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Annexin D1 (AnnAt1) (Annexin A1)

 ANXD1_ARATH             Reviewed;         317 AA.
Q9SYT0; Q39001; Q42023; Q56Y94; Q96527;
06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
22-NOV-2017, entry version 129.
RecName: Full=Annexin D1;
AltName: Full=AnnAt1;
AltName: Full=Annexin A1;
Name=ANN1; Synonyms=ANNAT1, ANX23-ATH, ATOXY5, OXY5;
OrderedLocusNames=At1g35720; ORFNames=F14D7.2;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND TISSUE SPECIFICITY.
TISSUE=Seedling;
PubMed=8855345; DOI=10.1073/pnas.93.20.11268;
Gidrol X., Sabelli P.A., Fern Y.S., Kush A.K.;
"Annexin-like protein from Arabidopsis thaliana rescues delta oxyR
mutant of Escherichia coli from H2O2 stress.";
Proc. Natl. Acad. Sci. U.S.A. 93:11268-11273(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Clark G.B., Roux S.J.;
"Isolation and characterization of two different Arabidopsis annexin
cDNAs.";
(er) Plant Gene Register PGR99-065(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-317.
Schantz R., Schantz M.L., Houlne G.;
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 5-87.
STRAIN=cv. Columbia;
Berthomieu P., Guerrier D., Giraudat J.;
Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 201-317.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[10]
SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=11457958; DOI=10.1104/pp.126.3.1072;
Clark G.B., Sessions A., Eastburn D.J., Roux S.J.;
"Differential expression of members of the annexin multigene family in
Arabidopsis.";
Plant Physiol. 126:1072-1084(2001).
[11]
IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, SUBCELLULAR LOCATION,
AND DISRUPTION PHENOTYPE.
PubMed=15161963; DOI=10.1105/tpc.021683;
Lee S., Lee E.J., Yang E.J., Lee J.E., Park A.R., Song W.H.,
Park O.K.;
"Proteomic identification of annexins, calcium-dependent membrane
binding proteins that mediate osmotic stress and abscisic acid signal
transduction in Arabidopsis.";
Plant Cell 16:1378-1391(2004).
[12]
FUNCTION, MUTAGENESIS OF HIS-40, BIOPHYSICOCHEMICAL PROPERTIES, AND
SUBUNIT.
PubMed=16153598; DOI=10.1016/j.bbrc.2005.08.181;
Gorecka K.M., Konopka-Postupolska D., Hennig J., Buchet R., Pikula S.;
"Peroxidase activity of annexin 1 from Arabidopsis thaliana.";
Biochem. Biophys. Res. Commun. 336:868-875(2005).
[13]
FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=15368128; DOI=10.1007/s00425-004-1374-7;
Clark G.B., Lee D., Dauwalder M., Roux S.J.;
"Immunolocalization and histochemical evidence for the association of
two different Arabidopsis annexins with secretion during early
seedling growth and development.";
Planta 220:621-631(2005).
[14]
INDUCTION, AND GENE FAMILY.
PubMed=16531057; DOI=10.1016/j.plaphy.2006.02.002;
Cantero A., Barthakur S., Bushart T.J., Chou S., Morgan R.O.,
Fernandez M.P., Clark G.B., Roux S.J.;
"Expression profiling of the Arabidopsis annexin gene family during
germination, de-etiolation and abiotic stress.";
Plant Physiol. Biochem. 44:13-24(2006).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=17272265; DOI=10.1074/mcp.M600408-MCP200;
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
"Multidimensional protein identification technology (MudPIT) analysis
of ubiquitinated proteins in plants.";
Mol. Cell. Proteomics 6:601-610(2007).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[18]
IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION AT SER-102;
THR-112; SER-155; TYR-156; TYR-284 AND SER-289.
PubMed=26452715; DOI=10.1016/j.febslet.2015.09.025;
Kim D., Ntui V.O., Zhang N., Xiong L.;
"Arabidopsis Yak1 protein (AtYak1) is a dual specificity protein
kinase.";
FEBS Lett. 589:3321-3327(2015).
[19]
X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 2-317.
Center for eukaryotic structural genomics (CESG);
"X-ray structure of gene product of annexin from Arabidopsis thaliana
gene At1g35720.";
Submitted (FEB-2005) to the PDB data bank.
-!- FUNCTION: Has a peroxidase activity. May act in counteracting
oxidative stress. May also mediate regulated, targeted secretion
of Golgi-derived vesicles during seedling development.
{ECO:0000269|PubMed:15368128, ECO:0000269|PubMed:16153598}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Active at pH 7.0 and 9.0, but not at pH 5.5.
