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Mannan-binding lectin serine protease 1 (EC 3.4.21.-) (Complement factor MASP-3) (Complement-activating component of Ra-reactive factor) (Mannose-binding lectin-associated serine protease 1) (MASP-1) (Mannose-binding protein-associated serine protease) (Ra-reactive factor serine protease p100) (RaRF) (Serine protease 5) [Cleaved into: Mannan-binding lectin serine protease 1 heavy chain; Mannan-binding lectin serine protease 1 light chain]

 MASP1_MOUSE             Reviewed;         704 AA.
P98064; A2RRH8; A2RRH9; Q8CD27; Q8CIR8; Q920S0;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
14-APR-2009, sequence version 2.
12-SEP-2018, entry version 158.
RecName: Full=Mannan-binding lectin serine protease 1;
EC=3.4.21.-;
AltName: Full=Complement factor MASP-3;
AltName: Full=Complement-activating component of Ra-reactive factor;
AltName: Full=Mannose-binding lectin-associated serine protease 1;
Short=MASP-1;
AltName: Full=Mannose-binding protein-associated serine protease;
AltName: Full=Ra-reactive factor serine protease p100;
Short=RaRF;
AltName: Full=Serine protease 5;
Contains:
RecName: Full=Mannan-binding lectin serine protease 1 heavy chain;
Contains:
RecName: Full=Mannan-binding lectin serine protease 1 light chain;
Flags: Precursor;
Name=Masp1; Synonyms=Crarf, Masp3;
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] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=8133044;
Takayama Y., Takada F., Takahashi A., Kawakami M.;
"A 100-kDa protein in the C4-activating component of Ra-reactive
factor is a new serine protease having module organization similar to
C1r and C1s.";
J. Immunol. 152:2308-2316(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), AND ALTERNATIVE
SPLICING (ISOFORM 1).
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=12847554; DOI=10.1038/sj.gene.6363970;
Stover C.M., Lynch N.J., Dahl M.R., Hanson S., Takahashi M.,
Frankenberger M., Ziegler-Heitbrock L., Eperon I., Thiel S.,
Schwaeble W.J.;
"Murine serine proteases MASP-1 and MASP-3, components of the lectin
pathway activation complex of complement, are encoded by a single
structural gene.";
Genes Immun. 4:374-384(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 465-704 (ISOFORM 1), AND PARTIAL PROTEIN
SEQUENCE.
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=8439319; DOI=10.1006/bbrc.1993.1103;
Takahashi A., Takayama Y., Hatsuse H., Kawakami M.;
"Presence of a serine protease in the complement-activating component
of the complement-dependent bactericidal factor, RaRF, in mouse
serum.";
Biochem. Biophys. Res. Commun. 190:681-687(1993).
[7]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=18424734; DOI=10.4049/jimmunol.180.9.6132;
Takahashi M., Iwaki D., Kanno K., Ishida Y., Xiong J., Matsushita M.,
Endo Y., Miura S., Ishii N., Sugamura K., Fujita T.;
"Mannose-binding lectin (MBL)-associated serine protease (MASP)-1
contributes to activation of the lectin complement pathway.";
J. Immunol. 180:6132-6138(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
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).
-!- FUNCTION: Functions in the lectin pathway of complement, which
performs a key role in innate immunity by recognizing pathogens
through patterns of sugar moieties and neutralizing them. The
lectin pathway is triggered upon binding of mannan-binding lectin
(MBL) and ficolins to sugar moieties which leads to activation of
the associated proteases MASP1 and MASP2. Functions as an
endopeptidase and may activate MASP2 or C2 or directly activate C3
the key component of complement reaction. Isoform 2 may have an
inhibitory effect on the activation of the lectin pathway of
complement or may cleave IGFBP5. Also plays a role in development.
{ECO:0000250|UniProtKB:P48740, ECO:0000269|PubMed:18424734}.
-!- ACTIVITY REGULATION: Inhibited by SERPING1 and A2M. {ECO:0000250}.
