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Chitinase-3-like protein 1 (BRP39 protein) (Breast regression protein 39) (Cartilage glycoprotein 39) (CGP-39) (GP-39)

 CH3L1_MOUSE             Reviewed;         389 AA.
Q61362; B0FEU7; D3Z2P2; Q3U291; Q4FJW9; Q8BKL8; Q99J84;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
14-MAY-2014, sequence version 3.
20-JUN-2018, entry version 150.
RecName: Full=Chitinase-3-like protein 1;
AltName: Full=BRP39 protein;
AltName: Full=Breast regression protein 39;
AltName: Full=Cartilage glycoprotein 39;
Short=CGP-39;
Short=GP-39;
Flags: Precursor;
Name=Chi3l1; Synonyms=Brp39, Chil1;
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).
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=7970700;
Morrison B.W., Leder P.;
"neu and ras initiate murine mammary tumors that share genetic markers
generally absent in c-myc and int-2-initiated tumors.";
Oncogene 9:3417-3426(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, MUTAGENESIS OF
LEU-136, AND CRYSTALLIZATION.
TISSUE=Mammary gland;
PubMed=19041398; DOI=10.1016/j.pep.2008.11.001;
Mohanty A.K., Fisher A.J., Yu Z., Pradeep M.A., Janjanam J.,
Kaushik J.K.;
"Cloning, expression, characterization and crystallization of BRP39, a
signalling glycoprotein expressed during mammary gland apoptosis.";
Protein Expr. Purif. 64:213-218(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Spinal ganglion;
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 MRNA] (ISOFORM 2).
Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E.,
Mollenhauer J., Wiemann S., Schick M., Korn B.;
"Cloning of mouse full open reading frames in Gateway(R) system entry
vector (pDONR201).";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
[7]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=16472595; DOI=10.1053/j.gastro.2005.12.007;
Mizoguchi E.;
"Chitinase 3-like-1 exacerbates intestinal inflammation by enhancing
bacterial adhesion and invasion in colonic epithelial cells.";
Gastroenterology 130:398-411(2006).
[8]
FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
PubMed=19414556; DOI=10.1084/jem.20081271;
Lee C.G., Hartl D., Lee G.R., Koller B., Matsuura H., Da Silva C.A.,
Sohn M.H., Cohn L., Homer R.J., Kozhich A.A., Humbles A., Kearley J.,
Coyle A., Chupp G., Reed J., Flavell R.A., Elias J.A.;
"Role of breast regression protein 39 (BRP-39)/chitinase 3-like-1 in
Th2 and IL-13-induced tissue responses and apoptosis.";
J. Exp. Med. 206:1149-1166(2009).
[9]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
DISRUPTION PHENOTYPE.
PubMed=20558631; DOI=10.1164/rccm.200912-1793OC;
Sohn M.H., Kang M.J., Matsuura H., Bhandari V., Chen N.Y., Lee C.G.,
Elias J.A.;
"The chitinase-like proteins breast regression protein-39 and YKL-40
regulate hyperoxia-induced acute lung injury.";
Am. J. Respir. Crit. Care Med. 182:918-928(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, and Spleen;
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).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND REGION.
PubMed=21546314; DOI=10.1016/j.clim.2011.04.007;
Chen C.C., Llado V., Eurich K., Tran H.T., Mizoguchi E.;
"Carbohydrate-binding motif in chitinase 3-like 1 (CHI3L1/YKL-40)
specifically activates Akt signaling pathway in colonic epithelial
cells.";
Clin. Immunol. 140:268-275(2011).
[12]
FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
PubMed=22817986; DOI=10.1016/j.chom.2012.05.017;
Dela Cruz C.S., Liu W., He C.H., Jacoby A., Gornitzky A., Ma B.,
Flavell R., Lee C.G., Elias J.A.;
"Chitinase 3-like-1 promotes Streptococcus pneumoniae killing and
augments host tolerance to lung antibacterial responses.";
Cell Host Microbe 12:34-46(2012).
