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Glucan 1,3-beta-glucosidase (EC 2.4.1.-) (EC 3.2.1.58) (Exo-1,3-beta-glucanase)

 EXG1_CANAL              Reviewed;         438 AA.
P29717; A0A1D8PCW5; Q5AI63; Q5AIZ3; Q9URL8;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
15-MAR-2017, sequence version 5.
28-MAR-2018, entry version 131.
RecName: Full=Glucan 1,3-beta-glucosidase;
EC=2.4.1.- {ECO:0000269|PubMed:10469155};
EC=3.2.1.58 {ECO:0000269|PubMed:10469155, ECO:0000269|PubMed:20875088, ECO:0000269|PubMed:21713010};
AltName: Full=Exo-1,3-beta-glucanase {ECO:0000303|PubMed:8436950};
Flags: Precursor;
Name=XOG1; Synonyms=EXG, EXG1, XOG;
OrderedLocusNames=CAALFM_C102990CA;
ORFNames=Ca49C10.05, CaO19.10507, CaO19.2990;
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
Candida/Lodderomyces clade; Candida.
NCBI_TaxID=237561;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 39-73.
STRAIN=ATCC 10261 / CBS 2718 / NBRC 1061;
PubMed=8436950; DOI=10.1099/00221287-139-2-325;
Chambers R.S., Broughton M.J., Cannon R.D., Carne A., Emerson G.W.,
Sullivan P.A.;
"An exo-beta-(1,3)-glucanase of Candida albicans: purification of the
enzyme and molecular cloning of the gene.";
J. Gen. Microbiol. 139:325-334(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE CAO19.10507).
STRAIN=1161;
Taylor K., Harris D., Barrell B.G., Rajandream M.A.;
"Candida albicans strain 1161 genome pilot sequencing project.";
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=15123810; DOI=10.1073/pnas.0401648101;
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
Davis R.W., Scherer S.;
"The diploid genome sequence of Candida albicans.";
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
[4]
GENOME REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
Chibana H., Nantel A., Magee P.T.;
"Assembly of the Candida albicans genome into sixteen supercontigs
aligned on the eight chromosomes.";
Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
"Assembly of a phased diploid Candida albicans genome facilitates
allele-specific measurements and provides a simple model for repeat
and indel structure.";
Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
[6]
PROTEIN SEQUENCE OF 39-73, SUBCELLULAR LOCATION, AND SUBUNIT.
STRAIN=3153A;
PubMed=1789004; DOI=10.1002/yea.320070808;
Luna-Arias J.P., Analuz E., Ridruejo J.C., Olivero I., Larriba G.;
"The major exoglucanase from Candida albicans: a non-glycosylated
secretory monomer related to its counterpart from Saccharomyces
cerevisiae.";
Yeast 7:833-841(1991).
[7]
ACTIVE SITE GLU-330.
PubMed=9013549; DOI=10.1074/jbc.272.6.3161;
MacKenzie L.F., Brooke G.S., Cutfield J.F., Sullivan P.A.,
Withers S.G.;
"Identification of Glu-330 as the catalytic nucleophile of Candida
albicans exo-beta-(1,3)-glucanase.";
J. Biol. Chem. 272:3161-3167(1997).
[8]
CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=10469155; DOI=10.1046/j.1432-1327.1999.00581.x;
Stubbs H.J., Brasch D.J., Emerson G.W., Sullivan P.A.;
"Hydrolase and transferase activities of the beta-1,3-exoglucanase of
Candida albicans.";
Eur. J. Biochem. 263:889-895(1999).
[9]
INDUCTION.
PubMed=14731272; DOI=10.1111/j.1365-2958.2003.03879.x;
Lee C.M., Nantel A., Jiang L., Whiteway M., Shen S.H.;
"The serine/threonine protein phosphatase SIT4 modulates yeast-to-
hypha morphogenesis and virulence in Candida albicans.";
Mol. Microbiol. 51:691-709(2004).
[10]
INDUCTION.
PubMed=17030998; DOI=10.1128/EC.00186-06;
Brown V., Sexton J.A., Johnston M.;
"A glucose sensor in Candida albicans.";
Eukaryot. Cell 5:1726-1737(2006).
