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Glycodelin (GD) (Placental protein 14) (PP14) (Pregnancy-associated endometrial alpha-2 globulin) (PAEG) (PEG) (Progestagen-associated endometrial protein) (Progesterone-associated endometrial protein) (Zona-binding inhibitory factor-1) (ZIF-1)

 PAEP_HUMAN              Reviewed;         180 AA.
P09466; Q5T6T1; Q9UG92;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-MAR-1992, sequence version 2.
31-JAN-2018, entry version 174.
RecName: Full=Glycodelin;
Short=GD;
AltName: Full=Placental protein 14 {ECO:0000303|PubMed:3569148, ECO:0000303|PubMed:9918684};
Short=PP14;
AltName: Full=Pregnancy-associated endometrial alpha-2 globulin {ECO:0000303|PubMed:3667877};
Short=PAEG;
Short=PEG;
AltName: Full=Progestagen-associated endometrial protein;
AltName: Full=Progesterone-associated endometrial protein;
AltName: Full=Zona-binding inhibitory factor-1 {ECO:0000303|PubMed:12672671};
Short=ZIF-1 {ECO:0000303|PubMed:12672671};
Flags: Precursor;
Name=PAEP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3194393; DOI=10.1073/pnas.85.23.8845;
Julkunen M., Seppala M., Janne O.A.;
"Complete amino acid sequence of human placental protein 14: a
progesterone-regulated uterine protein homologous to beta-
lactoglobulins.";
Proc. Natl. Acad. Sci. U.S.A. 85:8845-8849(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2206398; DOI=10.1089/dna.1990.9.401;
Vaisse C., Atger M., Potier B., Milgrom E.;
"Human placental protein 14 gene: sequence and characterization of a
short duplication.";
DNA Cell Biol. 9:401-413(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
PubMed=2006183; DOI=10.1073/pnas.88.6.2456;
Garde J., Bell S.C., Eperon I.C.;
"Multiple forms of mRNA encoding human pregnancy-associated
endometrial alpha 2-globulin, a beta-lactoglobulin homologue.";
Proc. Natl. Acad. Sci. U.S.A. 88:2456-2460(1991).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
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).
[7]
PROTEIN SEQUENCE OF 19-56, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=3667877; DOI=10.1210/jcem-65-5-1067;
Bell S.C., Keyte J.W., Waites G.T.;
"Pregnancy-associated endometrial alpha 2-globulin, the major
secretory protein of the luteal phase and first trimester pregnancy
endometrium, is not glycosylated prolactin but related to beta-
lactoglobulins.";
J. Clin. Endocrinol. Metab. 65:1067-1071(1987).
[8]
PROTEIN SEQUENCE OF 19-30.
PubMed=3569148; DOI=10.1210/endo-120-6-2620;
Huhtala M.L., Seppala M., Narvanen A., Palomaki P., Julkunen M.,
Bohn H.;
"Amino acid sequence homology between human placental protein 14 and
beta-lactoglobulins from various species.";
Endocrinology 120:2620-2622(1987).
[9]
PROTEIN SEQUENCE OF 19-38.
TISSUE=Decidua;
PubMed=11278680; DOI=10.1074/jbc.M010451200;
Vigne J.-L., Hornung D., Mueller M.D., Taylor R.N.;
"Purification and characterization of an immunomodulatory endometrial
protein, glycodelin.";
J. Biol. Chem. 276:17101-17105(2001).
[10]
PROTEIN SEQUENCE OF 19-43, STRUCTURE OF CARBOHYRATES OF GLYCODELIN-F,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND FUNCTION.
PubMed=12672671; DOI=10.1095/biolreprod.102.012658;
Chiu P.C., Koistinen R., Koistinen H., Seppala M., Lee K.F.,
Yeung W.S.;
"Zona-binding inhibitory factor-1 from human follicular fluid is an
isoform of glycodelin.";
Biol. Reprod. 69:365-372(2003).
[11]
FUNCTION OF GLYCODELIN-A.
PubMed=7531163;
Oehninger S., Coddington C.C., Hodgen G.D., Seppala M.;
"Factors affecting fertilization: endometrial placental protein 14
reduces the capacity of human spermatozoa to bind to the human zona
pellucida.";
Fertil. Steril. 63:377-383(1995).
[12]
STRUCTURE OF CARBOHYDRATES OF GLYCODELIN-A, GLYCOSYLATION AT ASN-46
AND ASN-81, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Amniotic fluid;
PubMed=7592613; DOI=10.1074/jbc.270.41.24116;
Dell A., Morris H.R., Easton R.L., Panico M., Patankar M.,
Oehniger S., Koistinen R., Koistinen H., Seppala M., Clark G.F.;
"Structural analysis of the oligosaccharides derived from glycodelin,
a human glycoprotein with potent immunosuppressive and contraceptive
activities.";
J. Biol. Chem. 270:24116-24126(1995).
[13]
STRUCTURE OF CARBOHYDRATES OF GLYCODELIN-S.