{ECO:0000269|PubMed:16153598};
-!- SUBUNIT: Monomer and homodimer. {ECO:0000269|PubMed:16153598}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Membrane.
Note=translocate from cytosol to membrane upon salt treatment;
this translocation is calcium dependent.
-!- TISSUE SPECIFICITY: Ubiquitous. Most abundant in stems.
{ECO:0000269|PubMed:15368128, ECO:0000269|PubMed:8855345}.
-!- DEVELOPMENTAL STAGE: Expressed in the elongation zone of the root
and in the root cap in germinating seedlings. Expressed later in
the internal cells of the root and in the epidermal cells and the
vascular tissue of the hypocotyl. By day 7, expressed in the
initiating trichomes on leaf primordia and in the vasculature of
hypocotyl and cotyledon. At the transition to reproductive growth
(day 14), expressed in the vasculature, epidermis, basal mesophyll
cells and pith meristem of leaves. {ECO:0000269|PubMed:11457958,
ECO:0000269|PubMed:15368128}.
-!- INDUCTION: Up-regulated by cold, dehydration, salt, osmotic and
oxidative stresses. Up-regulated by abscisic acid (ABA) and
salicylic acid (SA). {ECO:0000269|PubMed:15161963,
ECO:0000269|PubMed:16531057, ECO:0000269|PubMed:8855345}.
-!- DOMAIN: A pair of annexin repeats may form one binding site for
calcium and phospholipid.
-!- PTM: Phosphorylated.
-!- DISRUPTION PHENOTYPE: Plants are hypersensitive to osmotic stress
and abscisic acid (ABA) during germination and early seedling
growth. {ECO:0000269|PubMed:15161963}.
-!- MISCELLANEOUS: Binds lipids at millimolar calcium concentration.
-!- SIMILARITY: Belongs to the annexin (TC 1.A.31.1) family.
{ECO:0000305}.
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EMBL; U28415; AAC49472.1; -; mRNA.
EMBL; AF083913; AAD34236.1; -; mRNA.
EMBL; AC021198; AAF79882.1; -; Genomic_DNA.
EMBL; CP002684; AEE31825.1; -; Genomic_DNA.
EMBL; BT003359; AAO29977.1; -; mRNA.
EMBL; AF332435; AAG48798.1; -; mRNA.
EMBL; AY086570; AAM63633.1; -; mRNA.
EMBL; AY072347; AAL61954.1; -; mRNA.
EMBL; X99224; CAA67608.1; -; mRNA.
EMBL; Z18518; CAA79214.1; -; mRNA.
EMBL; AK221429; BAD94442.1; -; mRNA.
PIR; C86479; C86479.
RefSeq; NP_174810.1; NM_103274.4.
UniGene; At.25241; -.
UniGene; At.50678; -.
PDB; 1YCN; X-ray; 2.51 A; A/B=2-317.
PDB; 2Q4C; X-ray; 2.51 A; A/B=2-317.
PDBsum; 1YCN; -.
PDBsum; 2Q4C; -.
ProteinModelPortal; Q9SYT0; -.
SMR; Q9SYT0; -.
BioGrid; 25708; 24.
DIP; DIP-61421N; -.
IntAct; Q9SYT0; 3.
STRING; 3702.AT1G35720.1; -.
iPTMnet; Q9SYT0; -.
PaxDb; Q9SYT0; -.
PRIDE; Q9SYT0; -.
DNASU; 840476; -.
EnsemblPlants; AT1G35720.1; AT1G35720.1; AT1G35720.
GeneID; 840476; -.
Gramene; AT1G35720.1; AT1G35720.1; AT1G35720.
KEGG; ath:AT1G35720; -.
Araport; AT1G35720; -.
TAIR; locus:2011344; AT1G35720.
eggNOG; KOG0819; Eukaryota.
eggNOG; ENOG410XPUN; LUCA.
HOGENOM; HOG000158802; -.
InParanoid; Q9SYT0; -.
KO; K17098; -.
OMA; GTRHKTL; -.
OrthoDB; EOG09360FWC; -.
PhylomeDB; Q9SYT0; -.
BioCyc; ARA:AT1G35720-MONOMER; -.
Reactome; R-ATH-114608; Platelet degranulation.
Reactome; R-ATH-6798695; Neutrophil degranulation.
EvolutionaryTrace; Q9SYT0; -.
PRO; PR:Q9SYT0; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9SYT0; baseline and differential.
Genevisible; Q9SYT0; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0005618; C:cell wall; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0009579; C:thylakoid; IDA:TAIR.
GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IDA:TAIR.
