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Myelin-associated glycoprotein (1B236) (Brain neuron cytoplasmic protein 3) (Sialic acid-binding Ig-like lectin 4a) (Siglec-4a)

 MAG_RAT                 Reviewed;         626 AA.
P07722; P02685; P07723;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-APR-1988, sequence version 1.
22-NOV-2017, entry version 151.
RecName: Full=Myelin-associated glycoprotein;
AltName: Full=1B236 {ECO:0000303|PubMed:2438699, ECO:0000303|PubMed:4020419};
AltName: Full=Brain neuron cytoplasmic protein 3;
AltName: Full=Sialic acid-binding Ig-like lectin 4a;
Short=Siglec-4a;
Flags: Precursor;
Name=Mag;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS L-MAG AND S-MAG).
PubMed=2438699; DOI=10.1073/pnas.84.12.4337;
Lai C., Brow M.A., Nave K.-A., Noronha A.B., Quarles R.H., Bloom F.E.,
Milner R.J., Sutcliffe J.G.;
"Two forms of 1B236/myelin-associated glycoprotein, a cell adhesion
molecule for postnatal neural development, are produced by alternative
splicing.";
Proc. Natl. Acad. Sci. U.S.A. 84:4337-4341(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM L-MAG), PARTIAL PROTEIN SEQUENCE,
AND TISSUE SPECIFICITY.
PubMed=2432614; DOI=10.1073/pnas.84.2.600;
Arquint M., Roder J., Chia L.S., Down J., Wilkinson D., Bayley H.,
Braun P., Dunn R.;
"Molecular cloning and primary structure of myelin-associated
glycoprotein.";
Proc. Natl. Acad. Sci. U.S.A. 84:600-604(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM L-MAG).
PubMed=2435742; DOI=10.1083/jcb.104.4.957;
Salzer J.L., Holmes W.P., Colman D.R.;
"The amino acid sequences of the myelin-associated glycoproteins:
homology to the immunoglobulin gene superfamily.";
J. Cell Biol. 104:957-965(1987).
[4]
PROTEIN SEQUENCE OF 76-98; 459-477 AND 492-508, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
Lubec G., Kang S.U., Lubec S.;
Submitted (SEP-2007) to UniProtKB.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 309-626 (ISOFORM L-MAG).
PubMed=6586369;
Sutcliffe J.G., Milner R.J., Bloom F.E.;
"Cellular localization and function of the proteins encoded by brain-
specific mRNAs.";
Cold Spring Harb. Symp. Quant. Biol. 48:477-484(1983).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 309-626 (ISOFORM L-MAG), AND TISSUE
SPECIFICITY.
TISSUE=Brain;
PubMed=4020419;
Bloom F.E., Battenberg E.L.F., Milner R.J., Sutcliffe J.G.;
"Immunocytochemical mapping of 1B236, a brain-specific neuronal
polypeptide deduced from the sequence of a cloned mRNA.";
J. Neurosci. 5:1781-1802(1985).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 309-626 (ISOFORM L-MAG).
PubMed=6347394; DOI=10.1016/0092-8674(83)90010-7;
Sutcliffe J.G., Milner R.J., Shinnick T.M., Bloom F.E.;
"Identifying the protein products of brain-specific genes with
antibodies to chemically synthesized peptides.";
Cell 33:671-682(1983).
[8]
DISULFIDE BONDS, PALMITOYLATION AT CYS-531, AND PARTIAL PROTEIN
SEQUENCE.
PubMed=1703542; DOI=10.1083/jcb.111.6.2651;
Pedraza L., Owens G.C., Green L.A.D., Salzer J.L.;
"The myelin-associated glycoproteins: membrane disposition, evidence
of a novel disulfide linkage between immunoglobulin-like domains, and
posttranslational palmitylation.";
J. Cell Biol. 111:2651-2661(1990).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=8995428; DOI=10.1074/jbc.272.2.1248;
Collins B.E., Yang L.J., Mukhopadhyay G., Filbin M.T., Kiso M.,
Hasegawa A., Schnaar R.L.;
"Sialic acid specificity of myelin-associated glycoprotein binding.";
J. Biol. Chem. 272:1248-1255(1997).
[10]
FUNCTION, MUTAGENESIS OF ARG-118, SUBCELLULAR LOCATION, TOPOLOGY, AND
DOMAIN.