[11]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=19555771; DOI=10.1016/j.fgb.2009.06.005;
Maddi A., Bowman S.M., Free S.J.;
"Trifluoromethanesulfonic acid-based proteomic analysis of cell wall
and secreted proteins of the ascomycetous fungi Neurospora crassa and
Candida albicans.";
Fungal Genet. Biol. 46:768-781(2009).
[12]
INDUCTION.
PubMed=20402792; DOI=10.1111/j.1567-1364.2010.00626.x;
Li X., Du W., Zhao J., Zhang L., Zhu Z., Jiang L.;
"The MAP kinase-activated protein kinase Rck2p regulates cellular
responses to cell wall stresses, filamentation and virulence in the
human fungal pathogen Candida albicans.";
FEMS Yeast Res. 10:441-451(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=20167299; DOI=10.1016/j.jprot.2010.02.008;
Hernaez M.L., Ximenez-Embun P., Martinez-Gomariz M.,
Gutierrez-Blazquez M.D., Nombela C., Gil C.;
"Identification of Candida albicans exposed surface proteins in vivo
by a rapid proteomic approach.";
J. Proteomics 73:1404-1409(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
PubMed=20392151; DOI=10.3109/13693780903405782;
Kelly J., Kavanagh K.;
"Proteomic analysis of proteins released from growth-arrested Candida
albicans following exposure to caspofungin.";
Med. Mycol. 48:598-605(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=20641015; DOI=10.1002/yea.1775;
Sorgo A.G., Heilmann C.J., Dekker H.L., Brul S., de Koster C.G.,
Klis F.M.;
"Mass spectrometric analysis of the secretome of Candida albicans.";
Yeast 27:661-672(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
INDUCTION.
PubMed=21622905; DOI=10.1128/EC.05011-11;
Sorgo A.G., Heilmann C.J., Dekker H.L., Bekker M., Brul S.,
de Koster C.G., de Koning L.J., Klis F.M.;
"Effects of fluconazole on the secretome, the wall proteome, and wall
integrity of the clinical fungus Candida albicans.";
Eukaryot. Cell 10:1071-1081(2011).
[17]
INTERACTION WITH ANTIMICROBIAL PEPTIDE LL-37, CATALYTIC ACTIVITY,
ENZYME REGULATION, AND FUNCTION.
PubMed=21713010; DOI=10.1371/journal.pone.0021394;
Tsai P.W., Yang C.Y., Chang H.T., Lan C.Y.;
"Characterizing the role of cell-wall beta-1,3-exoglucanase Xog1p in
Candida albicans adhesion by the human antimicrobial peptide LL-37.";
PLoS ONE 6:E21394-E21394(2011).
[18]
FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
PubMed=22876186; DOI=10.1371/journal.ppat.1002848;
Taff H.T., Nett J.E., Zarnowski R., Ross K.M., Sanchez H., Cain M.T.,
Hamaker J., Mitchell A.P., Andes D.R.;
"A Candida biofilm-induced pathway for matrix glucan delivery:
implications for drug resistance.";
PLoS Pathog. 8:E1002848-E1002848(2012).
[19]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=23243062; DOI=10.1128/EC.00278-12;
Heilmann C.J., Sorgo A.G., Mohammadi S., Sosinska G.J.,
de Koster C.G., Brul S., de Koning L.J., Klis F.M.;
"Surface stress induces a conserved cell wall stress response in the
pathogenic fungus Candida albicans.";
Eukaryot. Cell 12:254-264(2013).
[20]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=23136884; DOI=10.1111/mmi.12087;
Rohm M., Lindemann E., Hiller E., Ermert D., Lemuth K., Trkulja D.,
Sogukpinar O., Brunner H., Rupp S., Urban C.F., Sohn K.;
"A family of secreted pathogenesis-related proteins in Candida
albicans.";
Mol. Microbiol. 87:132-151(2013).
[21]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 45-438, DISULFIDE BOND, AND
SUBSTRATE-BINDING.
