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Pancreatic triacylglycerol lipase (PL) (PTL) (Pancreatic lipase) (EC 3.1.1.3)

 LIPP_HUMAN              Reviewed;         465 AA.
P16233; Q5VSQ2;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
25-OCT-2017, entry version 183.
RecName: Full=Pancreatic triacylglycerol lipase;
Short=PL;
Short=PTL;
Short=Pancreatic lipase;
EC=3.1.1.3;
Flags: Precursor;
Name=PNLIP;
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=2479644;
Lowe M.E., Rosenblum J.L., Strauss A.W.;
"Cloning and characterization of human pancreatic lipase cDNA.";
J. Biol. Chem. 264:20042-20048(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pancreas;
PubMed=1379598;
Giller T., Buchwald P., Blum-Kaelin D., Hunziker W.;
"Two novel human pancreatic lipase related proteins, hPLRP1 and
hPLRP2. Differences in colipase dependence and in lipase activity.";
J. Biol. Chem. 267:16509-16516(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8406023; DOI=10.1016/0378-1119(93)90307-O;
Sims H.F., Jennens M.L., Lowe M.E.;
"The human pancreatic lipase-encoding gene: structure and conservation
of an Alu sequence in the lipase gene family.";
Gene 131:281-285(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[8]
CATALYTIC ACTIVITY.
PubMed=10769148; DOI=10.1021/bi9927235;
van Bennekum A.M., Fisher E.A., Blaner W.S., Harrison E.H.;
"Hydrolysis of retinyl esters by pancreatic triglyceride lipase.";
Biochemistry 39:4900-4906(2000).
[9]
INVOLVEMENT IN PNLIPD, AND VARIANT PNLIPD MET-221.
PubMed=24262094; DOI=10.1194/jlr.P041103;
Behar D.M., Basel-Vanagaite L., Glaser F., Kaplan M., Tzur S.,
Magal N., Eidlitz-Markus T., Haimi-Cohen Y., Sarig G., Bormans C.,
Shohat M., Zeharia A.;
"Identification of a novel mutation in the PNLIP gene in two brothers
with congenital pancreatic lipase deficiency.";
J. Lipid Res. 55:307-312(2014).
[10]
SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANT PNLIPD MET-221.
PubMed=25862608; DOI=10.1016/j.bbadis.2015.04.002;
Szabo A., Xiao X., Haughney M., Spector A., Sahin-Toth M., Lowe M.E.;
"A novel mutation in PNLIP causes pancreatic triglyceride lipase
deficiency through protein misfolding.";
Biochim. Biophys. Acta 1852:1372-1379(2015).
[11]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=2106079; DOI=10.1038/343771a0;
Winkler F.K., D'Arcy A., Hunziker W.;
"Structure of human pancreatic lipase.";
Nature 343:771-774(1990).
[12]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH CLPS.
PubMed=1522902; DOI=10.1038/359159a0;
van Tilbeurgh H., Sarda L., Verger R., Cambillau C.;
"Structure of the pancreatic lipase-procolipase complex.";
Nature 359:159-162(1992).
[13]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH CLPS.
PubMed=8479519; DOI=10.1038/362814a0;
van Tilbeurgh H., Egloff M.-P., Martinez C., Rugani N., Verger R.,
Cambillau C.;
"Interfacial activation of the lipase-procolipase complex by mixed
micelles revealed by X-ray crystallography.";
Nature 362:814-820(1993).
[14]
STRUCTURE BY NMR OF 354-465.
PubMed=8029213; DOI=10.1093/protein/7.4.563;
Carriere F., Thirstrup K., Boel E., Verger R., Thim L.;
"Structure-function relationships in naturally occurring mutants of
pancreatic lipase.";
Protein Eng. 7:563-569(1994).
-!- CATALYTIC ACTIVITY: Triacylglycerol + H(2)O = diacylglycerol + a
carboxylate. {ECO:0000269|PubMed:10769148}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25862608}.
-!- INDUCTION: By colipase/CLPS in the presence of bile salts.