TISSUE=Seminal plasma;
PubMed=8943270; DOI=10.1074/jbc.271.50.32159;
Morris H.R., Dell A., Easton R.L., Panico M., Koistinen H.,
Koistinen R., Oehninger S., Patankar M.S., Seppala M., Clark G.F.;
"Gender-specific glycosylation of human glycodelin affects its
contraceptive activity.";
J. Biol. Chem. 271:32159-32167(1996).
[14]
STRUCTURE OF CARBOHYDRATES OF GLYCODELIN-S, TISSUE SPECIFICITY, AND
SUBUNIT.
PubMed=9239694; DOI=10.1093/molehr/2.10.759;
Koistinen H., Koistinen R., Dell A., Morris H.R., Easton R.L.,
Patankar M.S., Oehninger S., Clark G.F., Seppala M.;
"Glycodelin from seminal plasma is a differentially glycosylated form
of contraceptive glycodelin-A.";
Mol. Hum. Reprod. 2:759-765(1996).
[15]
FUNCTION.
PubMed=9918684; DOI=10.1006/cimm.1998.1408;
Rachmilewitz J., Riely G.J., Tykocinski M.L.;
"Placental protein 14 functions as a direct T-cell inhibitor.";
Cell. Immunol. 191:26-33(1999).
[16]
FUNCTION OF GLYCODELIN-S.
PubMed=15883155; DOI=10.1074/jbc.M504103200;
Chiu P.C., Chung M.K., Tsang H.Y., Koistinen R., Koistinen H.,
Seppala M., Lee K.F., Yeung W.S.;
"Glycodelin-S in human seminal plasma reduces cholesterol efflux and
inhibits capacitation of spermatozoa.";
J. Biol. Chem. 280:25580-25589(2005).
[17]
STRUCTURE OF CARBOHYDRATES OF GLYCODELIN-C, FUNCTION, TISSUE
SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=17192260; DOI=10.1074/jbc.M607482200;
Chiu P.C., Chung M.K., Koistinen R., Koistinen H., Seppala M.,
Ho P.C., Ng E.H., Lee K.F., Yeung W.S.;
"Cumulus oophorus-associated glycodelin-C displaces sperm-bound
glycodelin-A and -F and stimulates spermatozoa-zona pellucida
binding.";
J. Biol. Chem. 282:5378-5388(2007).
[18] {ECO:0000244|PDB:4R0B}
X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 20-180, DISULFIDE BONDS, AND
SUBUNIT.
PubMed=25422905; DOI=10.1042/BJ20141003;
Schiefner A., Rodewald F., Neumaier I., Skerra A.;
"The dimeric crystal structure of the human fertility lipocalin
glycodelin reveals a protein scaffold for the presentation of complex
glycans.";
Biochem. J. 466:95-104(2015).
-!- FUNCTION: Glycoprotein that regulates critical steps during
fertilization and also has immunomonomodulatory effects. Four
glycoforms, namely glycodelin-S, -A, -F and -C have been
identified in reproductive tissues that differ in glycosylation
and biological activity. Glycodelin-A has contraceptive and
immunosuppressive activities (PubMed:9918684, PubMed:7531163).
Glycodelin-C stimulates binding of spermatozoa to the zona
pellucida (PubMed:17192260). Glycodelin-F inhibits spermatozoa-
zona pellucida binding and significantly suppresses progesterone-
induced acrosome reaction of spermatozoa (PubMed:12672671).
Glycodelin-S in seminal plasma maintains the uncapacitated state
of human spermatozoa (PubMed:15883155).
{ECO:0000269|PubMed:12672671, ECO:0000269|PubMed:15883155,
ECO:0000269|PubMed:17192260, ECO:0000269|PubMed:7531163,
ECO:0000269|PubMed:9918684}.
-!- SUBUNIT: Homodimer (PubMed:25422905, PubMed:9239694).
{ECO:0000269|PubMed:25422905, ECO:0000269|PubMed:9239694}.