PubMed=9298990; DOI=10.1083/jcb.138.6.1355;
Tang S., Shen Y.J., DeBellard M.E., Mukhopadhyay G., Salzer J.L.,
Crocker P.R., Filbin M.T.;
"Myelin-associated glycoprotein interacts with neurons via a sialic
acid binding site at ARG118 and a distinct neurite inhibition site.";
J. Cell Biol. 138:1355-1366(1997).
[11]
SUBCELLULAR LOCATION, TOPOLOGY, AND PHOSPHORYLATION.
PubMed=16998591; DOI=10.1017/S1740925X04000067;
Marta C.B., Taylor C.M., Cheng S., Quarles R.H., Bansal R.,
Pfeiffer S.E.;
"Myelin associated glycoprotein cross-linking triggers its
partitioning into lipid rafts, specific signaling events and
cytoskeletal rearrangements in oligodendrocytes.";
Neuron Glia Biol. 1:35-46(2004).
[12]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=17640868; DOI=10.1074/jbc.M704055200;
Mehta N.R., Lopez P.H., Vyas A.A., Schnaar R.L.;
"Gangliosides and Nogo receptors independently mediate myelin-
associated glycoprotein inhibition of neurite outgrowth in different
nerve cells.";
J. Biol. Chem. 282:27875-27886(2007).
[13]
FUNCTION.
PubMed=19158290; DOI=10.1523/JNEUROSCI.5204-08.2009;
Nguyen T., Mehta N.R., Conant K., Kim K.J., Jones M., Calabresi P.A.,
Melli G., Hoke A., Schnaar R.L., Ming G.L., Song H., Keswani S.C.,
Griffin J.W.;
"Axonal protective effects of the myelin-associated glycoprotein.";
J. Neurosci. 29:630-637(2009).
[14]
INTERACTION WITH RTN4R AND RTN4RL2, AND DOMAIN.
PubMed=19420245; DOI=10.1523/JNEUROSCI.4935-08.2009;
Robak L.A., Venkatesh K., Lee H., Raiker S.J., Duan Y.,
Lee-Osbourne J., Hofer T., Mage R.G., Rader C., Giger R.J.;
"Molecular basis of the interactions of the Nogo-66 receptor and its
homolog NgR2 with myelin-associated glycoprotein: development of
NgROMNI-Fc, a novel antagonist of CNS myelin inhibition.";
J. Neurosci. 29:5768-5783(2009).
[15]
FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF ARG-118.
PubMed=19367338; DOI=10.1371/journal.pone.0005218;
Woerter V., Schweigreiter R., Kinzel B., Mueller M., Barske C.,
Boeck G., Frentzel S., Bandtlow C.E.;
"Inhibitory activity of myelin-associated glycoprotein on sensory
neurons is largely independent of NgR1 and NgR2 and resides within Ig-
Like domains 4 and 5.";
PLoS ONE 4:E5218-E5218(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545; SER-547 AND
SER-549, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Adhesion molecule that mediates interactions between
myelinating cells and neurons by binding to neuronal sialic acid-
containing gangliosides and to the glycoproteins RTN4R and RTN4RL2
(PubMed:8995428, PubMed:9298990). Not required for initial
myelination, but seems to play a role in the maintenance of normal
axon myelination. Protects motoneurons against apoptosis, also
after injury; protection against apoptosis is probably mediated
via interaction with neuronal RTN4R and RTN4RL2. Required to
prevent degeneration of myelinated axons in adults; this probably
depends on binding to gangliosides on the axon cell membrane (By
similarity). Negative regulator of neurite outgrowth; in dorsal
root ganglion neurons the inhibition is mediated primarily via
binding to neuronal RTN4R or RTN4RL2 and to a lesser degree via
binding to neuronal gangliosides (PubMed:17640868). In cerebellar
granule cells the inhibition is mediated primarily via binding to
neuronal gangliosides (PubMed:17640868). In sensory neurons,
inhibition of neurite extension depends only partially on RTN4R,
RTN4RL2 and gangliosides (PubMed:19367338). Inhibits axon
longitudinal growth (PubMed:9298990). Inhibits axon outgrowth by
binding to RTN4R (By similarity). Preferentially binds to alpha-
2,3-linked sialic acid (PubMed:8995428). Binds ganglioside Gt1b
(PubMed:8995428). {ECO:0000250|UniProtKB:P20917,
ECO:0000269|PubMed:17640868, ECO:0000269|PubMed:19367338,
ECO:0000269|PubMed:8995428, ECO:0000269|PubMed:9298990}.
