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Macrophage migration inhibitory factor (MIF) (EC 5.3.2.1) (Delayed early response protein 6) (DER6) (Glycosylation-inhibiting factor) (GIF) (L-dopachrome isomerase) (L-dopachrome tautomerase) (EC 5.3.3.12) (Phenylpyruvate tautomerase)

 MIF_MOUSE               Reviewed;         115 AA.
P34884;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
12-SEP-2018, entry version 168.
RecName: Full=Macrophage migration inhibitory factor;
Short=MIF;
EC=5.3.2.1;
AltName: Full=Delayed early response protein 6;
Short=DER6;
AltName: Full=Glycosylation-inhibiting factor;
Short=GIF;
AltName: Full=L-dopachrome isomerase;
AltName: Full=L-dopachrome tautomerase;
EC=5.3.3.12;
AltName: Full=Phenylpyruvate tautomerase;
Name=Mif;
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], AND PROTEIN SEQUENCE OF 2-28.
TISSUE=Pituitary;
PubMed=8413654; DOI=10.1038/365756a0;
Bernhagen J., Calandra T., Mitchell R.A., Martin S.B., Tracey K.J.,
Voelter W., Manogue K.R., Cerami A., Bucala R.;
"MIF is a pituitary-derived cytokine that potentiates lethal
endotoxaemia.";
Nature 365:756-759(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
PubMed=1508193; DOI=10.1128/MCB.12.9.3919;
Lanahan A.A., Williams J.B., Sanders L.K., Nathans D.;
"Growth factor-induced delayed early response genes.";
Mol. Cell. Biol. 12:3919-3929(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
PubMed=8234256; DOI=10.1073/pnas.90.21.10056;
Mikayama T., Nakano T., Gomi H., Nakagawa Y., Liu Y.C., Iwamatsu A.,
Weiser W.Y., Ishizaka K., Sato M., Ishii Y.;
"Molecular cloning and functional expression of a cDNA encoding
glycosylation-inhibiting factor.";
Proc. Natl. Acad. Sci. U.S.A. 90:10056-10060(1993).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/Sv;
PubMed=7706726;
Mitchell R., Bacher M., Bernhagen J., Pushkarskaya T., Seldin M.F.,
Bucala R.;
"Cloning and characterization of the gene for mouse macrophage
migration inhibitory factor (MIF).";
J. Immunol. 154:3863-3870(1995).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/Sv;
PubMed=7558021; DOI=10.1006/geno.1995.1071;
Bozza M., Kolakowski L.F. Jr., Jenkins N.A., Gilbert D.J.,
Copeland N.G., David J.R., Gerard C.;
"Structural characterization and chromosomal location of the mouse
macrophage migration inhibitory factor gene and pseudogenes.";
Genomics 27:412-419(1995).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/Sv;
PubMed=7558020; DOI=10.1006/geno.1995.1070;
Kozak C.A., Adamson M.C., Buckler C.E., Segovia L., Paralkar V.,
Wistow G.;
"Genomic cloning of mouse MIF (macrophage inhibitory factor) and
genetic mapping of the human and mouse expressed gene and nine mouse
pseudogenes.";
Genomics 27:405-411(1995).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Kidney, and Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 2-12, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 6-115.
TISSUE=Lens;
PubMed=7679497; DOI=10.1073/pnas.90.4.1272;
Wistow G.J., Shaughnessy M., Lee D.C., Hodin J., Zelenka P.S.;
"A macrophage migration inhibitory factor is expressed in the
differentiating cells of the eye lens.";
Proc. Natl. Acad. Sci. U.S.A. 90:1272-1275(1993).
[10]
CHARACTERIZATION.
PubMed=7947826; DOI=10.1021/bi00251a025;
Bernhagen J., Mitchell R.A., Calandra T., Voelter W., Cerami A.,
Bucala R.;
"Purification, bioactivity, and secondary structure analysis of mouse
and human macrophage migration inhibitory factor (MIF).";
Biochemistry 33:14144-14155(1994).
[11]
SUBCELLULAR LOCATION, AND ROLE OF TAUTOMERASE INHIBITORS IN IMPROVED
SURVIVAL IN CASE OF SEPSIS.
PubMed=17526494; DOI=10.1074/jbc.M701825200;
Crichlow G.V., Cheng K.F., Dabideen D., Ochani M., Aljabari B.,
Pavlov V.A., Miller E.J., Lolis E., Al-Abed Y.;
"Alternative chemical modifications reverse the binding orientation of
a pharmacophore scaffold in the active site of macrophage migration
inhibitory factor.";
J. Biol. Chem. 282:23089-23095(2007).
[12]
INTERACTION WITH CD74; CXCR2 AND COPS5, CATALYTIC ACTIVITY, AND
MUTAGENESIS OF PRO-2.