PubMed=10610795; DOI=10.1006/jmbi.1999.3287;
Cutfield S.M., Davies G.J., Murshudov G., Anderson B.F., Moody P.C.,
Sullivan P.A., Cutfield J.F.;
"The structure of the exo-beta-(1,3)-glucanase from Candida albicans
in native and bound forms: relationship between a pocket and groove in
family 5 glycosyl hydrolases.";
J. Mol. Biol. 294:771-783(1999).
[22]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 39-438 IN COMPLEX WITH
SUBSTRATE, CATALYTIC ACTIVITY, AND MUTAGENESIS OF PHE-182; PHE-267;
PHE-296 AND GLU-330.
PubMed=20875088; DOI=10.1111/j.1742-4658.2010.07869.x;
Patrick W.M., Nakatani Y., Cutfield S.M., Sharpe M.L., Ramsay R.J.,
Cutfield J.F.;
"Carbohydrate binding sites in Candida albicans exo-beta-1,3-glucanase
and the role of the Phe-Phe 'clamp' at the active site entrance.";
FEBS J. 277:4549-4561(2010).
-!- FUNCTION: Major glucan 1,3-beta-glucosidase required for cell wall
integrity. Beta-glucanases participate in the metabolism of beta-
glucan, the main structural component of the cell wall. Can also
function biosynthetically as a transglycosylase. Functions to
deliver glucan from the cell to the extracellular matrix. Does not
appear to impact cell wall glucan content of biofilm cells, nor is
it necessary for filamentation or biofilm formation. Involved in
cell-substrate and cell-cell adhesion. Adhesion to host-cell
surfaces is the first critical step during mucosal infection. XOG1
is target of human antimicrobial peptide LL-37 for inhibition of
cell adhesion. {ECO:0000269|PubMed:21713010,
ECO:0000269|PubMed:22876186}.
-!- CATALYTIC ACTIVITY: Successive hydrolysis of beta-D-glucose units
from the non-reducing ends of (1->3)-beta-D-glucans, releasing
alpha-glucose. {ECO:0000269|PubMed:10469155,
ECO:0000269|PubMed:20875088, ECO:0000269|PubMed:21713010}.
-!- ENZYME REGULATION: Binding of human antimicrobial peptide LL-37
decreases the catalytic activity, which leads to the decrease of
cell adhesion. {ECO:0000269|PubMed:21713010}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=23.0 mM for laminaribiose {ECO:0000269|PubMed:10469155};
KM=12.7 mM for laminaritriose {ECO:0000269|PubMed:10469155};
KM=5.0 mM for laminaritetraose {ECO:0000269|PubMed:10469155};
KM=2.6 mM for laminaripentaose {ECO:0000269|PubMed:10469155};
KM=2.7 mM for laminarihexaose {ECO:0000269|PubMed:10469155};
KM=2.4 mM for laminariheptaose {ECO:0000269|PubMed:10469155};
KM=3.9 mM for laminarin {ECO:0000269|PubMed:10469155};
KM=17.9 mM for pustulan {ECO:0000269|PubMed:10469155};
KM=260 mM for gentiobiose {ECO:0000269|PubMed:10469155};
KM=120 mM for gentiotriose {ECO:0000269|PubMed:10469155};
KM=70 mM for cellobiose {ECO:0000269|PubMed:10469155};
KM=9.4 mM for cellotetraose {ECO:0000269|PubMed:10469155};
KM=12.0 mM for cellohexaose {ECO:0000269|PubMed:10469155};
KM=2.4 mM for p-nitrophenyl-beta-glucoside (pNPG)
{ECO:0000269|PubMed:10469155};
-!- SUBUNIT: Monomer. Interacts with the human antimicrobial peptide
LL-37. {ECO:0000269|PubMed:1789004, ECO:0000269|PubMed:20875088,
ECO:0000269|PubMed:21713010}.
-!- SUBCELLULAR LOCATION: Secreted, cell wall
{ECO:0000269|PubMed:1789004, ECO:0000269|PubMed:19555771,
ECO:0000269|PubMed:20167299, ECO:0000269|PubMed:20641015,
ECO:0000269|PubMed:21622905, ECO:0000269|PubMed:23136884,
ECO:0000269|PubMed:23243062}. Note=Is non-covalently attached to
the cell wall.
