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Proprotein convertase subtilisin/kexin type 5 (EC 3.4.21.-) (Proprotein convertase 5) (PC5) (Proprotein convertase 6) (PC6) (Subtilisin-like proprotein convertase 6) (SPC6) (Subtilisin/kexin-like protease PC5)

 PCSK5_MOUSE             Reviewed;        1877 AA.
Q04592; E9QPB7; Q62040;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
12-SEP-2018, entry version 171.
RecName: Full=Proprotein convertase subtilisin/kexin type 5;
EC=3.4.21.-;
AltName: Full=Proprotein convertase 5;
Short=PC5;
AltName: Full=Proprotein convertase 6;
Short=PC6;
AltName: Full=Subtilisin-like proprotein convertase 6;
Short=SPC6;
AltName: Full=Subtilisin/kexin-like protease PC5;
Flags: Precursor;
Name=Pcsk5;
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] OF 330-1877 (ISOFORM PC5B).
STRAIN=ICR; TISSUE=Intestine;
PubMed=8335106; DOI=10.1016/0014-5793(93)80163-O;
Nakagawa T., Murakami K., Nakayama K.;
"Identification of an isoform with an extremely large Cys-rich region
of PC6, a Kex2-like processing endoprotease.";
FEBS Lett. 327:165-171(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PC5A).
TISSUE=Brain, and Intestine;
PubMed=8468318;
Nakagawa T., Hosaka M., Torii S., Watanabe T., Murakami K.,
Nakayama K.;
"Identification and functional expression of a new member of the
mammalian Kex2-like processing endoprotease family: its striking
structural similarity to PACE4.";
J. Biochem. 113:132-135(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PC5A).
TISSUE=Adrenal cortex;
PubMed=8341687; DOI=10.1073/pnas.90.14.6691;
Lusson J., Vieau D., Hamelin J., Day R., Chretien M., Seidah N.G.;
"cDNA structure of the mouse and rat subtilisin/kexin-like PC5: a
candidate proprotein convertase expressed in endocrine and
nonendocrine cells.";
Proc. Natl. Acad. Sci. U.S.A. 90:6691-6695(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
PARTIAL PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
PubMed=8947550; DOI=10.1083/jcb.135.5.1261;
De Bie I., Marcinkiewicz M., Malide D., Lazure C., Nakayama K.,
Bendayan M., Seidah N.G.;
"The isoforms of proprotein convertase PC5 are sorted to different
subcellular compartments.";
J. Cell Biol. 135:1261-1275(1996).
[6]
DEVELOPMENTAL STAGE.
PubMed=8698813; DOI=10.1083/jcb.134.1.181;
Constam D.B., Calfon M., Robertson E.J.;
"SPC4, SPC6, and the novel protease SPC7 are coexpressed with bone
morphogenetic proteins at distinct sites during embryogenesis.";
J. Cell Biol. 134:181-191(1996).
[7]
DEVELOPMENTAL STAGE.
PubMed=9291583;
DOI=10.1002/(SICI)1520-6408(1997)21:1<75::AID-DVG9>3.0.CO;2-5;
Rancourt S.L., Rancourt D.E.;
"Murine subtilisin-like proteinase SPC6 is expressed during embryonic
implantation, somitogenesis, and skeletal formation.";
Dev. Genet. 21:75-81(1997).
-!- FUNCTION: Serine endoprotease that processes various proproteins
by cleavage at paired basic amino acids, recognizing the RXXX[KR]R
consensus motif. Likely functions in the constitutive and
regulated secretory pathways. Plays an essential role in pregnancy
establishment by proteolytic activation of a number of important
factors such as BMP2, CALD1 and alpha-integrins. May be
responsible for the maturation of gastrointestinal peptides. May
be involved in the cellular proliferation of adrenal cortex via
the activation of growth factors. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform PC5A: Secreted. Note=Secreted
through the regulated secretory pathway.