PubMed=19188446; DOI=10.1128/MCB.01907-08;
Fingerle-Rowson G., Kaleswarapu D.R., Schlander C., Kabgani N.,
Brocks T., Reinart N., Busch R., Schuetz A., Lue H., Du X., Liu A.,
Xiong H., Chen Y., Nemajerova A., Hallek M., Bernhagen J., Leng L.,
Bucala R.;
"A tautomerase-null macrophage migration-inhibitory factor (MIF) gene
knock-in mouse model reveals that protein interactions and not
enzymatic activity mediate MIF-dependent growth regulation.";
Mol. Cell. Biol. 29:1922-1932(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-78, SUCCINYLATION [LARGE
SCALE ANALYSIS] AT LYS-78, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[15]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=10360941; DOI=10.1021/bi9904048;
Taylor A.B., Johnson W.H. Jr., Czerwinski R.M., Li H.S., Hackert M.L.,
Whitman C.P.;
"Crystal structure of macrophage migration inhibitory factor complexed
with (E)-2-fluoro-p-hydroxycinnamate at 1.8 A resolution: implications
for enzymatic catalysis and inhibition.";
Biochemistry 38:7444-7452(1999).
[16]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), TAUTOMERASE ACTIVITY,
IDENTIFICATION BY MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE,
AND MUTAGENESIS OF PRO-2.
PubMed=10933783; DOI=10.1021/bi000373c;
Stamps S.L., Taylor A.B., Wang S.C., Hackert M.L., Whitman C.P.;
"Mechanism of the phenylpyruvate tautomerase activity of macrophage
migration inhibitory factor: properties of the P1G, P1A, Y95F, and
N97A mutants.";
Biochemistry 39:9671-9678(2000).
[17]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH INHIBITOR,
TAUTOMERASE ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, AND
SUBUNIT.
PubMed=16780921; DOI=10.1016/j.bioorg.2006.05.001;
Golubkov P.A., Johnson W.H. Jr., Czerwinski R.M., Person M.D.,
Wang S.C., Whitman C.P., Hackert M.L.;
"Inactivation of the phenylpyruvate tautomerase activity of macrophage
migration inhibitory factor by 2-oxo-4-phenyl-3-butynoate.";
Bioorg. Chem. 34:183-199(2006).
-!- FUNCTION: Pro-inflammatory cytokine. Involved in the innate immune
response to bacterial pathogens. The expression of MIF at sites of
inflammation suggests a role as mediator in regulating the
function of macrophages in host defense. Counteracts the anti-
inflammatory activity of glucocorticoids. Has phenylpyruvate
tautomerase and dopachrome tautomerase activity (in vitro), but
the physiological substrate is not known. It is not clear whether
the tautomerase activity has any physiological relevance, and
whether it is important for cytokine activity (By similarity).
{ECO:0000250|UniProtKB:P14174}.
-!- CATALYTIC ACTIVITY: Keto-phenylpyruvate = enol-phenylpyruvate.
{ECO:0000269|PubMed:19188446}.
-!- CATALYTIC ACTIVITY: L-dopachrome = 5,6-dihydroxyindole-2-
carboxylate. {ECO:0000269|PubMed:19188446}.
-!- SUBUNIT: Homotrimer. Interacts with BNIPL (By similarity).
Interacts with the CD74 extracellular domain. Interacts with COPS5
and with the CXCR2 extracellular domain.
{ECO:0000250|UniProtKB:P14174, ECO:0000269|PubMed:16780921,
ECO:0000269|PubMed:19188446}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17526494,
ECO:0000269|PubMed:8234256}. Cytoplasm
{ECO:0000250|UniProtKB:P14174}. Note=Does not have a cleavable
signal sequence and is secreted via a specialized, non-classical
pathway. Secreted by macrophages upon stimulation by bacterial
lipopolysaccharide (LPS), or by M.tuberculosis antigens (By
similarity). {ECO:0000250|UniProtKB:P14174}.
-!- MISCELLANEOUS: MIF tautomerase inhibitors improve survival in case
of sepsis.
-!- SIMILARITY: Belongs to the MIF family. {ECO:0000305}.
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EMBL; Z23048; CAA80583.1; -; mRNA.
EMBL; U19825; AAA91637.1; -; Genomic_DNA.
EMBL; L10613; AAA37693.1; -; mRNA.
EMBL; U20156; AAA91638.1; -; Genomic_DNA.
EMBL; L39357; AAA74321.1; -; Genomic_DNA.
EMBL; BC024895; AAH24895.1; -; mRNA.