[13]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=21866546; DOI=10.1002/ijc.26379;
Libreros S., Garcia-Areas R., Shibata Y., Carrio R.,
Torroella-Kouri M., Iragavarapu-Charyulu V.;
"Induction of proinflammatory mediators by CHI3L1 is reduced by chitin
treatment: decreased tumor metastasis in a breast cancer model.";
Int. J. Cancer 131:377-386(2012).
-!- FUNCTION: Carbohydrate-binding lectin with a preference for
chitin. Has no chitinase activity. May play a role in tissue
remodeling and in the capacity of cells to respond to and cope
with changes in their environment. Plays a role in T-helper cell
type 2 (Th2) inflammatory response and IL-13-induced inflammation,
regulating allergen sensitization, inflammatory cell apoptosis,
dendritic cell accumulation and M2 macrophage differentiation.
Facilitates invasion of pathogenic enteric bacteria into colonic
mucosa and lymphoid organs. Mediates activation of AKT1 signaling
pathway and subsequent IL8 production in colonic epithelial cells.
Regulates antibacterial responses in lung by contributing to
macrophage bacterial killing, controlling bacterial dissemination
and augmenting host tolerance. Also regulates hyperoxia-induced
injury, inflammation and epithelial apoptosis in lung.
{ECO:0000269|PubMed:16472595, ECO:0000269|PubMed:19041398,
ECO:0000269|PubMed:19414556, ECO:0000269|PubMed:20558631,
ECO:0000269|PubMed:21546314, ECO:0000269|PubMed:22817986}.
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space. Cytoplasm.
Endoplasmic reticulum. Note=Detected in bronchoalveolar lavage
(BAL) fluids. Localizes mainly to endoplasmic reticulum when
overexpressed in cells, with some protein also detected throughout
the cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=3;
Name=1;
IsoId=Q61362-1; Sequence=Displayed;
Name=2;
IsoId=Q61362-2; Sequence=VSP_054524;
Note=Produced by alternative initiation at Met-9 of isoform 1.;
Name=3;
IsoId=Q61362-3; Sequence=VSP_054523;
Note=May be produced by alternative splicing of isoform 1. Gene
prediction based on EST data.;
-!- TISSUE SPECIFICITY: Detected in lung in pulmonary macrophages and
alveolar type 2 cells and in bronchoalveolar lavage (BAL) fluids.
Expressed in mammary tumor cells (at protein level). Expressed in
lung. Not detected in non-inflammatory colon.
{ECO:0000269|PubMed:16472595, ECO:0000269|PubMed:19414556,
ECO:0000269|PubMed:20558631, ECO:0000269|PubMed:21866546}.
-!- INDUCTION: Up-regulated in colon under several inflammatory
conditions. Up-regulated upon pulmonary inflammation elicited by
sensitization and challenge with the chitin-free aeroallergen
ovalbumin or with chitin-containing antigen house dust mite (HDM)
extract. Up-regulated in lungs after S.pneumoniae infection. Up-
regulated in splenic cells of mammary tumor-bearing animals. Down-
regulated by hyperoxia in lung. {ECO:0000269|PubMed:16472595,
ECO:0000269|PubMed:19414556, ECO:0000269|PubMed:20558631,
ECO:0000269|PubMed:21866546, ECO:0000269|PubMed:22817986}.
-!- DISRUPTION PHENOTYPE: Mice are viable, fertile and appear normal,
but have defective antigen-induced Th2 inflammatory responses and
defective IL-13-induced responses, displaying accelerated cell
death responses and diminished M2 macrophage differentiation.
Mutant mice are more sensitive to S.pneumoniae infection,
displaying enhanced mortality, exacerbated lung injury and
decreased bacterial clearance compared to wild-type mice. Mutant
mice also have an exacerbated response to hyperoxia, displaying
enhanced protein leak, tissue inflammation and chemokine
production and premature death. {ECO:0000269|PubMed:19414556,
ECO:0000269|PubMed:20558631, ECO:0000269|PubMed:22817986}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family.
{ECO:0000305}.
-!- CAUTION: Although it belongs to the glycosyl hydrolase 18 family,
Leu-149 is present instead of the conserved Glu which is an active
site residue. Therefore this protein lacks chitinase activity.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH03780.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH04734.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH05611.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA63603.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; X93035; CAA63603.1; ALT_INIT; mRNA.