-!- SUBUNIT: Homodimer. Interacts with the oligomeric lectins MBL2,
FCN2 and FCN3; triggers the lectin pathway of complement through
activation of C3. Interacts with SERPING1. Interacts with COLEC11;
probably triggers the lectin pathway of complement.
{ECO:0000250|UniProtKB:P48740}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8133044}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=MASP-1;
IsoId=P98064-1; Sequence=Displayed;
Name=2; Synonyms=MASP-3;
IsoId=P98064-2; Sequence=VSP_036814, VSP_036815;
Note=Contains a N-linked (GlcNAc...) asparagine at position 538
Contains a N-linked (GlcNAc...) asparagine at position 604.
{ECO:0000250|UniProtKB:P48740};
-!- TISSUE SPECIFICITY: Protein of the plasma which is primarily
expressed by liver. {ECO:0000269|PubMed:18424734,
ECO:0000269|PubMed:8133044}.
-!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
aspartate and asparagine is (R) stereospecific within EGF domains.
{ECO:0000250}.
-!- PTM: N-glycosylated. Some N-linked glycan are of the complex-type
(By similarity). {ECO:0000250}.
-!- PTM: Autoproteolytic processing of the proenzyme produces the
active enzyme composed on the heavy and the light chain held
together by a disulfide bond. Isoform 1 but not isoform 2 is
activated through autoproteolytic processing (By similarity).
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice are smaller and more vulnerable
indicating developmental and growth defects. Mice serum has low C4
and C3 cleavage activity together with low MASP2 activation.
{ECO:0000269|PubMed:18424734}.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; D16492; BAA03944.1; -; mRNA.
EMBL; AB049755; BAB69688.1; -; mRNA.
EMBL; AY135527; AAN39850.1; -; Genomic_DNA.
EMBL; AY135525; AAN39850.1; JOINED; Genomic_DNA.
EMBL; AK031598; BAC27469.1; -; mRNA.
EMBL; CH466521; EDK97670.1; -; Genomic_DNA.
EMBL; CH466521; EDK97671.1; -; Genomic_DNA.
EMBL; BC131637; AAI31638.1; -; mRNA.
EMBL; BC131638; AAI31639.1; -; mRNA.
CCDS; CCDS37303.1; -. [P98064-1]
PIR; PC1235; PC1235.
RefSeq; NP_032581.2; NM_008555.2. [P98064-1]
RefSeq; XP_006521891.1; XM_006521828.3.
UniGene; Mm.1213; -.
ProteinModelPortal; P98064; -.
SMR; P98064; -.
STRING; 10090.ENSMUSP00000087327; -.
MEROPS; S01.132; -.
iPTMnet; P98064; -.
PhosphoSitePlus; P98064; -.
MaxQB; P98064; -.
PaxDb; P98064; -.
PeptideAtlas; P98064; -.
PRIDE; P98064; -.
Ensembl; ENSMUST00000089883; ENSMUSP00000087327; ENSMUSG00000022887. [P98064-1]
Ensembl; ENSMUST00000229619; ENSMUSP00000155665; ENSMUSG00000022887. [P98064-2]
GeneID; 17174; -.
KEGG; mmu:17174; -.
UCSC; uc007ytr.1; mouse. [P98064-1]
UCSC; uc007yts.1; mouse. [P98064-2]
CTD; 5648; -.
MGI; MGI:88492; Masp1.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118890; -.
HOGENOM; HOG000237311; -.
HOVERGEN; HBG000559; -.
InParanoid; P98064; -.
KO; K03992; -.
OMA; DLSQRWV; -.
OrthoDB; EOG091G02DS; -.
PhylomeDB; P98064; -.
TreeFam; TF330373; -.
BRENDA; 3.4.21.B7; 3474.
Reactome; R-MMU-166662; Lectin pathway of complement activation.
Reactome; R-MMU-166663; Initial triggering of complement.