-!- SUBCELLULAR LOCATION: Isoform PC5B: Endomembrane system; Single-
pass type I membrane protein. Note=Type I membrane protein
localized to a paranuclear post-Golgi network compartment in
communication with early endosomes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms seem to exist.;
Name=PC5B; Synonyms=Long;
IsoId=Q04592-1; Sequence=Displayed;
Name=PC5A; Synonyms=Short;
IsoId=Q04592-2; Sequence=VSP_005438, VSP_005439;
-!- TISSUE SPECIFICITY: PC5A is expressed in most tissues but is most
abundant in the intestine and adrenals. PC5B is expressed in the
intestine, adrenals and lung but not in the brain.
-!- DEVELOPMENTAL STAGE: Weakly expressed throughout the embryo,
except in the developing nervous system, the ribs and the liver,
but markedly up-regulated at discrete sites during development. At
E6.5, prominent expression observed in differentiated decidua. At
E7.5, intense expression in extraembryonic endoderm, amnion and
nascent mesoderm. At E8.5, abundant expression in somites and yolk
sac followed by a confinement to dermamyotome compartment. Between
E9.5 and E11.5, abundant expression in AER (thickened ectodermal
cells of limb buds). At E12.5, expression in the limbs is confined
to the condensing mesenchyme surrounding the cartilage. At this
stage, strong expression also detected in vertebral and facial
cartilage primordia and in the muscle of the tongue. At E16.5,
abundant expression in epithelial cells of the intestinal villi.
Isoform A is most abundant at all stages but significant levels of
isoform B occur at E12.5. {ECO:0000269|PubMed:8698813,
ECO:0000269|PubMed:9291583}.
-!- DOMAIN: The propeptide domain acts as an intramolecular chaperone
assisting the folding of the zymogen within the endoplasmic
reticulum.
-!- DOMAIN: AC 1 and AC 2 (clusters of acidic amino acids) contain
sorting information. AC 1 directs TGN localization and interacts
with the TGN sorting protein PACS-1.
-!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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EMBL; D17583; BAA04507.1; -; mRNA.
EMBL; D12619; BAA02143.1; -; mRNA.
EMBL; L14932; AAA74636.1; -; mRNA.
EMBL; AC125203; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC126940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC133509; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC147369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS50401.1; -. [Q04592-1]
CCDS; CCDS50402.1; -. [Q04592-2]
PIR; A48225; A48225.
PIR; S34583; S34583.
RefSeq; NP_001177412.1; NM_001190483.2. [Q04592-1]
UniGene; Mm.3401; -.
ProteinModelPortal; Q04592; -.
SMR; Q04592; -.
BioGrid; 202061; 4.
IntAct; Q04592; 1.
MINT; Q04592; -.
STRING; 10090.ENSMUSP00000025618; -.
iPTMnet; Q04592; -.
PhosphoSitePlus; Q04592; -.
MaxQB; Q04592; -.
PaxDb; Q04592; -.
PeptideAtlas; Q04592; -.
PRIDE; Q04592; -.
Ensembl; ENSMUST00000025618; ENSMUSP00000025618; ENSMUSG00000024713. [Q04592-1]
Ensembl; ENSMUST00000050715; ENSMUSP00000050272; ENSMUSG00000024713. [Q04592-2]
GeneID; 18552; -.
KEGG; mmu:18552; -.
UCSC; uc008gxp.2; mouse. [Q04592-1]
CTD; 5125; -.
MGI; MGI:97515; Pcsk5.
eggNOG; KOG3525; Eukaryota.
eggNOG; COG1404; LUCA.
eggNOG; COG4935; LUCA.
GeneTree; ENSGT00750000117358; -.
HOGENOM; HOG000192536; -.
HOVERGEN; HBG008705; -.
InParanoid; Q04592; -.
KO; K08654; -.
OMA; SSCRTCE; -.
OrthoDB; EOG091G05HI; -.
TreeFam; TF314277; -.
BRENDA; 3.4.21.B26; 3474.
Reactome; R-MMU-167060; NGF processing.
Reactome; R-MMU-8963889; Assembly of active LPL and LIPC lipase complexes.
ChiTaRS; Pcsk5; mouse.
PRO; PR:Q04592; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000024713; Expressed in 260 organ(s), highest expression level in cumulus cell.
CleanEx; MM_PCSK5; -.