-!- SUBUNIT: Monomer and homodimer (By similarity). Interacts (via the
first three N-terminal Ig-like domains) with RTN4R and RTN4RL2
(PubMed:19420245). {ECO:0000250|UniProtKB:P20917,
ECO:0000269|PubMed:19420245}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16998591,
ECO:0000269|PubMed:19367338, ECO:0000269|PubMed:8995428,
ECO:0000269|PubMed:9298990}; Single-pass type I membrane protein
{ECO:0000269|PubMed:16998591, ECO:0000269|PubMed:19367338,
ECO:0000269|PubMed:9298990}. Membrane raft
{ECO:0000269|PubMed:16998591}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=L-MAG;
IsoId=P07722-1; Sequence=Displayed;
Name=S-MAG;
IsoId=P07722-2; Sequence=VSP_002529, VSP_002530;
-!- TISSUE SPECIFICITY: Detected in myelin (PubMed:17640868). Detected
in olfactory bulb and throughout the brain (at protein level)
(PubMed:4020419). Detected in brain (PubMed:2432614).
{ECO:0000269|PubMed:2432614, ECO:0000269|PubMed:4020419}.
-!- DOMAIN: The C-terminal cytoplasmic region found only in isoform L-
MAG is required for normal myelination in the central nervous
system (CNS), but is apparently not required for normal
myelination in the peripheral nervous system (PNS).
{ECO:0000250|UniProtKB:P20917}.
-!- DOMAIN: The extracellular domain is required to protect against
axon degeneration (By similarity). The first three Ig-like domains
mediate interaction with RTN4R and RTN4RL2, but are not sufficient
to inhibit neurite outgrowth (PubMed:19420245). The two C-terminal
extracellular Ig-like C2-type domains are required for inhibition
of axon longitudinal growth (PubMed:9298990, PubMed:19420245,
PubMed:19367338). Besides, the two C-terminal extracellular Ig-
like C2-type domains are required for protection against apoptosis
after nerve injury (By similarity). {ECO:0000250|UniProtKB:P20917,
ECO:0000269|PubMed:19367338, ECO:0000269|PubMed:19420245,
ECO:0000269|PubMed:9298990}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P20916}.
-!- PTM: Phosphorylated on tyrosine residues.
{ECO:0000269|PubMed:16998591}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC
(sialic acid binding Ig-like lectin) family. {ECO:0000305}.
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EMBL; M14871; AAA41556.1; -; mRNA.
EMBL; M22357; AAA41558.1; -; mRNA.
EMBL; M16800; AAA41557.1; -; mRNA.
EMBL; X05301; CAA28920.1; -; mRNA.
EMBL; M11721; AAA42082.1; -; mRNA.
EMBL; M36702; AAA40831.1; -; mRNA.
EMBL; V01544; CAA24786.1; -; Genomic_DNA.
PIR; A29028; BNRT3.
RefSeq; NP_058886.1; NM_017190.4. [P07722-1]
RefSeq; XP_006228886.1; XM_006228824.3. [P07722-1]
RefSeq; XP_008757360.1; XM_008759138.2. [P07722-1]
RefSeq; XP_017444540.1; XM_017589051.1. [P07722-1]
RefSeq; XP_017444541.1; XM_017589052.1. [P07722-1]
RefSeq; XP_017444542.1; XM_017589053.1. [P07722-1]
UniGene; Rn.87331; -.
ProteinModelPortal; P07722; -.
SMR; P07722; -.
BioGrid; 248059; 1.
MINT; MINT-237515; -.
STRING; 10116.ENSRNOP00000028544; -.
iPTMnet; P07722; -.
PhosphoSitePlus; P07722; -.
PaxDb; P07722; -.
PRIDE; P07722; -.
Ensembl; ENSRNOT00000028544; ENSRNOP00000028544; ENSRNOG00000021023. [P07722-1]
GeneID; 29409; -.