Reactome; R-MMU-2855086; Ficolins bind to repetitive carbohydrate structures on the target cell surface.
Reactome; R-MMU-3000480; Scavenging by Class A Receptors.
PRO; PR:P98064; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000022887; Expressed in 18 organ(s), highest expression level in liver.
CleanEx; MM_MASP1; -.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0001867; P:complement activation, lectin pathway; IMP:UniProtKB.
CDD; cd00033; CCP; 2.
CDD; cd00041; CUB; 2.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.60.120.290; -; 2.
InterPro; IPR000859; CUB_dom.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR035914; Sperma_CUB_dom_sf.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00431; CUB; 2.
Pfam; PF00084; Sushi; 2.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00032; CCP; 2.
SMART; SM00042; CUB; 2.
SMART; SM00179; EGF_CA; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF49854; SSF49854; 2.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57535; SSF57535; 1.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS01180; CUB; 2.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS50923; SUSHI; 2.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Alternative splicing; Autocatalytic cleavage; Calcium;
Complement activation lectin pathway; Complete proteome;
Direct protein sequencing; Disulfide bond; EGF-like domain;
Glycoprotein; Hydrolase; Hydroxylation; Immunity; Innate immunity;
Metal-binding; Protease; Reference proteome; Repeat; Secreted;
Serine protease; Signal; Sushi.
SIGNAL 1 24
CHAIN 25 704 Mannan-binding lectin serine protease 1.
/FTId=PRO_0000027595.
CHAIN 25 453 Mannan-binding lectin serine protease 1
heavy chain.
/FTId=PRO_0000027596.
CHAIN 454 704 Mannan-binding lectin serine protease 1
light chain.
/FTId=PRO_0000027597.
DOMAIN 25 143 CUB 1. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 144 187 EGF-like; calcium-binding. {ECO:0000250}.
DOMAIN 190 302 CUB 2. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 304 369 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 370 439 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 454 701 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
REGION 25 305 Interaction with MBL1. {ECO:0000250}.
REGION 25 283 Interaction with FCN2. {ECO:0000250}.
REGION 25 189 Homodimerization. {ECO:0000250}.
REGION 25 189 Interaction with MBL2. {ECO:0000250}.
ACT_SITE 495 495 Charge relay system. {ECO:0000250}.
ACT_SITE 557 557 Charge relay system. {ECO:0000250}.
ACT_SITE 651 651 Charge relay system. {ECO:0000250}.
METAL 73 73 Calcium 1. {ECO:0000250}.
METAL 81 81 Calcium 1. {ECO:0000250}.
METAL 126 126 Calcium 1. {ECO:0000250}.
METAL 128 128 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 144 144 Calcium 2. {ECO:0000250}.
METAL 145 145 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 147 147 Calcium 2. {ECO:0000250}.
METAL 164 164 Calcium 2. {ECO:0000250}.
METAL 165 165 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 168 168 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 240 240 Calcium 3. {ECO:0000250}.
METAL 250 250 Calcium 3. {ECO:0000250}.
METAL 287 287 Calcium 3. {ECO:0000250}.
METAL 289 289 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
SITE 453 454 Cleavage; by autolysis. {ECO:0000250}.
MOD_RES 164 164 (3R)-3-hydroxyasparagine. {ECO:0000255}.
CARBOHYD 54 54 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 183 183 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 390 390 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 412 412 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 78 96 {ECO:0000250}.
DISULFID 148 162 {ECO:0000250}.
DISULFID 158 171 {ECO:0000250}.
DISULFID 173 186 {ECO:0000250}.
DISULFID 190 217 {ECO:0000250}.
DISULFID 247 265 {ECO:0000250}.
DISULFID 306 354 {ECO:0000250}.
DISULFID 334 367 {ECO:0000250}.
DISULFID 372 419 {ECO:0000250}.
DISULFID 402 437 {ECO:0000250}.