-!- INDUCTION: Expression is maximal during the early rapid growth
phase and increases during biofilm growth. Induced by caspofungin.
Transcripts is also regulated by RCK2, SIT4, and HTG4.
{ECO:0000269|PubMed:14731272, ECO:0000269|PubMed:17030998,
ECO:0000269|PubMed:20392151, ECO:0000269|PubMed:20402792,
ECO:0000269|PubMed:21622905, ECO:0000269|PubMed:22876186}.
-!- DISRUPTION PHENOTYPE: Leads to enhanced susceptibility to the
commonly used antifungal, fluconazole, during biofilm growth only.
{ECO:0000269|PubMed:22876186}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A)
family. {ECO:0000305}.
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EMBL; X56556; CAA39908.1; -; Genomic_DNA.
EMBL; AL033497; CAA21969.1; -; Genomic_DNA.
EMBL; CP017623; AOW25980.1; -; Genomic_DNA.
PIR; A47702; A47702.
PIR; T52149; T52149.
RefSeq; XP_721488.2; XM_716395.2.
PDB; 1CZ1; X-ray; 1.85 A; A=45-438.
PDB; 1EQC; X-ray; 1.85 A; A=45-438.
PDB; 1EQP; X-ray; 1.90 A; A=45-438.
PDB; 2PB1; X-ray; 1.90 A; A=39-438.
PDB; 2PBO; X-ray; 1.85 A; A=39-438.
PDB; 2PC8; X-ray; 1.80 A; A=39-438.
PDB; 2PF0; X-ray; 1.90 A; A=39-438.
PDB; 3N9K; X-ray; 1.70 A; A=40-438.
PDB; 3O6A; X-ray; 2.00 A; A=40-438.
PDB; 4M80; X-ray; 1.86 A; A=40-438.
PDB; 4M81; X-ray; 1.86 A; A=40-438.
PDB; 4M82; X-ray; 1.59 A; A=40-438.
PDBsum; 1CZ1; -.
PDBsum; 1EQC; -.
PDBsum; 1EQP; -.
PDBsum; 2PB1; -.
PDBsum; 2PBO; -.
PDBsum; 2PC8; -.
PDBsum; 2PF0; -.
PDBsum; 3N9K; -.
PDBsum; 3O6A; -.
PDBsum; 4M80; -.
PDBsum; 4M81; -.
PDBsum; 4M82; -.
ProteinModelPortal; P29717; -.
SMR; P29717; -.
DrugBank; DB01816; Castanospermine.
CAZy; GH5; Glycoside Hydrolase Family 5.
mycoCLAP; EXG5A_CANAL; -.
PRIDE; P29717; -.
EnsemblFungi; AOW25980; AOW25980; CAALFM_C102990CA.
GeneID; 3636837; -.
KEGG; cal:CAALFM_C102990CA; -.
CGD; CAL0000190583; XOG1.
HOGENOM; HOG000114462; -.
InParanoid; P29717; -.
OMA; EGAPGWD; -.
OrthoDB; EOG092C22A6; -.
BRENDA; 3.2.1.58; 1096.
SABIO-RK; P29717; -.
EvolutionaryTrace; P29717; -.
PMAP-CutDB; P29717; -.
PRO; PR:P29717; -.
Proteomes; UP000000559; Chromosome 1.
GO; GO:0009986; C:cell surface; IDA:CGD.
GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IDA:CGD.
GO; GO:0050839; F:cell adhesion molecule binding; IDA:CGD.
GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IDA:CGD.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0031589; P:cell-substrate adhesion; IDA:CGD.
GO; GO:0006073; P:cellular glucan metabolic process; IMP:CGD.
GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0044407; P:single-species biofilm formation in or on host organism; IMP:CGD.
GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
InterPro; IPR001547; Glyco_hydro_5.
InterPro; IPR018087; Glyco_hydro_5_CS.
InterPro; IPR017853; Glycoside_hydrolase_SF.
Pfam; PF00150; Cellulase; 1.