-!- INTERACTION:
Q96HH9:GRAMD2B; NbExp=5; IntAct=EBI-465167, EBI-2832937;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12672671,
ECO:0000269|PubMed:17192260, ECO:0000269|PubMed:3667877}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P09466-1; Sequence=Displayed;
Name=2;
IsoId=P09466-2; Sequence=VSP_003140;
Name=3;
IsoId=P09466-3; Sequence=VSP_003141;
-!- TISSUE SPECIFICITY: This protein is, the main protein synthesized
and secreted in the endometrium from mid-luteal phase of the
menstrual cycle and during the first semester of pregnancy
(PubMed:3667877). Glycodelin-A is expressed in amniotic fluid,
endometrium/decidua and maternal serum (at protein level)
(PubMed:3194393). Glycodelin-F is expressed in follicular fluid,
luteinized granulosa cells and the oviduct (at protein level)
(PubMed:12672671). Glycodelin-S is expressed in seminal plasma and
seminal vesicles (at protein level) (PubMed:9239694). Glycodelin-C
is detected in cumulus cells (at protein level), but cumulus cells
do not synthesize Glycodelin-C but take up and convert glycodelin-
A and -F vis glycan remodeling (PubMed:17192260).
{ECO:0000269|PubMed:12672671, ECO:0000269|PubMed:17192260,
ECO:0000269|PubMed:3194393, ECO:0000269|PubMed:3667877,
ECO:0000269|PubMed:9239694}.
-!- PTM: Four distinct glycoforms A, C, F and S arise from different
N-linked oligosaccharide chains at amino acid residues Asn-46 and
Asn-81. Glycodelin-A and -F are taken up by the cumulus cells in
which partial deglycosylation takes place to produce glycodelin-C.
{ECO:0000269|PubMed:12672671, ECO:0000269|PubMed:17192260,
ECO:0000269|PubMed:7592613, ECO:0000269|PubMed:8943270}.
-!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA60147.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAB43305.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PAEPID46067ch9q34.html";
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EMBL; J04129; AAA60147.1; ALT_INIT; mRNA.
EMBL; M34046; AAA60148.1; -; Genomic_DNA.
EMBL; M61886; AAA35801.1; -; mRNA.
EMBL; M61886; AAA35802.1; -; mRNA.
EMBL; AL050169; CAB43305.1; ALT_INIT; mRNA.
EMBL; AL354761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC069451; AAH69451.1; -; mRNA.
EMBL; BC069562; AAH69562.1; -; mRNA.
EMBL; BC112304; AAI12305.1; -; mRNA.
EMBL; BC113728; AAI13729.1; -; mRNA.
CCDS; CCDS35173.1; -. [P09466-1]
PIR; A35570; A39167.
RefSeq; NP_001018058.1; NM_001018048.1. [P09466-2]
RefSeq; NP_001018059.1; NM_001018049.2. [P09466-1]
RefSeq; NP_002562.2; NM_002571.3. [P09466-1]
RefSeq; XP_011517051.1; XM_011518749.2. [P09466-1]
RefSeq; XP_011517053.1; XM_011518751.1. [P09466-2]
UniGene; Hs.532325; -.
PDB; 4R0B; X-ray; 2.45 A; A=20-180.
PDBsum; 4R0B; -.
ProteinModelPortal; P09466; -.
SMR; P09466; -.
BioGrid; 111084; 19.
IntAct; P09466; 14.
MINT; MINT-1209116; -.
STRING; 9606.ENSP00000277508; -.
DrugBank; DB02405; 12-Bromododecanoic Acid.
DrugBank; DB04077; Glycerol.
DrugBank; DB03796; Palmitic Acid.
iPTMnet; P09466; -.
PhosphoSitePlus; P09466; -.
UniCarbKB; P09466; -.
BioMuta; PAEP; -.
DMDM; 130701; -.
PaxDb; P09466; -.
PeptideAtlas; P09466; -.
PRIDE; P09466; -.
DNASU; 5047; -.
Ensembl; ENST00000277508; ENSP00000277508; ENSG00000122133. [P09466-1]
Ensembl; ENST00000371766; ENSP00000360831; ENSG00000122133. [P09466-1]
Ensembl; ENST00000479141; ENSP00000417898; ENSG00000122133. [P09466-1]
GeneID; 5047; -.
KEGG; hsa:5047; -.
UCSC; uc004cgd.2; human. [P09466-1]
CTD; 5047; -.
DisGeNET; 5047; -.
EuPathDB; HostDB:ENSG00000122133.16; -.
GeneCards; PAEP; -.
HGNC; HGNC:8573; PAEP.
HPA; CAB016762; -.
HPA; HPA020108; -.
HPA; HPA029473; -.
MIM; 173310; gene.
neXtProt; NX_P09466; -.
OpenTargets; ENSG00000122133; -.
PharmGKB; PA32904; -.
eggNOG; ENOG410JCG3; Eukaryota.
eggNOG; ENOG4111386; LUCA.
GeneTree; ENSGT00620000088158; -.
HOGENOM; HOG000113272; -.
HOVERGEN; HBG104361; -.
InParanoid; P09466; -.
