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Annexin A2 (Annexin II) (Annexin-2) (Calpactin I heavy chain) (Calpactin-1 heavy chain) (Chromobindin-8) (Lipocortin II) (Placental anticoagulant protein IV) (PAP-IV) (Protein I) (p36)

 ANXA2_MOUSE             Reviewed;         339 AA.
P07356;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 186.
RecName: Full=Annexin A2;
AltName: Full=Annexin II;
AltName: Full=Annexin-2;
AltName: Full=Calpactin I heavy chain;
AltName: Full=Calpactin-1 heavy chain;
AltName: Full=Chromobindin-8;
AltName: Full=Lipocortin II;
AltName: Full=Placental anticoagulant protein IV;
Short=PAP-IV;
AltName: Full=Protein I;
AltName: Full=p36;
Name=Anxa2; Synonyms=Anx2, Cal1h;
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].
PubMed=3013423; DOI=10.1016/0092-8674(86)90737-3;
Saris C.J.M., Tack B.F., Kristensen T., Glenney J.R. Jr., Hunter T.;
"The cDNA sequence for the protein-tyrosine kinase substrate p36
(calpactin I heavy chain) reveals a multidomain protein with internal
repeats.";
Cell 46:201-212(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16 AND 322-339.
PubMed=2138915; DOI=10.1021/bi00457a019;
Amiguet P., D'Eustachio P., Kristensen T., Wetsel R.A., Saris C.J.M.,
Hunter T., Chaplin D.D., Tack B.F.;
"Structure and chromosome assignment of the murine p36 (calpactin I
heavy chain) gene.";
Biochemistry 29:1226-1232(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
PubMed=8634333; DOI=10.1016/0167-4781(95)00238-3;
Fey M.F., Moffat G.J., Vik D.P., Meisenhelder J., Saris C.J.,
Hunter T., Tack B.F.;
"Complete structure of the murine p36 (annexin II) gene.
Identification of mRNAs for both the murine and the human gene with
alternatively spliced 5' noncoding exons.";
Biochim. Biophys. Acta 1306:160-170(1996).
[5]
INTERACTION WITH DYSF.
PubMed=14506282; DOI=10.1074/jbc.M307247200;
Lennon N.J., Kho A., Bacskai B.J., Perlmutter S.L., Hyman B.T.,
Brown R.H. Jr.;
"Dysferlin interacts with annexins A1 and A2 and mediates sarcolemmal
wound-healing.";
J. Biol. Chem. 278:50466-50473(2003).
[6]
ISGYLATION.
PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
"Proteomic identification of proteins conjugated to ISG15 in mouse and
human cells.";
Biochem. Biophys. Res. Commun. 336:496-506(2005).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-199, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[9]
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).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22848640; DOI=10.1371/journal.pone.0041865;
Seidah N.G., Poirier S., Denis M., Parker R., Miao B., Mapelli C.,
Prat A., Wassef H., Davignon J., Hajjar K.A., Mayer G.;
"Annexin A2 is a natural extrahepatic inhibitor of the PCSK9-induced
LDL receptor degradation.";
PLoS ONE 7:E41865-E41865(2012).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-49; LYS-152 AND LYS-227, 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).
-!- FUNCTION: Calcium-regulated membrane-binding protein whose
affinity for calcium is greatly enhanced by anionic phospholipids.
It binds two calcium ions with high affinity. May be involved in
heat-stress response (By similarity). Inhibits PCSK9-enhanced LDLR
degradation, probably reduces PCSK9 protein levels via a
translational mechanism but also competes with LDLR for binding
with PCSK9 (PubMed:22848640). {ECO:0000250|UniProtKB:P07355,
ECO:0000269|PubMed:22848640}.
-!- SUBUNIT: Heterotetramer containing 2 light chains of S100A10/p11
and 2 heavy chains of ANXA2/p36 (By similarity). Interacts with
ATP1B1 (By similarity). Interacts with DYSF (PubMed:14506282).
Interacts with COCH. Interacts (via repeat Annexin 1) with PCSK9
(via the C-terminal domain); the interaction inhibits the
degradation of LDLR. Interacts with CEACAM1 (via the cytoplasmic
domain); this interaction is regulated by phosphorylation of
CEACAM1 (By similarity). {ECO:0000250|UniProtKB:A2SW69,
ECO:0000250|UniProtKB:P07355, ECO:0000250|UniProtKB:Q6TEQ7,
ECO:0000269|PubMed:14506282}.
-!- INTERACTION:
P08207:S100a10; NbExp=2; IntAct=EBI-738510, EBI-643986;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix, basement membrane. Melanosome {ECO:0000250}. Note=In the
lamina beneath the plasma membrane.
-!- DOMAIN: A pair of annexin repeats may form one binding site for
calcium and phospholipid.