KEGG; rno:29409; -.
UCSC; RGD:3035; rat. [P07722-1]
CTD; 4099; -.
RGD; 3035; Mag.
eggNOG; ENOG410IUGJ; Eukaryota.
eggNOG; ENOG410XQVV; LUCA.
GeneTree; ENSGT00760000119139; -.
HOGENOM; HOG000113464; -.
HOVERGEN; HBG006317; -.
InParanoid; P07722; -.
KO; K06771; -.
OMA; CQASFPN; -.
OrthoDB; EOG091G03Q5; -.
PhylomeDB; P07722; -.
TreeFam; TF332441; -.
Reactome; R-RNO-193634; Axonal growth inhibition (RHOA activation).
Reactome; R-RNO-210991; Basigin interactions.
PRO; PR:P07722; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000021023; -.
ExpressionAtlas; P07722; baseline and differential.
Genevisible; P07722; RN.
GO; GO:0043218; C:compact myelin; ISO:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0097453; C:mesaxon; IDA:RGD.
GO; GO:0043209; C:myelin sheath; ISO:RGD.
GO; GO:0035749; C:myelin sheath adaxonal region; IDA:RGD.
GO; GO:0033270; C:paranode region of axon; ISO:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0043220; C:Schmidt-Lanterman incisure; IDA:RGD.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:1905576; F:ganglioside GT1b binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0005102; F:receptor binding; IPI:RGD.
GO; GO:0033691; F:sialic acid binding; IDA:UniProtKB.
GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IMP:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
GO; GO:0022010; P:central nervous system myelination; ISO:RGD.
GO; GO:0030517; P:negative regulation of axon extension; IMP:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0045665; P:negative regulation of neuron differentiation; IDA:RGD.
GO; GO:0010977; P:negative regulation of neuron projection development; IDA:RGD.
GO; GO:0007399; P:nervous system development; IEP:RGD.
GO; GO:0048711; P:positive regulation of astrocyte differentiation; IDA:RGD.
GO; GO:0031643; P:positive regulation of myelination; ISO:RGD.
GO; GO:0021762; P:substantia nigra development; ISO:RGD.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR013162; CD80_C2-set.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
Pfam; PF08205; C2-set_2; 1.
SMART; SM00409; IG; 4.
SMART; SM00408; IGc2; 2.
SUPFAM; SSF48726; SSF48726; 4.
PROSITE; PS50835; IG_LIKE; 2.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Lectin; Lipid-binding; Lipoprotein; Membrane;
Palmitate; Phosphoprotein; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 19
CHAIN 20 626 Myelin-associated glycoprotein.
/FTId=PRO_0000014858.
TOPO_DOM 20 516 Extracellular. {ECO:0000255}.
TRANSMEM 517 536 Helical. {ECO:0000255}.
TOPO_DOM 537 626 Cytoplasmic. {ECO:0000255}.
DOMAIN 22 120 Ig-like V-type.
DOMAIN 139 237 Ig-like C2-type 1.
DOMAIN 241 325 Ig-like C2-type 2.
DOMAIN 327 412 Ig-like C2-type 3.
DOMAIN 413 508 Ig-like C2-type 4.
REGION 20 325 Interaction with RTN4R and RTN4RL2.
{ECO:0000269|PubMed:19420245}.
REGION 65 67 Ganglioside GT1b binding.
{ECO:0000250|UniProtKB:P20917}.
REGION 124 128 Ganglioside GT1b binding.
{ECO:0000250|UniProtKB:P20917}.
REGION 577 626 Required for normal axon myelination in
the central nervous system.
{ECO:0000250|UniProtKB:P20917}.
BINDING 118 118 Ganglioside GT1b.
{ECO:0000250|UniProtKB:P20917}.
MOD_RES 545 545 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 547 547 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 549 549 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
LIPID 531 531 S-palmitoyl cysteine.
{ECO:0000269|PubMed:1703542}.
CARBOHYD 99 99 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 223 223 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 246 246 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 315 315 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 332 332 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 406 406 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 450 450 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 454 454 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 37 165 {ECO:0000305|PubMed:1703542}.
DISULFID 42 100 {ECO:0000305|PubMed:1703542}.