OMA; SMMCQYL; -.
OrthoDB; EOG091G0M2T; -.
PhylomeDB; P09466; -.
TreeFam; TF342475; -.
GeneWiki; PAEP; -.
GenomeRNAi; 5047; -.
PRO; PR:P09466; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000122133; -.
CleanEx; HS_PAEP; -.
ExpressionAtlas; P09466; baseline and differential.
Genevisible; P09466; HS.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0036094; F:small molecule binding; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; IDA:CACAO.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
GO; GO:1902491; P:negative regulation of sperm capacitation; IMP:UniProtKB.
GO; GO:0032725; P:positive regulation of granulocyte macrophage colony-stimulating factor production; IDA:CACAO.
GO; GO:2000667; P:positive regulation of interleukin-13 secretion; IDA:CACAO.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; IDA:CACAO.
GO; GO:2000359; P:regulation of binding of sperm to zona pellucida; IDA:UniProtKB.
Gene3D; 2.40.128.20; -; 1.
InterPro; IPR002447; Blactoglobulin.
InterPro; IPR012674; Calycin.
InterPro; IPR002345; Lipocalin.
InterPro; IPR022272; Lipocalin_CS.
InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
PANTHER; PTHR11430; PTHR11430; 1.
Pfam; PF00061; Lipocalin; 1.
PRINTS; PR01172; BLCTOGLOBULN.
SUPFAM; SSF50814; SSF50814; 1.
PROSITE; PS00213; LIPOCALIN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Polymorphism;
Reference proteome; Secreted; Signal.
SIGNAL 1 18 {ECO:0000269|PubMed:11278680,
ECO:0000269|PubMed:3569148,
ECO:0000269|PubMed:3667877}.
CHAIN 19 180 Glycodelin.
/FTId=PRO_0000017953.
CARBOHYD 46 46 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:7592613}.
/FTId=CAR_000123.
CARBOHYD 81 81 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:7592613}.
/FTId=CAR_000124.
DISULFID 84 178 {ECO:0000244|PDB:4R0B,
ECO:0000269|PubMed:25422905}.
DISULFID 124 137 {ECO:0000244|PDB:4R0B,
ECO:0000269|PubMed:25422905}.
VAR_SEQ 33 126 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_003141.
VAR_SEQ 33 54 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_003140.
VARIANT 28 28 L -> V (in dbSNP:rs34284195).
/FTId=VAR_050178.
VARIANT 126 126 Q -> K (in dbSNP:rs3748210).
/FTId=VAR_034355.
CONFLICT 35 37 GTW -> VTA (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 36 36 T -> K (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 95 95 E -> G (in Ref. 1). {ECO:0000305}.
CONFLICT 152 152 Q -> E (in Ref. 1). {ECO:0000305}.
HELIX 30 33 {ECO:0000244|PDB:4R0B}.
STRAND 38 46 {ECO:0000244|PDB:4R0B}.
HELIX 47 49 {ECO:0000244|PDB:4R0B}.
STRAND 60 66 {ECO:0000244|PDB:4R0B}.
STRAND 72 79 {ECO:0000244|PDB:4R0B}.
STRAND 81 93 {ECO:0000244|PDB:4R0B}.
STRAND 99 104 {ECO:0000244|PDB:4R0B}.
STRAND 107 115 {ECO:0000244|PDB:4R0B}.
STRAND 117 127 {ECO:0000244|PDB:4R0B}.
STRAND 129 132 {ECO:0000244|PDB:4R0B}.
STRAND 134 144 {ECO:0000244|PDB:4R0B}.
HELIX 148 158 {ECO:0000244|PDB:4R0B}.
STRAND 159 162 {ECO:0000244|PDB:4R0B}.
STRAND 167 170 {ECO:0000244|PDB:4R0B}.
TURN 173 175 {ECO:0000244|PDB:4R0B}.
SEQUENCE 180 AA; 20624 MW; 0813A74A4231149E CRC64;
MLCLLLTLGV ALVCGVPAMD IPQTKQDLEL PKLAGTWHSM AMATNNISLM ATLKAPLRVH
ITSLLPTPED NLEIVLHRWE NNSCVEKKVL GEKTENPKKF KINYTVANEA TLLDTDYDNF
LFLCLQDTTT PIQSMMCQYL ARVLVEDDEI MQGFIRAFRP LPRHLWYLLD LKQMEEPCRF


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DL-PAEP-Hu Human Progestagen Associated Endometrial Protein (PAEP) ELISA Kit 96T
pro-1397 Recombinant Human Progesterone-Associated Endometrial Protein 1mg
pro-1397 Recombinant Human Progesterone-Associated Endometrial Protein 2


 

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