ExpressionAtlas; Q04592; baseline and differential.
Genevisible; Q04592; MM.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0005797; C:Golgi medial cisterna; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043204; C:perikaryon; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:1990635; C:proximal dendrite; ISO:MGI.
GO; GO:0030141; C:secretory granule; IDA:MGI.
GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
GO; GO:0004175; F:endopeptidase activity; IDA:BHF-UCL.
GO; GO:0008233; F:peptidase activity; ISO:MGI.
GO; GO:0042277; F:peptide binding; IDA:BHF-UCL.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:BHF-UCL.
GO; GO:0009952; P:anterior/posterior pattern specification; IMP:BHF-UCL.
GO; GO:0003279; P:cardiac septum development; IMP:MGI.
GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
GO; GO:0042089; P:cytokine biosynthetic process; IDA:BHF-UCL.
GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
GO; GO:0007566; P:embryo implantation; IMP:BHF-UCL.
GO; GO:0048566; P:embryonic digestive tract development; IMP:BHF-UCL.
GO; GO:0048706; P:embryonic skeletal system development; IMP:BHF-UCL.
GO; GO:0007507; P:heart development; IMP:BHF-UCL.
GO; GO:0001822; P:kidney development; IMP:BHF-UCL.
GO; GO:0035108; P:limb morphogenesis; IMP:BHF-UCL.
GO; GO:0043043; P:peptide biosynthetic process; IDA:BHF-UCL.
GO; GO:0016486; P:peptide hormone processing; IDA:BHF-UCL.
GO; GO:0033625; P:positive regulation of integrin activation; ISO:MGI.
GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; ISO:MGI.
GO; GO:1905609; P:positive regulation of smooth muscle cell-matrix adhesion; ISO:MGI.
GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; ISO:MGI.
GO; GO:0016485; P:protein processing; IDA:BHF-UCL.
GO; GO:0002001; P:renin secretion into blood stream; IEA:Ensembl.
GO; GO:0030323; P:respiratory tube development; IMP:BHF-UCL.
GO; GO:0006465; P:signal peptide processing; ISO:MGI.
GO; GO:0019058; P:viral life cycle; IDA:BHF-UCL.
CDD; cd00064; FU; 17.
CDD; cd04059; Peptidases_S8_Protein_converta; 1.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 3.30.70.850; -; 1.
Gene3D; 3.40.50.200; -; 1.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR006212; Furin_repeat.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR032778; GF_recep_IV.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR034182; Kexin/furin.
InterPro; IPR002884; P_dom.
InterPro; IPR000209; Peptidase_S8/S53_dom.
InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
InterPro; IPR023827; Peptidase_S8_Asp-AS.
InterPro; IPR022398; Peptidase_S8_His-AS.
InterPro; IPR023828; Peptidase_S8_Ser-AS.
InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
InterPro; IPR032815; S8_pro-domain.
InterPro; IPR038466; S8_pro-domain_sf.
Pfam; PF15913; Furin-like_2; 1.
Pfam; PF14843; GF_recep_IV; 2.
Pfam; PF01483; P_proprotein; 1.
Pfam; PF00082; Peptidase_S8; 1.
Pfam; PF16470; S8_pro-domain; 1.
PRINTS; PR00723; SUBTILISIN.
SMART; SM00181; EGF; 18.
SMART; SM00261; FU; 22.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF52743; SSF52743; 1.
SUPFAM; SSF57184; SSF57184; 8.
PROSITE; PS51829; P_HOMO_B; 1.
PROSITE; PS00136; SUBTILASE_ASP; 1.
PROSITE; PS00137; SUBTILASE_HIS; 1.
PROSITE; PS00138; SUBTILASE_SER; 1.
1: Evidence at protein level;
Alternative splicing; Cleavage on pair of basic residues;
Complete proteome; Direct protein sequencing; Glycoprotein; Hydrolase;
Membrane; Pregnancy; Protease; Reference proteome; Repeat; Secreted;
Serine protease; Signal; Transmembrane; Transmembrane helix; Zymogen.
SIGNAL 1 34
PROPEP 35 116
/FTId=PRO_0000027104.