DISULFID 159 217 {ECO:0000305|PubMed:1703542}.
DISULFID 261 305 {ECO:0000305|PubMed:1703542}.
DISULFID 347 392 {ECO:0000305|PubMed:1703542}.
DISULFID 421 430 {ECO:0000305|PubMed:1703542}.
DISULFID 432 488 {ECO:0000305|PubMed:1703542}.
VAR_SEQ 574 582 EKRLGSERR -> REVSTRDCH (in isoform S-
MAG). {ECO:0000303|PubMed:2438699}.
/FTId=VSP_002529.
VAR_SEQ 583 626 Missing (in isoform S-MAG).
{ECO:0000303|PubMed:2438699}.
/FTId=VSP_002530.
MUTAGEN 118 118 R->A,D: Abolishes inhibition of neurite
outgrowth from CNS neurons.
{ECO:0000269|PubMed:9298990}.
MUTAGEN 118 118 R->A: No effect on inhibition of neurite
outgrowth from sensory neurons.
{ECO:0000269|PubMed:19367338}.
CONFLICT 309 310 NA -> KS (in Ref. 5, 6 and 7).
{ECO:0000305}.
SEQUENCE 626 AA; 69353 MW; E97998E280ECD635 CRC64;
MIFLTTLPLF WIMISASRGG HWGAWMPSSI SAFEGTCVSI PCRFDFPDEL RPAVVHGVWY
FNSPYPKNYP PVVFKSRTQV VHESFQGRSR LLGDLGLRNC TLLLSTLSPE LGGKYYFRGD
LGGYNQYTFS EHSVLDIINT PNIVVPPEVV AGTEVEVSCM VPDNCPELRP ELSWLGHEGL
GEPTVLGRLR EDEGTWVQVS LLHFVPTREA NGHRLGCQAA FPNTTLQFEG YASLDVKYPP
VIVEMNSSVE AIEGSHVSLL CGADSNPPPL LTWMRDGMVL REAVAESLYL DLEEVTPAED
GIYACLAENA YGQDNRTVEL SVMYAPWKPT VNGTVVAVEG ETVSILCSTQ SNPDPILTIF
KEKQILATVI YESQLQLELP AVTPEDDGEY WCVAENQYGQ RATAFNLSVE FAPIILLESH
CAAARDTVQC LCVVKSNPEP SVAFELPSRN VTVNETEREF VYSERSGLLL TSILTLRGQA
QAPPRVICTS RNLYGTQSLE LPFQGAHRLM WAKIGPVGAV VAFAILIAIV CYITQTRRKK
NVTESPSFSA GDNPHVLYSP EFRISGAPDK YESEKRLGSE RRLLGLRGEP PELDLSYSHS
DLGKRPTKDS YTLTEELAEY AEIRVK


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EIAAB38914 Homo sapiens,Human,Sialic acid-binding Ig-like lectin 1,Sialoadhesin,SIGLEC1,Siglec-1,SN
EIAAB38453 Homo sapiens,Human,Sialic acid-binding Ig-like lectin 14,SIGLEC14,Siglec-14,UNQ294_PRO333
20-783-70272 MOUSE ANTI HUMAN CD33 APC - Sialic acid-binding Ig-like lectin 3; Siglec-3; gp67 Monoclonal 100 TESTS
20-783-70275 MOUSE ANTI HUMAN CD33 - Sialic acid-binding Ig-like lectin 3; Siglec-3; gp67 Monoclonal 0.1 mg
20-783-70271 MOUSE ANTI HUMAN CD33 - Sialic acid-binding Ig-like lectin 3; Siglec-3; gp67 Monoclonal 0.2 mg
20-783-70276 MOUSE ANTI HUMAN CD33 RPE - Sialic acid-binding Ig-like lectin 3; Siglec-3; gp67 Monoclonal 100 TESTS
20-783-73838 MOUSE ANTI HUMAN CD33 Low Endotoxin - Sialic acid-binding Ig-like lectin 3; Siglec-3; gp67 Monoclonal 0.5 mg
EIAAB38913 Mouse,Mus musculus,Sa,SER,Sheep erythrocyte receptor,Sialic acid-binding Ig-like lectin 1,Sialoadhesin,Siglec1,Siglec-1,Sn


 

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