EMBL; EU313768; ABY53363.1; -; mRNA.
EMBL; AK051475; BAC34654.1; -; mRNA.
EMBL; AK155412; BAE33251.1; -; mRNA.
EMBL; CT010283; CAJ18491.1; -; mRNA.
EMBL; AC137104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC003780; AAH03780.1; ALT_INIT; mRNA.
EMBL; BC004734; AAH04734.1; ALT_INIT; mRNA.
EMBL; BC005611; AAH05611.1; ALT_INIT; mRNA.
CCDS; CCDS48368.1; -. [Q61362-1]
PIR; S61551; S61551.
RefSeq; NP_031721.2; NM_007695.3. [Q61362-1]
RefSeq; XP_006529174.1; XM_006529111.3. [Q61362-3]
UniGene; Mm.38274; -.
PDB; 5XEP; X-ray; 2.60 A; A/B/C/D/E/F=9-389.
PDBsum; 5XEP; -.
ProteinModelPortal; Q61362; -.
SMR; Q61362; -.
IntAct; Q61362; 1.
MINT; Q61362; -.
STRING; 10090.ENSMUSP00000080717; -.
CAZy; GH18; Glycoside Hydrolase Family 18.
PhosphoSitePlus; Q61362; -.
PaxDb; Q61362; -.
PeptideAtlas; Q61362; -.
PRIDE; Q61362; -.
Ensembl; ENSMUST00000082060; ENSMUSP00000080717; ENSMUSG00000064246. [Q61362-1]
Ensembl; ENSMUST00000153856; ENSMUSP00000117117; ENSMUSG00000064246. [Q61362-2]
Ensembl; ENSMUST00000156873; ENSMUSP00000119205; ENSMUSG00000064246. [Q61362-3]
GeneID; 12654; -.
KEGG; mmu:12654; -.
UCSC; uc007crg.2; mouse. [Q61362-1]
CTD; 12654; -.
MGI; MGI:1340899; Chil1.
eggNOG; KOG2806; Eukaryota.
eggNOG; COG3325; LUCA.
GeneTree; ENSGT00550000074323; -.
HOGENOM; HOG000111109; -.
HOVERGEN; HBG011684; -.
InParanoid; Q61362; -.
KO; K17523; -.
OMA; SNDHIDT; -.
OrthoDB; EOG091G014W; -.
TreeFam; TF315610; -.
Reactome; R-MMU-6798695; Neutrophil degranulation.
ChiTaRS; Chil1; mouse.
PRO; PR:Q61362; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000064246; -.
CleanEx; MM_CHI3L1; -.
ExpressionAtlas; Q61362; baseline and differential.
Genevisible; Q61362; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IBA:GO_Central.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0008061; F:chitin binding; ISS:UniProtKB.
GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
GO; GO:0072606; P:interleukin-8 secretion; IDA:UniProtKB.
GO; GO:0030324; P:lung development; ISS:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
GO; GO:0070555; P:response to interleukin-1; ISS:UniProtKB.
GO; GO:0070741; P:response to interleukin-6; ISS:UniProtKB.
GO; GO:0009612; P:response to mechanical stimulus; ISS:UniProtKB.
GO; GO:0034612; P:response to tumor necrosis factor; ISS:UniProtKB.
Gene3D; 3.10.50.10; -; 1.
InterPro; IPR028538; CHI3L1.
InterPro; IPR011583; Chitinase_II.
InterPro; IPR029070; Chitinase_insertion_sf.
InterPro; IPR001223; Glyco_hydro18_cat.
InterPro; IPR017853; Glycoside_hydrolase_SF.
PANTHER; PTHR11177:SF202; PTHR11177:SF202; 1.
Pfam; PF00704; Glyco_hydro_18; 1.
SMART; SM00636; Glyco_18; 1.
SUPFAM; SSF51445; SSF51445; 2.
SUPFAM; SSF54556; SSF54556; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; Alternative splicing;
Antimicrobial; Apoptosis; Complete proteome; Cytoplasm;
Disulfide bond; Endoplasmic reticulum; Glycoprotein;
Inflammatory response; Reference proteome; Secreted; Signal.
SIGNAL 1 29 {ECO:0000250}.