CHAIN 117 1877 Proprotein convertase subtilisin/kexin
type 5.
/FTId=PRO_0000027105.
TOPO_DOM 117 1768 Extracellular. {ECO:0000255}.
TRANSMEM 1769 1789 Helical. {ECO:0000255}.
TOPO_DOM 1790 1877 Cytoplasmic. {ECO:0000255}.
DOMAIN 168 455 Peptidase S8.
DOMAIN 463 603 P/Homo B. {ECO:0000255|PROSITE-
ProRule:PRU01173}.
REPEAT 632 682 FU 1.
REPEAT 685 732 FU 2.
REPEAT 736 779 FU 3.
REPEAT 781 826 FU 4.
REPEAT 834 881 FU 5.
REPEAT 884 929 FU 6.
REPEAT 931 981 FU 7.
REPEAT 984 1030 FU 8.
REPEAT 1034 1079 FU 9.
REPEAT 1081 1123 FU 10.
REPEAT 1127 1168 FU 11.
REPEAT 1206 1248 FU 12.
REPEAT 1252 1299 FU 13.
REPEAT 1301 1345 FU 14.
REPEAT 1347 1390 FU 15.
REPEAT 1392 1438 FU 16.
REPEAT 1442 1487 FU 17.
REPEAT 1491 1536 FU 18.
REPEAT 1540 1585 FU 19.
REPEAT 1589 1636 FU 20.
REPEAT 1640 1685 FU 21.
REPEAT 1691 1738 FU 22.
REGION 638 1753 CRM (Cys-rich motif).
REGION 1825 1844 AC 1.
REGION 1856 1877 AC 2.
MOTIF 521 523 Cell attachment site. {ECO:0000255}.
ACT_SITE 173 173 Charge relay system. {ECO:0000250}.
ACT_SITE 214 214 Charge relay system. {ECO:0000250}.
ACT_SITE 388 388 Charge relay system. {ECO:0000250}.
SITE 116 117 Cleavage; by autolysis. {ECO:0000250}.
CARBOHYD 227 227 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 383 383 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 667 667 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 754 754 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 804 804 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 854 854 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 951 951 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1016 1016 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1220 1220 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1317 1317 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1523 1523 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1711 1711 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1733 1733 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 878 915 GEYIDDQGHCQTCEASCAKCWGPTQEDCISCPVTRVLD ->
ATEESWAEGGFCMLVKKNNLCQRKVLQQLCCKTCTFQG
(in isoform PC5A).
{ECO:0000303|PubMed:8341687,
ECO:0000303|PubMed:8468318}.
/FTId=VSP_005438.
VAR_SEQ 916 1877 Missing (in isoform PC5A).
{ECO:0000303|PubMed:8341687,
ECO:0000303|PubMed:8468318}.
/FTId=VSP_005439.
CONFLICT 704 704 N -> D (in Ref. 1; BAA04507, 2; BAA02143
and 3; AAA74636). {ECO:0000305}.
CONFLICT 986 986 A -> T (in Ref. 1; BAA04507).
{ECO:0000305}.
CONFLICT 1002 1002 V -> I (in Ref. 1; BAA04507).
{ECO:0000305}.
CONFLICT 1139 1139 N -> T (in Ref. 1; BAA04507).
{ECO:0000305}.