EMBL; BC086928; AAH86928.1; -; mRNA.
EMBL; L07607; AAA37111.1; -; mRNA.
CCDS; CCDS23934.1; -.
PIR; A44499; A44499.
RefSeq; NP_034928.1; NM_010798.2.
UniGene; Mm.2326; -.
PDB; 1MFF; X-ray; 2.00 A; A/B/C=2-115.
PDB; 1MFI; X-ray; 1.80 A; A/B/C=2-115.
PDB; 2GDG; X-ray; 1.45 A; A/B/C=2-115.
PDBsum; 1MFF; -.
PDBsum; 1MFI; -.
PDBsum; 2GDG; -.
ProteinModelPortal; P34884; -.
SMR; P34884; -.
BioGrid; 201418; 1.
IntAct; P34884; 4.
MINT; P34884; -.
STRING; 10090.ENSMUSP00000041149; -.
BindingDB; P34884; -.
ChEMBL; CHEMBL1926491; -.
iPTMnet; P34884; -.
PhosphoSitePlus; P34884; -.
SwissPalm; P34884; -.
EPD; P34884; -.
PaxDb; P34884; -.
PeptideAtlas; P34884; -.
PRIDE; P34884; -.
TopDownProteomics; P34884; -.
Ensembl; ENSMUST00000038169; ENSMUSP00000041149; ENSMUSG00000033307.
GeneID; 17319; -.
KEGG; mmu:17319; -.
UCSC; uc007ftc.1; mouse.
CTD; 4282; -.
MGI; MGI:96982; Mif.
eggNOG; KOG1759; Eukaryota.
eggNOG; ENOG41122MF; LUCA.
GeneTree; ENSGT00910000144267; -.
HOGENOM; HOG000112325; -.
HOVERGEN; HBG003240; -.
InParanoid; P34884; -.
KO; K07253; -.
OMA; PDRIYIN; -.
OrthoDB; EOG091G0ZNJ; -.
PhylomeDB; P34884; -.
TreeFam; TF313853; -.
BRENDA; 5.3.2.1; 3474.
Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
Reactome; R-MMU-6798695; Neutrophil degranulation.
EvolutionaryTrace; P34884; -.
PRO; PR:P34884; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000033307; Expressed in 149 organ(s), highest expression level in Ammon's horn.
CleanEx; MM_MIF; -.
ExpressionAtlas; P34884; baseline and differential.
Genevisible; P34884; MM.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005576; C:extracellular region; ISO:MGI.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0042056; F:chemoattractant activity; ISO:MGI.
GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL.
GO; GO:0005126; F:cytokine receptor binding; ISO:MGI.
GO; GO:0004167; F:dopachrome isomerase activity; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0050178; F:phenylpyruvate tautomerase activity; IMP:MGI.
GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
GO; GO:0002035; P:brain renin-angiotensin system; ISO:MGI.
GO; GO:0019752; P:carboxylic acid metabolic process; ISO:MGI.
GO; GO:0007569; P:cell aging; IMP:MGI.
GO; GO:0008283; P:cell proliferation; ISO:MGI.
GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:MGI.
GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IMP:MGI.
GO; GO:0042756; P:drinking behavior; ISO:MGI.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:BHF-UCL.
GO; GO:0090344; P:negative regulation of cell aging; ISO:MGI.
GO; GO:0071157; P:negative regulation of cell cycle arrest; ISO:MGI.
GO; GO:0032269; P:negative regulation of cellular protein metabolic process; IDA:BHF-UCL.
GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IDA:BHF-UCL.
GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISO:MGI.
GO; GO:0010760; P:negative regulation of macrophage chemotaxis; ISO:MGI.
GO; GO:0002906; P:negative regulation of mature B cell apoptotic process; IDA:BHF-UCL.
GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; IMP:BHF-UCL.
GO; GO:0002675; P:positive regulation of acute inflammatory response; ISO:MGI.
GO; GO:0002821; P:positive regulation of adaptive immune response; NAS:BHF-UCL.
GO; GO:0090238; P:positive regulation of arachidonic acid secretion; IDA:BHF-UCL.
GO; GO:0048680; P:positive regulation of axon regeneration; ISO:MGI.
GO; GO:0030890; P:positive regulation of B cell proliferation; ISO:MGI.
GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; IDA:BHF-UCL.
GO; GO:0050715; P:positive regulation of cytokine secretion; ISO:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:BHF-UCL.
GO; GO:0046326; P:positive regulation of glucose import; ISO:MGI.
GO; GO:0045821; P:positive regulation of glycolytic process; ISO:MGI.
GO; GO:0050778; P:positive regulation of immune response; ISO:MGI.
GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; IMP:BHF-UCL.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:BHF-UCL.
GO; GO:0061081; P:positive regulation of myeloid leukocyte cytokine production involved in immune response; IMP:BHF-UCL.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
GO; GO:0042327; P:positive regulation of phosphorylation; ISO:MGI.
GO; GO:0043268; P:positive regulation of potassium ion transport; ISO:MGI.
GO; GO:0061078; P:positive regulation of prostaglandin secretion involved in immune response; IMP:BHF-UCL.
GO; GO:0010739; P:positive regulation of protein kinase A signaling; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
GO; GO:0001516; P:prostaglandin biosynthetic process; ISO:MGI.
GO; GO:0070207; P:protein homotrimerization; ISO:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IMP:MGI.
GO; GO:0007283; P:spermatogenesis; ISO:MGI.
Gene3D; 3.30.429.10; -; 1.
InterPro; IPR001398; Macrophage_inhib_fac.
InterPro; IPR019829; Macrophage_inhib_fac_CS.
InterPro; IPR014347; Tautomerase/MIF_sf.
PANTHER; PTHR11954; PTHR11954; 1.
Pfam; PF01187; MIF; 1.
ProDom; PD004816; Macrophage_inhib_fac; 1.
SUPFAM; SSF55331; SSF55331; 1.
PROSITE; PS01158; MIF; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytokine; Cytoplasm;
Direct protein sequencing; Immunity; Inflammatory response;
Innate immunity; Isomerase; Reference proteome; Secreted.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:10933783,
ECO:0000269|PubMed:8413654,
ECO:0000269|Ref.8}.
CHAIN 2 115 Macrophage migration inhibitory factor.
/FTId=PRO_0000158066.
ACT_SITE 2 2 Proton acceptor; via imino nitrogen.
BINDING 33 33 Substrate.
BINDING 65 65 Substrate; via amide nitrogen.
{ECO:0000250}.
BINDING 98 98 Substrate.
MOD_RES 78 78 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 78 78 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MUTAGEN 2 2 P->G: Loss of tautomerase activity,
reduced activation of intracellular
signaling pathways, and reduced
interaction with CXCR2 and COPS5.
{ECO:0000269|PubMed:10933783,
ECO:0000269|PubMed:19188446}.
STRAND 3 10 {ECO:0000244|PDB:2GDG}.
HELIX 12 14 {ECO:0000244|PDB:2GDG}.
HELIX 19 31 {ECO:0000244|PDB:2GDG}.
HELIX 35 37 {ECO:0000244|PDB:2GDG}.
STRAND 39 43 {ECO:0000244|PDB:2GDG}.
STRAND 47 50 {ECO:0000244|PDB:2GDG}.
STRAND 58 66 {ECO:0000244|PDB:2GDG}.
HELIX 70 88 {ECO:0000244|PDB:2GDG}.
HELIX 92 94 {ECO:0000244|PDB:2GDG}.
STRAND 95 101 {ECO:0000244|PDB:2GDG}.
HELIX 104 106 {ECO:0000244|PDB:2GDG}.
STRAND 107 109 {ECO:0000244|PDB:2GDG}.
SEQUENCE 115 AA; 12504 MW; 92D207B81B149945 CRC64;
MPMFIVNTNV PRASVPEGFL SELTQQLAQA TGKPAQYIAV HVVPDQLMTF SGTNDPCALC
SLHSIGKIGG AQNRNYSKLL CGLLSDRLHI SPDRVYINYY DMNAANVGWN GSTFA


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EIAAB11708 D-dopachrome decarboxylase,D-dopachrome tautomerase,DDT,Homo sapiens,Human,Phenylpyruvate tautomerase II
DCTN1 DCT Gene dopachrome tautomerase (dopachrome delta-isomerase, tyrosine-related protein 2)
EIAAB44691 DCT,DCT,DT,L-dopachrome Delta-isomerase,L-dopachrome tautomerase,Pig,Sus scrofa,TRP2,TRP-2,Tyrosinase-related protein 2,TYRP2
EIAAB44688 Bos taurus,Bovine,DCT,DCT,DT,L-dopachrome Delta-isomerase,L-dopachrome tautomerase,TRP2,TRP-2,Tyrosinase-related protein 2,TYRP2
EIAAB44692 DCT,DCT,DT,Homo sapiens,Human,L-dopachrome Delta-isomerase,L-dopachrome tautomerase,TRP2,TRP-2,Tyrosinase-related protein 2,TYRP2
CSB-EL006562PI Pig dopachrome tautomerase (dopachrome delta-isomerase, tyrosine-related protein 2) (DCT) ELISA kit, Species Pig, Sample Type serum, plasma 96T


 

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