-!- DISEASE: Pancreatic lipase deficiency (PNLIPD) [MIM:614338]: An
autosomal recessive disorder characterized by exocrine pancreatic
failure. Clinical findings include oily/greasy stools from infancy
or early childhood, absence of discernible pancreatic disease, and
significantly decreased pancreatic lipolytic activity.
{ECO:0000269|PubMed:24262094, ECO:0000269|PubMed:25862608}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Pancreatic lipase entry;
URL="https://en.wikipedia.org/wiki/Pancreatic_lipase";
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EMBL; J05125; AAA36740.1; -; mRNA.
EMBL; M93285; AAA60129.1; -; mRNA.
EMBL; L24529; AAA99053.1; -; Genomic_DNA.
EMBL; L11242; AAA99053.1; JOINED; Genomic_DNA.
EMBL; L24502; AAA99053.1; JOINED; Genomic_DNA.
EMBL; L24522; AAA99053.1; JOINED; Genomic_DNA.
EMBL; L24523; AAA99053.1; JOINED; Genomic_DNA.
EMBL; L24525; AAA99053.1; JOINED; Genomic_DNA.
EMBL; L24526; AAA99053.1; JOINED; Genomic_DNA.
EMBL; L24527; AAA99053.1; JOINED; Genomic_DNA.
EMBL; L24528; AAA99053.1; JOINED; Genomic_DNA.
EMBL; AK313941; BAG36659.1; -; mRNA.
EMBL; AL731653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471066; EAW49451.1; -; Genomic_DNA.
EMBL; BC014309; AAH14309.1; -; mRNA.
CCDS; CCDS7594.1; -.
PIR; C43357; C43357.
RefSeq; NP_000927.1; NM_000936.3.
UniGene; Hs.501135; -.
PDB; 1LPA; X-ray; 3.04 A; B=17-465.
PDB; 1LPB; X-ray; 2.46 A; B=17-465.
PDB; 1N8S; X-ray; 3.04 A; A=17-465.
PDBsum; 1LPA; -.
PDBsum; 1LPB; -.
PDBsum; 1N8S; -.
ProteinModelPortal; P16233; -.
SMR; P16233; -.
BioGrid; 111407; 10.
IntAct; P16233; 1.
MINT; MINT-1179407; -.
STRING; 9606.ENSP00000358223; -.
BindingDB; P16233; -.
ChEMBL; CHEMBL1812; -.
DrugBank; DB04233; (Hydroxyethyloxy)Tri(Ethyloxy)Octane.
DrugBank; DB08909; Glycerol Phenylbutyrate.
DrugBank; DB08222; METHOXYUNDECYLPHOSPHINIC ACID.
DrugBank; DB01083; Orlistat.
GuidetoPHARMACOLOGY; 2590; -.
SwissLipids; SLP:000000529; -.
ESTHER; human-PNLIP; Pancreatic_lipase.
iPTMnet; P16233; -.
PhosphoSitePlus; P16233; -.
BioMuta; PNLIP; -.
DMDM; 126318; -.
PaxDb; P16233; -.
PeptideAtlas; P16233; -.
PRIDE; P16233; -.
Ensembl; ENST00000369221; ENSP00000358223; ENSG00000175535.
GeneID; 5406; -.
KEGG; hsa:5406; -.
UCSC; uc001lcm.4; human.
CTD; 5406; -.
DisGeNET; 5406; -.
EuPathDB; HostDB:ENSG00000175535.6; -.
GeneCards; PNLIP; -.
HGNC; HGNC:9155; PNLIP.
HPA; HPA062430; -.
HPA; HPA062494; -.
MalaCards; PNLIP; -.
MIM; 246600; gene.
MIM; 614338; phenotype.
neXtProt; NX_P16233; -.
OpenTargets; ENSG00000175535; -.
PharmGKB; PA33478; -.
eggNOG; ENOG410IHRX; Eukaryota.
eggNOG; ENOG410Y92X; LUCA.
GeneTree; ENSGT00760000119069; -.
HOGENOM; HOG000038552; -.
HOVERGEN; HBG003243; -.
InParanoid; P16233; -.
KO; K14073; -.
OMA; MSQVVGH; -.
OrthoDB; EOG091G0DJ5; -.
PhylomeDB; P16233; -.
TreeFam; TF324997; -.