SEQUENCE 1877 AA; 209257 MW; 68F7B768E063872B CRC64;
MDWDWGNRCS RPGRRDLLCV LALLAGCLLP VCRTRVYTNH WAVKIAGGFA EADRIASKYG
FINVGQIGAL KDYYHFYHSR TIKRSVLSSR GTHSFISMEP KVEWIQQQVV KKRTKRDYDL
SHAQSTYFND PKWPSMWYMH CSDNTHPCQS DMNIEGAWKR GYTGKNIVVT ILDDGIERTH
PDLMQNYDAL ASCDVNGNDL DPMPRYDASN ENKHGTRCAG EVAATANNSH CTVGIAFNAK
IGGVRMLDGD VTDMVEAKSV SYNPQHVHIY SASWGPDDDG KTVDGPAPLT RQAFENGVRM
GRRGLGSVFV WASGNGGRSK DHCSCDGYTN SIYTISISST AESGKKPWYL EECSSTLATT
YSSGESYDKK IITTDLRQRC TDNHTGTSAS APMAAGIIAL ALEANPFLTW RDVQHVIVRT
SRAGHLNAND WKTNAAGFKV SHLYGFGLMD AEAMVMEAEK WTTVPQQHVC VESTDRQIKT
IRPNSAVRSI YKASGCSDNP NHHVNYLEHV VVRITITHPR RGDLAIYLTS PSGTRSQLLA
NRLFDHSMEG FKNWEFMTIH CWGERAAGDW VLEVYDTPSQ LRNFKTPGKL KEWSLVLYGT
SVQPYSPTNE FPKVERFRYS RVEDPTDDYG AEDYAGPCDP ECSEVGCDGP GPDHCSDCLH
YYYKLKNNTR ICVSSCPPGH YHADKKRCRK CAPNCESCFG SHGNQCLSCK YGYFLNEETS
SCVTQCPDGS YEDIKKNVCG KCSENCKACI GFHNCTECKG GLSLQGSRCS VTCEDGQFFN
GHDCQPCHRF CATCSGAGAD GCINCTEGYV MEEGRCVQSC SVSYYLDHSS EGGYKSCKRC
DNSCLTCNGP GFKNCSSCPS GYLLDLGTCQ MGAICKDGEY IDDQGHCQTC EASCAKCWGP
TQEDCISCPV TRVLDDGRCV MNCPSWKFEF KKQCHPCHYT CQGCQGSGPS NCTSCRADKH
GQERFLYHGE CLENCPVGHY PAKGHACLPC PDNCELCYNP HVCSRCMSGY VIIPPNHTCQ
KLECRQGEFQ DSEYEECMPC EEGCLGCTED DPGACTSCAT GYYMFERHCY KACPEKTFGV
KWECRACGTN CGSCDQHECY WCEEGFFLSG GSCVQDCGPG FHGDQELGEC KPCHRACENC
TGSGYNQCSS CQEGLQLWHG TCLWSTWPQV EGKDWNEAVP TEKPSLVRSL LQDRRKWKVQ
IKRDATSQNQ PCHSSCKTCN GSLCASCPTG MYLWLQACVP SCPQGTWPSV TSGSCEKCSE
DCVSCSGADL CQQCLSQPDN TLLLHEGRCY HSCPEGFYAK DGVCEHCSSP CKTCEGNATS
CNSCEGDFVL DHGVCWKTCP EKHVAVEGVC KHCPERCQDC IHEKTCKECM PDFFLYNDMC
HRSCPKSFYP DMRQCVPCHK NCLECNGPKE DDCKVCADTS KALHNGLCLD ECPEGTYKEE
ENDECRDCPE SCLICSSAWT CLACREGFTV VHDVCTAPKE CAAVEYWDEG SHRCQPCHKK
CSRCSGPSED QCYTCPRETF LLNTTCVKEC PEGYHTDKDS QQCVLCHSSC RTCEGPHSMQ
CLSCRPGWFQ LGKECLLQCR DGYYGESTSG RCEKCDKSCK SCRGPRPTDC QSCDTFFFLL
RSKGQCHRAC PEHYYADQHA QTCERCHPTC DKCSGKEAWS CLSCVWSYHL LKGICIPECI
VGEYREGKGE NFNCKKCHES CMECKGPGSK NCTGCSAGLL LDMDDNRCLH CCNASHSRRS
QDCCDCQSST DECILPAREA EFYEHTKTAL LVTSGAMLLL LLGAAAVVWR KSRSRPVAKG
RYEKLAEPTV SYSSYRSSYL DEDQVIEYRD RDYDEDDEDD IVYMGQDGTV YRKFKYGLLD
ETEDDELEYD DESYSYQ


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UB-E10517 Rat Proprotein Convertase Subtilisin per Kexin Type 9(PCSK9)ELISA kit 96T
C250 Human Proprotein Convertase Subtilisin Kexin Type 9 Pcsk9 l0


 

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