DISULFID 441 577 Interchain (between heavy and light
chains). {ECO:0000255|PROSITE-
ProRule:PRU00059, ECO:0000255|PROSITE-
ProRule:PRU00274, ECO:0000255|PROSITE-
ProRule:PRU00302}.
DISULFID 480 496 {ECO:0000250}.
DISULFID 619 636 {ECO:0000250}.
DISULFID 647 677 {ECO:0000250}.
VAR_SEQ 443 443 V -> QPSRALPNLVKRIIGGRNAELGLFPWQALIVVEDTS
RVPNDKWFGSGALLSESWILTAAHVLRSQRRDNTVIPVSKE
HVTVYLGLHDVRDKSGAVNSSAARVILHPDFNIQNYNHDIA
LVQLQKPVPLGAHVMPICLPRPEPEGPAPHMLGLVAGWGIS
NPNVTVDEIILSGTRTLSDVLQYVKLPVVSHAECKASYESR
SGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVIFDEMSQHW
VAQGLVSWGGPEECGSKQVYGVYTKVSNYVDWLWEEMNSPR
AVRDLQVER (in isoform 2).
{ECO:0000303|PubMed:12847554,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_036814.
VAR_SEQ 444 704 Missing (in isoform 2).
{ECO:0000303|PubMed:12847554,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_036815.
CONFLICT 257 257 G -> A (in Ref. 5; AAI31638).
{ECO:0000305}.
CONFLICT 345 345 E -> G (in Ref. 1; BAA03944 and 2;
BAB69688). {ECO:0000305}.
CONFLICT 428 428 E -> K (in Ref. 1; BAA03944).
{ECO:0000305}.
CONFLICT 465 465 M -> T (in Ref. 2; AAN39850).
{ECO:0000305}.
SEQUENCE 704 AA; 79968 MW; 4CF0B17916C10961 CRC64;
MRFLSFWRLL LYHALCLALP EVSAHTVELN EMFGQIQSPG YPDSYPSDSE VTWNITVPEG
FRIKLYFMHF NLESSYLCEY DYVKVETEDQ VLATFCGRET TDTEQTPGQE VVLSPGTFMS
VTFRSDFSNE ERFTGFDAHY MAVDVDECKE REDEELSCDH YCHNYIGGYY CSCRFGYILH
TDNRTCRVEC SGNLFTQRTG TITSPDYPNP YPKSSECSYT IDLEEGFMVS LQFEDIFDIE
DHPEVPCPYD YIKIKAGSKV WGPFCGEKSP EPISTQTHSV QILFRSDNSG ENRGWRLSYR
AAGNECPKLQ PPVYGKIEPS QAVYSFKDQV LVSCDTGYKV LKDNEVMDTF QIECLKDGAW
SNKIPTCKIV DCGAPAGLKH GLVTFSTRNN LTTYKSEIRY SCQQPYYKML HNTTGVYTCS
AHGTWTNEVL KRSLPTCLPV CGVPKFSRKQ ISRIFNGRPA QKGTMPWIAM LSHLNGQPFC
GGSLLGSNWV LTAAHCLHQS LDPEEPTLHS SYLLSPSDFK IIMGKHWRRR SDEDEQHLHV
KRTTLHPLYN PSTFENDLGL VELSESPRLN DFVMPVCLPE QPSTEGTMVI VSGWGKQFLQ
RFPENLMEIE IPIVNSDTCQ EAYTPLKKKV TKDMICAGEK EGGKDACAGD SGGPMVTKDA
ERDQWYLVGV VSWGEDCGKK DRYGVYSYIY PNKDWIQRIT GVRN


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E2234h ELISA Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
E2234h ELISA kit Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
U2234h CLIA Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
U2234r CLIA kit Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus 96T
U2234r CLIA Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus 96T
U2234m CLIA Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus 96T
E2234r ELISA Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus 96T
E2234h Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2
U2234m CLIA kit Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus 96T
E2234m ELISA kit Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus 96T
E2234m ELISA Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus 96T
E2234r ELISA kit Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus 96T
E2234m Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus
E2234r Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus


 

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