BioCyc; MetaCyc:HS10947-MONOMER; -.
Reactome; R-HSA-192456; Digestion of dietary lipid.
Reactome; R-HSA-975634; Retinoid metabolism and transport.
SABIO-RK; P16233; -.
ChiTaRS; PNLIP; human.
EvolutionaryTrace; P16233; -.
GeneWiki; Pancreatic_lipase; -.
GenomeRNAi; 5406; -.
PRO; PR:P16233; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000175535; -.
CleanEx; HS_PNLIP; -.
Genevisible; P16233; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0016298; F:lipase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004806; F:triglyceride lipase activity; ISS:UniProtKB.
GO; GO:0030299; P:intestinal cholesterol absorption; IEA:Ensembl.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0044241; P:lipid digestion; TAS:Reactome.
GO; GO:0006629; P:lipid metabolic process; IMP:UniProtKB.
GO; GO:0061365; P:positive regulation of triglyceride lipase activity; IDA:CACAO.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
CDD; cd00707; Pancreat_lipase_like; 1.
Gene3D; 2.60.60.20; -; 1.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR013818; Lipase/vitellogenin.
InterPro; IPR016272; Lipase_LIPH.
InterPro; IPR033906; Lipase_N.
InterPro; IPR002331; Lipase_panc.
InterPro; IPR001024; PLAT/LH2_dom.
InterPro; IPR036392; PLAT/LH2_dom_sf.
InterPro; IPR000734; TAG_lipase.
PANTHER; PTHR11610; PTHR11610; 1.
Pfam; PF00151; Lipase; 1.
Pfam; PF01477; PLAT; 1.
PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
PRINTS; PR00823; PANCLIPASE.
PRINTS; PR00821; TAGLIPASE.
SMART; SM00308; LH2; 1.
SUPFAM; SSF49723; SSF49723; 1.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00120; LIPASE_SER; 1.
PROSITE; PS50095; PLAT; 1.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Disease mutation;
Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
Lipid metabolism; Metal-binding; Reference proteome; Secreted; Signal.
SIGNAL 1 16
CHAIN 17 465 Pancreatic triacylglycerol lipase.
/FTId=PRO_0000017785.
DOMAIN 355 465 PLAT. {ECO:0000255|PROSITE-
ProRule:PRU00152}.
ACT_SITE 169 169 Nucleophile.
ACT_SITE 193 193 Charge relay system.
ACT_SITE 280 280 Charge relay system.
METAL 204 204 Calcium; via carbonyl oxygen.
METAL 207 207 Calcium; via carbonyl oxygen.
METAL 209 209 Calcium.
METAL 212 212 Calcium.
CARBOHYD 183 183 N-linked (GlcNAc...) asparagine.
DISULFID 20 26
DISULFID 107 118
DISULFID 254 278
DISULFID 302 313
DISULFID 316 321
DISULFID 449 465
VARIANT 221 221 T -> M (in PNLIPD; loss of function in
lipid catabolic process; the mutant is
not secreted; dbSNP:rs746000327).
{ECO:0000269|PubMed:24262094,
ECO:0000269|PubMed:25862608}.
/FTId=VAR_078977.
STRAND 18 21 {ECO:0000244|PDB:1LPB}.
TURN 22 24 {ECO:0000244|PDB:1LPB}.
STRAND 25 28 {ECO:0000244|PDB:1LPB}.
TURN 31 33 {ECO:0000244|PDB:1LPB}.
STRAND 34 38 {ECO:0000244|PDB:1LPB}.
HELIX 48 51 {ECO:0000244|PDB:1LPB}.
STRAND 54 58 {ECO:0000244|PDB:1LPB}.
STRAND 60 65 {ECO:0000244|PDB:1LPB}.
STRAND 67 69 {ECO:0000244|PDB:1LPB}.
HELIX 73 78 {ECO:0000244|PDB:1LPB}.
STRAND 87 91 {ECO:0000244|PDB:1LPB}.
HELIX 101 110 {ECO:0000244|PDB:1LPB}.
TURN 111 113 {ECO:0000244|PDB:1LPB}.
STRAND 117 122 {ECO:0000244|PDB:1LPB}.