GO; GO:0005509; F:calcium ion binding; ISS:TAIR.
GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
GO; GO:0005507; F:copper ion binding; IDA:TAIR.
GO; GO:0004601; F:peroxidase activity; IDA:TAIR.
GO; GO:0042803; F:protein homodimerization activity; IDA:TAIR.
GO; GO:0008270; F:zinc ion binding; IDA:TAIR.
GO; GO:0070588; P:calcium ion transmembrane transport; IDA:TAIR.
GO; GO:0071435; P:potassium ion export; IDA:TAIR.
GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0009409; P:response to cold; IEP:TAIR.
GO; GO:0009408; P:response to heat; IEP:TAIR.
GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
GO; GO:0009651; P:response to salt stress; IEP:TAIR.
GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
Gene3D; 1.10.220.10; -; 4.
InterPro; IPR001464; Annexin.
InterPro; IPR018502; Annexin_repeat.
InterPro; IPR018252; Annexin_repeat_CS.
InterPro; IPR037104; Annexin_sf.
InterPro; IPR009118; AnnexinD_plant.
Pfam; PF00191; Annexin; 4.
PRINTS; PR00196; ANNEXIN.
PRINTS; PR01814; ANNEXINPLANT.
SMART; SM00335; ANX; 4.
PROSITE; PS00223; ANNEXIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Annexin; Calcium;
Calcium/phospholipid-binding; Complete proteome; Cytoplasm; Membrane;
Phosphoprotein; Reference proteome; Repeat; Stress response.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 317 Annexin D1.
/FTId=PRO_0000278815.
REPEAT 15 80 Annexin 1.
REPEAT 87 152 Annexin 2.
REPEAT 170 236 Annexin 3.
REPEAT 246 311 Annexin 4.
COMPBIAS 224 227 Poly-Asp.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 102 102 Phosphoserine.
{ECO:0000269|PubMed:26452715}.
MOD_RES 112 112 Phosphothreonine.
{ECO:0000269|PubMed:26452715}.
MOD_RES 155 155 Phosphoserine.
{ECO:0000269|PubMed:26452715}.
MOD_RES 156 156 Phosphotyrosine.
{ECO:0000269|PubMed:26452715}.
MOD_RES 284 284 Phosphotyrosine.
{ECO:0000269|PubMed:26452715}.
MOD_RES 289 289 Phosphoserine.
{ECO:0000269|PubMed:26452715}.
MUTAGEN 40 40 H->A: Loss of peroxidase activity.
{ECO:0000269|PubMed:16153598}.
CONFLICT 59 59 E -> K (in Ref. 1; AAC49472).
{ECO:0000305}.
CONFLICT 196 196 R -> I (in Ref. 7; CAA67608).
{ECO:0000305}.
CONFLICT 229 232 FLAL -> LPCT (in Ref. 1; AAC49472).
{ECO:0000305}.
CONFLICT 293 294 EK -> R (in Ref. 7; CAA67608).
{ECO:0000305}.
CONFLICT 300 301 TR -> NC (in Ref. 7; CAA67608).
{ECO:0000305}.
CONFLICT 305 305 E -> G (in Ref. 7; CAA67608).
{ECO:0000305}.
CONFLICT 311 312 LL -> IF (in Ref. 7; CAA67608).
{ECO:0000305}.
HELIX 13 24 {ECO:0000244|PDB:2Q4C}.
HELIX 32 38 {ECO:0000244|PDB:2Q4C}.
HELIX 43 57 {ECO:0000244|PDB:2Q4C}.
TURN 61 65 {ECO:0000244|PDB:2Q4C}.
HELIX 72 81 {ECO:0000244|PDB:2Q4C}.
HELIX 84 89 {ECO:0000244|PDB:2Q4C}.
HELIX 91 97 {ECO:0000244|PDB:2Q4C}.
HELIX 105 111 {ECO:0000244|PDB:2Q4C}.
HELIX 115 122 {ECO:0000244|PDB:2Q4C}.
TURN 123 129 {ECO:0000244|PDB:2Q4C}.
HELIX 133 140 {ECO:0000244|PDB:2Q4C}.
HELIX 143 153 {ECO:0000244|PDB:2Q4C}.
HELIX 165 181 {ECO:0000244|PDB:2Q4C}.
HELIX 187 195 {ECO:0000244|PDB:2Q4C}.
HELIX 198 210 {ECO:0000244|PDB:2Q4C}.
STRAND 211 214 {ECO:0000244|PDB:2Q4C}.
HELIX 216 219 {ECO:0000244|PDB:2Q4C}.
TURN 220 222 {ECO:0000244|PDB:2Q4C}.