-!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
-!- DISRUPTION PHENOTYPE: Animals show a 40% increase of LDL-
cholesterol levels in plasma. {ECO:0000269|PubMed:22848640}.
-!- MISCELLANEOUS: It may cross-link plasma membrane phospholipids
with actin and the cytoskeleton and be involved with exocytosis.
-!- SIMILARITY: Belongs to the annexin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Red velvet - Issue 86
of September 2007;
URL="https://web.expasy.org/spotlight/back_issues/086";
-----------------------------------------------------------------------
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EMBL; M14044; AAA37360.1; -; mRNA.
EMBL; BC003327; AAH03327.1; -; mRNA.
EMBL; BC005763; AAH05763.1; -; mRNA.
EMBL; M33321; AAA37361.1; -; Genomic_DNA.
EMBL; M33322; AAA37362.1; -; Genomic_DNA.
EMBL; D10024; BAA00914.1; -; mRNA.
EMBL; S82177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS23316.1; -.
PIR; A23943; LUMS36.
RefSeq; NP_031611.1; NM_007585.3.
RefSeq; XP_006510859.1; XM_006510796.2.
UniGene; Mm.238343; -.
PDB; 4HRE; X-ray; 2.79 A; A/B/C/D=1-339.
PDBsum; 4HRE; -.
ProteinModelPortal; P07356; -.
SMR; P07356; -.
BioGrid; 198448; 21.
CORUM; P07356; -.
IntAct; P07356; 17.
MINT; MINT-274998; -.
STRING; 10090.ENSMUSP00000034756; -.
TCDB; 9.A.48.1.1; the unconventional protein secretion (ups) system.
iPTMnet; P07356; -.
PhosphoSitePlus; P07356; -.
SwissPalm; P07356; -.
REPRODUCTION-2DPAGE; IPI00468203; -.
REPRODUCTION-2DPAGE; P07356; -.
SWISS-2DPAGE; P07356; -.
EPD; P07356; -.
PaxDb; P07356; -.
PeptideAtlas; P07356; -.
PRIDE; P07356; -.
Ensembl; ENSMUST00000034756; ENSMUSP00000034756; ENSMUSG00000032231.
GeneID; 12306; -.
KEGG; mmu:12306; -.
UCSC; uc009qng.1; mouse.
CTD; 302; -.
MGI; MGI:88246; Anxa2.
eggNOG; KOG0819; Eukaryota.
eggNOG; ENOG410XPUN; LUCA.
GeneTree; ENSGT00760000118972; -.
HOGENOM; HOG000158803; -.
HOVERGEN; HBG061815; -.
InParanoid; P07356; -.
KO; K17092; -.
OMA; FIQQDTK; -.
OrthoDB; EOG091G0H6H; -.
PhylomeDB; P07356; -.
TreeFam; TF105452; -.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-75205; Dissolution of Fibrin Clot.
ChiTaRS; Anxa2; mouse.
PRO; PR:P07356; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032231; -.
CleanEx; MM_ANXA2; -.
ExpressionAtlas; P07356; baseline and differential.
Genevisible; P07356; MM.
GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
GO; GO:0016323; C:basolateral plasma membrane; IDA:BHF-UCL.
GO; GO:0005938; C:cell cortex; IEA:Ensembl.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005913; C:cell-cell adherens junction; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005769; C:early endosome; IDA:MGI.
GO; GO:0005768; C:endosome; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0031012; C:extracellular matrix; ISO:MGI.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:MGI.
GO; GO:0031902; C:late endosome membrane; ISO:MGI.
GO; GO:0005811; C:lipid droplet; ISO:MGI.
GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
GO; GO:0044354; C:macropinosome; IEA:Ensembl.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0030496; C:midbody; ISO:MGI.
GO; GO:0035749; C:myelin sheath adaxonal region; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:1990667; C:PCSK9-AnxA2 complex; ISS:BHF-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0001726; C:ruffle; IEA:Ensembl.
GO; GO:0042383; C:sarcolemma; IDA:MGI.
GO; GO:0043220; C:Schmidt-Lanterman incisure; IDA:BHF-UCL.
GO; GO:0031982; C:vesicle; ISO:MGI.
GO; GO:0044730; F:bone sialoprotein binding; IEA:Ensembl.
GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; ISO:MGI.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005544; F:calcium-dependent phospholipid binding; ISO:MGI.
GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
GO; GO:0019834; F:phospholipase A2 inhibitor activity; ISO:MGI.
GO; GO:0002020; F:protease binding; ISO:MGI.
GO; GO:0017137; F:Rab GTPase binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0044548; F:S100 protein binding; ISO:MGI.
GO; GO:0001525; P:angiogenesis; IMP:MGI.
GO; GO:0007589; P:body fluid secretion; IEA:Ensembl.
GO; GO:0052362; P:catabolism by host of symbiont protein; ISO:MGI.
GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
GO; GO:0042730; P:fibrinolysis; IMP:MGI.
GO; GO:0001765; P:membrane raft assembly; ISO:MGI.
GO; GO:0006936; P:muscle contraction; TAS:Reactome.
GO; GO:0052405; P:negative regulation by host of symbiont molecular function; ISO:MGI.
GO; GO:0044147; P:negative regulation of development of symbiont involved in interaction with host; ISO:MGI.
GO; GO:0032804; P:negative regulation of low-density lipoprotein particle receptor catabolic process; IMP:BHF-UCL.
GO; GO:0036035; P:osteoclast development; ISO:MGI.
GO; GO:0051099; P:positive regulation of binding; IMP:MGI.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:1905581; P:positive regulation of low-density lipoprotein particle clearance; IMP:BHF-UCL.
GO; GO:1905597; P:positive regulation of low-density lipoprotein particle receptor binding; IMP:BHF-UCL.
GO; GO:1905599; P:positive regulation of low-density lipoprotein receptor activity; IMP:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:0001921; P:positive regulation of receptor recycling; IMP:BHF-UCL.
GO; GO:1905602; P:positive regulation of receptor-mediated endocytosis involved in cholesterol transport; IMP:BHF-UCL.
GO; GO:0044090; P:positive regulation of vacuole organization; ISO:MGI.
GO; GO:0031340; P:positive regulation of vesicle fusion; ISO:MGI.
GO; GO:0051290; P:protein heterotetramerization; ISO:MGI.
GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
GO; GO:0097066; P:response to thyroid hormone; IEA:Ensembl.
GO; GO:0006900; P:vesicle budding from membrane; ISO:MGI.
Gene3D; 1.10.220.10; -; 4.
InterPro; IPR001464; Annexin.
InterPro; IPR018502; Annexin_repeat.
InterPro; IPR018252; Annexin_repeat_CS.
InterPro; IPR037104; Annexin_sf.
InterPro; IPR002389; ANX2.
PANTHER; PTHR10502:SF18; PTHR10502:SF18; 1.
Pfam; PF00191; Annexin; 4.
PRINTS; PR00196; ANNEXIN.
PRINTS; PR00198; ANNEXINII.
SMART; SM00335; ANX; 4.
PROSITE; PS00223; ANNEXIN; 4.
1: Evidence at protein level;
3D-structure; Acetylation; Annexin; Basement membrane; Calcium;
Calcium/phospholipid-binding; Complete proteome; Extracellular matrix;
Isopeptide bond; Phosphoprotein; Reference proteome; Repeat; Secreted;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P04272}.
CHAIN 2 339 Annexin A2.
/FTId=PRO_0000067471.
REPEAT 42 102 Annexin 1.
REPEAT 114 174 Annexin 2.
REPEAT 199 259 Annexin 3.
REPEAT 274 334 Annexin 4.
REGION 2 24 S100A10-binding site. {ECO:0000255}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P04272}.
MOD_RES 24 24 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:P07355}.
MOD_RES 26 26 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:P07355}.
MOD_RES 49 49 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 152 152 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 184 184 Phosphoserine.
{ECO:0000250|UniProtKB:P07355}.
MOD_RES 199 199 Phosphotyrosine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 227 227 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
CROSSLNK 49 49 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P07355}.
CROSSLNK 49 49 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P07355}.
HELIX 4 8 {ECO:0000244|PDB:4HRE}.
HELIX 35 46 {ECO:0000244|PDB:4HRE}.
HELIX 53 61 {ECO:0000244|PDB:4HRE}.
HELIX 65 79 {ECO:0000244|PDB:4HRE}.
HELIX 83 90 {ECO:0000244|PDB:4HRE}.
HELIX 93 103 {ECO:0000244|PDB:4HRE}.
HELIX 106 118 {ECO:0000244|PDB:4HRE}.
HELIX 125 134 {ECO:0000244|PDB:4HRE}.
HELIX 137 151 {ECO:0000244|PDB:4HRE}.
HELIX 155 162 {ECO:0000244|PDB:4HRE}.
HELIX 165 175 {ECO:0000244|PDB:4HRE}.
HELIX 188 201 {ECO:0000244|PDB:4HRE}.
STRAND 204 207 {ECO:0000244|PDB:4HRE}.
HELIX 210 219 {ECO:0000244|PDB:4HRE}.
HELIX 222 235 {ECO:0000244|PDB:4HRE}.
HELIX 240 247 {ECO:0000244|PDB:4HRE}.
HELIX 251 264 {ECO:0000244|PDB:4HRE}.
HELIX 266 278 {ECO:0000244|PDB:4HRE}.
STRAND 279 282 {ECO:0000244|PDB:4HRE}.
HELIX 285 294 {ECO:0000244|PDB:4HRE}.