SUPFAM; SSF51445; SSF51445; 1.
PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
1: Evidence at protein level;
3D-structure; Cell adhesion; Cell wall;
Cell wall biogenesis/degradation; Cleavage on pair of basic residues;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycosidase; Hydrolase; Reference proteome; Secreted; Signal;
Transferase; Virulence; Zymogen.
SIGNAL 1 21 Or 25. {ECO:0000255}.
PROPEP 22 38 {ECO:0000269|PubMed:1789004,
ECO:0000269|PubMed:8436950}.
/FTId=PRO_0000007878.
CHAIN 39 438 Glucan 1,3-beta-glucosidase.
/FTId=PRO_0000007879.
ACT_SITE 230 230 Proton donor.
{ECO:0000250|UniProtKB:O85465}.
ACT_SITE 330 330 Nucleophile.
{ECO:0000269|PubMed:9013549}.
BINDING 65 65 Substrate. {ECO:0000269|PubMed:20875088}.
BINDING 67 67 Substrate. {ECO:0000269|PubMed:20875088}.
BINDING 230 230 Substrate. {ECO:0000269|PubMed:20875088}.
BINDING 293 293 Substrate. {ECO:0000269|PubMed:20875088}.
BINDING 300 300 Substrate. {ECO:0000269|PubMed:20875088}.
DISULFID 313 435 {ECO:0000269|PubMed:10610795}.
DISULFID 338 364 {ECO:0000269|PubMed:10610795}.
MUTAGEN 182 182 F->A: Decreases catalytic activity.
Impairs catalytic activity; when
associated with Ala-296.
{ECO:0000269|PubMed:20875088}.
MUTAGEN 267 267 F->A: Decreases catalytic activity.
Impairs catalytic activity; when
associated with Ala-296 or Ser-330.
{ECO:0000269|PubMed:20875088}.
MUTAGEN 296 296 F->A: Impairs catalytic activity; when
associated with Ala-182.
{ECO:0000269|PubMed:20875088}.
MUTAGEN 296 296 F->W,I: Decreases catalytic activity.
{ECO:0000269|PubMed:20875088}.
MUTAGEN 330 330 E->Q: Impairs catalytic activity.
{ECO:0000269|PubMed:20875088}.
MUTAGEN 330 330 E->S: Impairs catalytic activity; when
associated with Ala-267.
{ECO:0000269|PubMed:20875088}.
CONFLICT 102 102 S -> L (in Ref. 2; CAA21969).
{ECO:0000305}.
CONFLICT 193 193 F -> S (in Ref. 2; CAA21969).
{ECO:0000305}.
TURN 48 50 {ECO:0000244|PDB:4M82}.
STRAND 53 57 {ECO:0000244|PDB:4M82}.
STRAND 61 63 {ECO:0000244|PDB:4M82}.
TURN 66 68 {ECO:0000244|PDB:4M82}.
HELIX 70 72 {ECO:0000244|PDB:4M82}.
HELIX 74 76 {ECO:0000244|PDB:4M82}.
HELIX 89 112 {ECO:0000244|PDB:4M82}.
HELIX 115 123 {ECO:0000244|PDB:4M82}.
STRAND 128 134 {ECO:0000244|PDB:4M82}.
HELIX 135 137 {ECO:0000244|PDB:4M82}.
HELIX 150 163 {ECO:0000244|PDB:4M82}.
STRAND 167 174 {ECO:0000244|PDB:4M82}.
HELIX 183 185 {ECO:0000244|PDB:4M82}.
HELIX 198 213 {ECO:0000244|PDB:4M82}.
HELIX 216 218 {ECO:0000244|PDB:4M82}.
TURN 219 221 {ECO:0000244|PDB:4M82}.
STRAND 222 227 {ECO:0000244|PDB:4M82}.
HELIX 233 235 {ECO:0000244|PDB:4M82}.
HELIX 238 254 {ECO:0000244|PDB:4M82}.
STRAND 261 264 {ECO:0000244|PDB:4M82}.
TURN 270 275 {ECO:0000244|PDB:4M82}.
HELIX 279 281 {ECO:0000244|PDB:4M82}.
