQ LESRKTESEH
WPMSSIFFDA GSKGSLSPCC GQASTPLSSM GGRSNTQWPP DPPLHFGPTK WPVGDQSAES
LGALPVGSSQ LEPPSAPPHV SMFKMRSAKD FGARGPYMMS PAMIALSNKL KLKRQLEYEE
QAFQDTSGGD PPGTSSSHLM WKRMKSLMGG TCPLMPDKTI SANMAPDEFT QKSMRGLGQP
LRHLPPPQPP STRSSGENAK TGFPPQCYAS QFQDYGPPGA QKVSGVASRL LGPSFEPYLL
PELTRYDCEV NVPVPGSSTL LQGRDLLRAL DQAT


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PR-880 HIF-1 alpha NTAD (530-698)His Hypoxia-Inducible Factor-1 alpha, N- terminal Activation Domain human, recombinant, E. coli 10
U0798b CLIA Bos taurus,Bovine,HIF1A,HIF-1-alpha,HIF1-alpha,Hypoxia-inducible factor 1-alpha 96T
E0798b ELISA kit Bos taurus,Bovine,HIF1A,HIF-1-alpha,HIF1-alpha,Hypoxia-inducible factor 1-alpha 96T
E0798b ELISA Bos taurus,Bovine,HIF1A,HIF-1-alpha,HIF1-alpha,Hypoxia-inducible factor 1-alpha 96T
U0798r CLIA Hif1a,HIF-1-alpha,HIF1-alpha,Hypoxia-inducible factor 1-alpha,Rat,Rattus norvegicus 96T
E0798r ELISA Hif1a,HIF-1-alpha,HIF1-alpha,Hypoxia-inducible factor 1-alpha,Rat,Rattus norvegicus 96T
E0798r ELISA kit Hif1a,HIF-1-alpha,HIF1-alpha,Hypoxia-inducible factor 1-alpha,Rat,Rattus norvegicus 96T
bs-1447P Peptides: HIF-2 Alpha (Hypoxia-inducible factor-2 Alpha) Protein Length:12-25 amino acids. 200ug lyophilized
18-003-43264 Hypoxia-inducible factor 1 alpha inhibitor - EC 1.14.11.16; Hypoxia-inducible factor asparagine hydroxylase; Factor inhibiting HIF-1; FIH-1 Polyclonal 0.05 mg Aff Pur
30-813 EGLN3 catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. It hydroxylates HIF-1 alpha at 'Pro-564', and HIF-2 alpha. EGLN3 functions as a c 0.05 mg


 

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