TURN 296 299 {ECO:0000244|PDB:4HRE}.
HELIX 300 311 {ECO:0000244|PDB:4HRE}.
HELIX 315 322 {ECO:0000244|PDB:4HRE}.
HELIX 325 335 {ECO:0000244|PDB:4HRE}.
SEQUENCE 339 AA; 38676 MW; 4407E572097FB2C0 CRC64;
MSTVHEILCK LSLEGDHSTP PSAYGSVKPY TNFDAERDAL NIETAVKTKG VDEVTIVNIL
TNRSNVQRQD IAFAYQRRTK KELPSALKSA LSGHLETVIL GLLKTPAQYD ASELKASMKG
LGTDEDSLIE IICSRTNQEL QEINRVYKEM YKTDLEKDII SDTSGDFRKL MVALAKGRRA
EDGSVIDYEL IDQDARELYD AGVKRKGTDV PKWISIMTER SVCHLQKVFE RYKSYSPYDM
LESIKKEVKG DLENAFLNLV QCIQNKPLYF ADRLYDSMKG KGTRDKVLIR IMVSRSEVDM
LKIRSEFKRK YGKSLYYYIQ QDTKGDYQKA LLYLCGGDD


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E1944p ELISA kit Annexin A2,Annexin II,Annexin-2,ANX2,ANXA2,Calpactin I heavy chain,Calpactin-1 heavy chain,Chromobindin-8,Lipocortin II,p36,PAP-IV,Pig,Placental anticoagulant protein IV,Protein I,Sus scrof 96T
E1944r ELISA kit Annexin A2,Annexin II,Annexin-2,Anx2,Anxa2,Calpactin I heavy chain,Calpactin-1 heavy chain,Chromobindin-8,Lipocortin II,p36,PAP-IV,Placental anticoagulant protein IV,Protein I,Rat,Rattus no 96T
E1944h ELISA Annexin A2,Annexin II,Annexin-2,ANX2,ANX2L4,ANXA2,CAL1H,Calpactin I heavy chain,Calpactin-1 heavy chain,Chromobindin-8,Homo sapiens,Human,Lipocortin II,LPC2D,p36,PAP-IV,Placental anticoagulant p 96T
U1944h CLIA Annexin A2,Annexin II,Annexin-2,ANX2,ANX2L4,ANXA2,CAL1H,Calpactin I heavy chain,Calpactin-1 heavy chain,Chromobindin-8,Homo sapiens,Human,Lipocortin II,LPC2D,p36,PAP-IV,Placental anticoagulant pr 96T
E1944c ELISA Annexin A2,Annexin II,Annexin-2,ANX2,ANXA2,Calpactin I heavy chain,Calpactin-1 heavy chain,Chicken,Chromobindin-8,Gallus gallus,Lipocortin II,p36,PAP-IV,Placental anticoagulant protein IV,Protei 96T
U1944c CLIA kit Annexin A2,Annexin II,Annexin-2,ANX2,ANXA2,Calpactin I heavy chain,Calpactin-1 heavy chain,Chicken,Chromobindin-8,Gallus gallus,Lipocortin II,p36,PAP-IV,Placental anticoagulant protein IV,Pr 96T
E1944c ELISA kit Annexin A2,Annexin II,Annexin-2,ANX2,ANXA2,Calpactin I heavy chain,Calpactin-1 heavy chain,Chicken,Chromobindin-8,Gallus gallus,Lipocortin II,p36,PAP-IV,Placental anticoagulant protein IV,P 96T
U1944c CLIA Annexin A2,Annexin II,Annexin-2,ANX2,ANXA2,Calpactin I heavy chain,Calpactin-1 heavy chain,Chicken,Chromobindin-8,Gallus gallus,Lipocortin II,p36,PAP-IV,Placental anticoagulant protein IV,Protein 96T
E1944h ELISA kit Annexin A2,Annexin II,Annexin-2,ANX2,ANX2L4,ANXA2,CAL1H,Calpactin I heavy chain,Calpactin-1 heavy chain,Chromobindin-8,Homo sapiens,Human,Lipocortin II,LPC2D,p36,PAP-IV,Placental anticoagul 96T
U1944h CLIA kit Annexin A2,Annexin II,Annexin-2,ANX2,ANX2L4,ANXA2,CAL1H,Calpactin I heavy chain,Calpactin-1 heavy chain,Chromobindin-8,Homo sapiens,Human,Lipocortin II,LPC2D,p36,PAP-IV,Placental anticoagula 96T
18-272-196776 Annexin II - Rabbit polyclonal to Annexin II; Annexin-2; Annexin II; Lipocortin II; Calpactin I heavy chain; Chromobindin-8; p36; Protein I; Placental anticoagulant protein IV; PAP-IV Polyclonal 0.1 mg


 

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