STRAND 285 292 {ECO:0000244|PDB:4M82}.
HELIX 298 301 {ECO:0000244|PDB:4M82}.
HELIX 305 321 {ECO:0000244|PDB:4M82}.
STRAND 323 331 {ECO:0000244|PDB:4M82}.
STRAND 335 337 {ECO:0000244|PDB:4M82}.
TURN 340 343 {ECO:0000244|PDB:4M82}.
HELIX 365 367 {ECO:0000244|PDB:4M82}.
HELIX 370 372 {ECO:0000244|PDB:4M82}.
HELIX 375 393 {ECO:0000244|PDB:4M82}.
TURN 394 396 {ECO:0000244|PDB:4M82}.
STRAND 397 401 {ECO:0000244|PDB:4M82}.
HELIX 409 411 {ECO:0000244|PDB:4M82}.
HELIX 413 418 {ECO:0000244|PDB:4M82}.
SEQUENCE 438 AA; 50056 MW; 6FEAEA80C1B0121C CRC64;
MQLSFILTSS VFILLLEFVK ASVISNPFKP NGNLKFKRGG GHNVAWDYDN NVIRGVNLGG
WFVLEPYMTP SLFEPFQNGN DQSGVPVDEY HWTQTLGKEA ASRILQKHWS TWITEQDFKQ
ISNLGLNFVR IPIGYWAFQL LDNDPYVQGQ VQYLEKALGW ARKNNIRVWI DLHGAPGSQN
GFDNSGLRDS YNFQNGDNTQ VTLNVLNTIF KKYGGNEYSD VVIGIELLNE PLGPVLNMDK
LKQFFLDGYN SLRQTGSVTP VIIHDAFQVF GYWNNFLTVA EGQWNVVVDH HHYQVFSGGE
LSRNINDHIS VACNWGWDAK KESHWNVAGE WSAALTDCAK WLNGVNRGAR YEGAYDNAPY
IGSCQPMLDI SQWSDEHKTD TRRYIEAQLD AFEYTGGWVF WSWKTENAPE WSFQTLTYNG
LFPQPVTDRQ FPNQCGFH


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DS-MB-03704 Rat Anti-Mouse beta-Glucan Receptor Antibodies 0.5 mg
DS-MB-03705 Rat Anti-Mouse beta-Glucan Receptor [+RPE] Antibodies 100 TESTS
DS-MB-03696 Rat Anti-Mouse beta-Glucan Receptor Antibodies 0.1 mg
DS-MB-03706 Rat Anti-Mouse beta-Glucan Receptor [+RPE] Antibodies 25 TESTS
DS-MB-03697 Rat Anti-Mouse beta-Glucan Receptor Antibodies 25
DS-MB-03695 Rat Anti-Mouse beta-Glucan Receptor Antibodies 0.25 mg
DS-MB-03699 Rat Anti-Mouse beta-Glucan Receptor [+Biotin] Antibodies 25
DS-MB-03701 Rat Anti-Mouse beta-Glucan Receptor [+FITC] Antibodies 50
DS-MB-03703 Rat Anti-Mouse beta-Glucan Receptor [+FITC] Antibodies 25
DS-MB-03698 Rat Anti-Mouse beta-Glucan Receptor [+Biotin] Antibodies 0.1 mg
DS-MB-03702 Rat Anti-Mouse beta-Glucan Receptor [+FITC] Antibodies 0.5 mg
DS-MB-03700 Rat Anti-Mouse beta-Glucan Receptor [+FITC] Antibodies 0.1 mg
bs-2455R Rabbit Anti-Beta Glucan Receptor Polyclonal Antibody 100ul
bs-2455R-Cy7 Rabbit Anti-Beta Glucan Receptor Polyclonal Antibody, Cy7 Conjugated 100ul
bs-2455R-Cy5 Rabbit Anti-Beta Glucan Receptor Polyclonal Antibody, Cy5 Conjugated 100ul
bs-2455R-Cy3 Rabbit Anti-Beta Glucan Receptor Polyclonal Antibody, Cy3 Conjugated 100ul


 

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