HELIX 124 127 {ECO:0000244|PDB:1LPB}.
HELIX 131 156 {ECO:0000244|PDB:1LPB}.
HELIX 160 162 {ECO:0000244|PDB:1LPB}.
STRAND 163 168 {ECO:0000244|PDB:1LPB}.
HELIX 170 180 {ECO:0000244|PDB:1LPB}.
TURN 181 184 {ECO:0000244|PDB:1LPB}.
STRAND 186 193 {ECO:0000244|PDB:1LPB}.
TURN 197 201 {ECO:0000244|PDB:1LPB}.
TURN 204 206 {ECO:0000244|PDB:1LPB}.
HELIX 210 212 {ECO:0000244|PDB:1LPB}.
STRAND 216 219 {ECO:0000244|PDB:1LPB}.
TURN 227 229 {ECO:0000244|PDB:1LPB}.
STRAND 239 245 {ECO:0000244|PDB:1LPB}.
STRAND 248 250 {ECO:0000244|PDB:1LPB}.
HELIX 258 262 {ECO:0000244|PDB:1LPB}.
HELIX 268 291 {ECO:0000244|PDB:1LPB}.
TURN 294 297 {ECO:0000244|PDB:1LPB}.
HELIX 305 309 {ECO:0000244|PDB:1LPB}.
STRAND 323 325 {ECO:0000244|PDB:1LPB}.
HELIX 328 330 {ECO:0000244|PDB:1LPB}.
TURN 332 335 {ECO:0000244|PDB:1LPB}.
STRAND 336 344 {ECO:0000244|PDB:1LPB}.
STRAND 348 351 {ECO:0000244|PDB:1LPB}.
STRAND 355 365 {ECO:0000244|PDB:1LPB}.
STRAND 368 378 {ECO:0000244|PDB:1LPB}.
STRAND 386 393 {ECO:0000244|PDB:1LPB}.
STRAND 398 407 {ECO:0000244|PDB:1LPB}.
STRAND 411 420 {ECO:0000244|PDB:1LPB}.
STRAND 431 440 {ECO:0000244|PDB:1LPB}.
STRAND 445 449 {ECO:0000244|PDB:1LPB}.
STRAND 460 464 {ECO:0000244|PDB:1LPB}.
SEQUENCE 465 AA; 51157 MW; 2BC49CC7F0E2DF52 CRC64;
MLPLWTLSLL LGAVAGKEVC YERLGCFSDD SPWSGITERP LHILPWSPKD VNTRFLLYTN
ENPNNFQEVA ADSSSISGSN FKTNRKTRFI IHGFIDKGEE NWLANVCKNL FKVESVNCIC
VDWKGGSRTG YTQASQNIRI VGAEVAYFVE FLQSAFGYSP SNVHVIGHSL GAHAAGEAGR
RTNGTIGRIT GLDPAEPCFQ GTPELVRLDP SDAKFVDVIH TDGAPIVPNL GFGMSQVVGH
LDFFPNGGVE MPGCKKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPDGFAGF
PCASYNVFTA NKCFPCPSGG CPQMGHYADR YPGKTNDVGQ KFYLDTGDAS NFARWRYKVS
VTLSGKKVTG HILVSLFGNK GNSKQYEIFK GTLKPDSTHS NEFDSDVDVG DLQMVKFIWY
NNVINPTLPR VGASKIIVET NVGKQFNFCS PETVREEVLL TLTPC


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YHB0822Ra Rat Pancreatic triacylglycerol lipase,PNLIP ELISA Kit 48T
E1123Ra Rat Pancreatic triacylglycerol lipase,PNLIP ELISA Kit 96T
YHB0822Ra Rat Pancreatic triacylglycerol lipase,PNLIP ELISA Kit 96T
CSB-EL018262DO Dog Pancreatic triacylglycerol lipase(PNLIP) ELISA kit 96T
E1122Ra Rat Pancreatic triacylglycerol lipase,PNLIP ELISA Kit 48T
CSB-EL018262CA Cat Pancreatic triacylglycerol lipase(PNLIP) ELISA kit 96T
E1123Ra Rat Pancreatic triacylglycerol lipase,PNLIP ELISA Kit 48T


 

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