HELIX 228 238 {ECO:0000244|PDB:2Q4C}.
TURN 239 241 {ECO:0000244|PDB:2Q4C}.
HELIX 244 256 {ECO:0000244|PDB:2Q4C}.
HELIX 264 273 {ECO:0000244|PDB:2Q4C}.
TURN 274 276 {ECO:0000244|PDB:2Q4C}.
HELIX 277 288 {ECO:0000244|PDB:2Q4C}.
HELIX 292 296 {ECO:0000244|PDB:2Q4C}.
STRAND 297 299 {ECO:0000244|PDB:1YCN}.
HELIX 303 310 {ECO:0000244|PDB:2Q4C}.
SEQUENCE 317 AA; 36204 MW; 92516D630325005F CRC64;
MATLKVSDSV PAPSDDAEQL RTAFEGWGTN EDLIISILAH RSAEQRKVIR QAYHETYGED
LLKTLDKELS NDFERAILLW TLEPGERDAL LANEATKRWT SSNQVLMEVA CTRTSTQLLH
ARQAYHARYK KSLEEDVAHH TTGDFRKLLV SLVTSYRYEG DEVNMTLAKQ EAKLVHEKIK
DKHYNDEDVI RILSTRSKAQ INATFNRYQD DHGEEILKSL EEGDDDDKFL ALLRSTIQCL
TRPELYFVDV LRSAINKTGT DEGALTRIVT TRAEIDLKVI GEEYQRRNSI PLEKAITKDT
RGDYEKMLVA LLGEDDA


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E1731b ELISA kit 35-beta calcimedin,Annexin A4,Annexin IV,Annexin-4,ANX4,ANXA4,Bos taurus,Bovine,Carbohydrate-binding protein p33_p41,Chromobindin-4,Endonexin I,Lipocortin IV,P32.5,PAP-II,Placental anticoag 96T
U1731b CLIA 35-beta calcimedin,Annexin A4,Annexin IV,Annexin-4,ANX4,ANXA4,Bos taurus,Bovine,Carbohydrate-binding protein p33_p41,Chromobindin-4,Endonexin I,Lipocortin IV,P32.5,PAP-II,Placental anticoagulant 96T
E1731h ELISA 35-beta calcimedin,Annexin A4,Annexin IV,Annexin-4,ANX4,ANXA4,Carbohydrate-binding protein p33_p41,Chromobindin-4,Endonexin I,Homo sapiens,Human,Lipocortin IV,P32.5,PAP-II,Placental anticoagulan 96T
E1731h ELISA kit 35-beta calcimedin,Annexin A4,Annexin IV,Annexin-4,ANX4,ANXA4,Carbohydrate-binding protein p33_p41,Chromobindin-4,Endonexin I,Homo sapiens,Human,Lipocortin IV,P32.5,PAP-II,Placental anticoa 96T
U1731h CLIA 35-beta calcimedin,Annexin A4,Annexin IV,Annexin-4,ANX4,ANXA4,Carbohydrate-binding protein p33_p41,Chromobindin-4,Endonexin I,Homo sapiens,Human,Lipocortin IV,P32.5,PAP-II,Placental anticoagulant 96T
15-288-22296 Annexin A9 - Annexin-31; Annexin XXXI; Pemphaxin Polyclonal 0.05 mg
18-003-42800 Annexin A11 - Annexin XI; Calcyclin-associated annexin 50; CAP-50; 56 kDa autoantigen Polyclonal 0.1 mg Protein A
15-288-22296 Annexin A9 - Annexin-31; Annexin XXXI; Pemphaxin Polyclonal 0.1 mg
25-366 Annexin IV (ANX4) belongs to the annexin family of calcium-dependent phospholipid binding proteins. Although their functions are still not clearly defined, several members of the annexin family have b 0.05 mg
28-552 Annexin A4 (ANXA4) belongs to the annexin family of calcium-dependent phospholipid binding proteins. Although their functions are still not clearly defined, several members of the annexin family have 0.1 mg
E1731p ELISA 35-beta calcimedin,Annexin A4,Annexin IV,Annexin-4,ANX4,ANXA4,Chromobindin-4,Endonexin I,Lipocortin IV,P32.5,PAP-II,Pig,Placental anticoagulant protein II,PP4-X,Protein II,Sus scrofa 96T
U1731p CLIA 35-beta calcimedin,Annexin A4,Annexin IV,Annexin-4,ANX4,ANXA4,Chromobindin-4,Endonexin I,Lipocortin IV,P32.5,PAP-II,Pig,Placental anticoagulant protein II,PP4-X,Protein II,Sus scrofa 96T


 

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