CHAIN 30 389 Chitinase-3-like protein 1.
/FTId=PRO_0000011966.
REGION 79 80 Chitooligosaccharide binding.
{ECO:0000250}.
REGION 106 109 Chitooligosaccharide binding.
{ECO:0000250}.
REGION 213 216 Chitooligosaccharide binding.
{ECO:0000250}.
REGION 333 347 Important for AKT1 activation and IL8
production.
BINDING 150 150 Chitooligosaccharide. {ECO:0000250}.
BINDING 361 361 Chitooligosaccharide. {ECO:0000250}.
CARBOHYD 68 68 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
DISULFID 34 59 {ECO:0000250}.
DISULFID 309 372 {ECO:0000250}.
VAR_SEQ 1 16 MHTSTEARMGMRAALT -> MTLQLA (in isoform
3). {ECO:0000305}.
/FTId=VSP_054523.
VAR_SEQ 1 8 Missing (in isoform 2).
{ECO:0000303|PubMed:19041398,
ECO:0000303|Ref.4}.
/FTId=VSP_054524.
MUTAGEN 136 136 L->E: No effect on chiting-binding. No
restoration of chitinase activity.
{ECO:0000269|PubMed:19041398}.
CONFLICT 112 112 E -> G (in Ref. 4; ABY53363).
{ECO:0000305}.
CONFLICT 258 258 A -> V (in Ref. 3; BAE33251).
{ECO:0000305}.
CONFLICT 339 339 D -> H (in Ref. 1; CAA63603).
{ECO:0000305}.
CONFLICT 348 348 G -> R (in Ref. 4; ABY53363).
{ECO:0000305}.
STRAND 31 38 {ECO:0000244|PDB:5XEP}.
HELIX 39 42 {ECO:0000244|PDB:5XEP}.
HELIX 45 47 {ECO:0000244|PDB:5XEP}.
HELIX 51 53 {ECO:0000244|PDB:5XEP}.
STRAND 60 69 {ECO:0000244|PDB:5XEP}.
HELIX 82 90 {ECO:0000244|PDB:5XEP}.
HELIX 91 94 {ECO:0000244|PDB:5XEP}.
STRAND 100 106 {ECO:0000244|PDB:5XEP}.
TURN 108 110 {ECO:0000244|PDB:5XEP}.
HELIX 112 119 {ECO:0000244|PDB:5XEP}.
HELIX 122 139 {ECO:0000244|PDB:5XEP}.
STRAND 143 147 {ECO:0000244|PDB:5XEP}.
HELIX 153 155 {ECO:0000244|PDB:5XEP}.
HELIX 156 173 {ECO:0000244|PDB:5XEP}.
STRAND 182 188 {ECO:0000244|PDB:5XEP}.
HELIX 191 197 {ECO:0000244|PDB:5XEP}.
HELIX 200 204 {ECO:0000244|PDB:5XEP}.
STRAND 208 213 {ECO:0000244|PDB:5XEP}.
HELIX 220 222 {ECO:0000244|PDB:5XEP}.
STRAND 242 245 {ECO:0000244|PDB:5XEP}.
HELIX 246 255 {ECO:0000244|PDB:5XEP}.
HELIX 260 262 {ECO:0000244|PDB:5XEP}.
STRAND 263 279 {ECO:0000244|PDB:5XEP}.
STRAND 286 290 {ECO:0000244|PDB:5XEP}.
TURN 295 297 {ECO:0000244|PDB:5XEP}.
HELIX 305 312 {ECO:0000244|PDB:5XEP}.
STRAND 316 319 {ECO:0000244|PDB:5XEP}.
TURN 321 323 {ECO:0000244|PDB:5XEP}.
STRAND 326 330 {ECO:0000244|PDB:5XEP}.
STRAND 333 336 {ECO:0000244|PDB:5XEP}.
HELIX 340 352 {ECO:0000244|PDB:5XEP}.
STRAND 356 361 {ECO:0000244|PDB:5XEP}.
HELIX 363 365 {ECO:0000244|PDB:5XEP}.
HELIX 379 388 {ECO:0000244|PDB:5XEP}.
SEQUENCE 389 AA; 43893 MW; 9E7D66069B233834 CRC64;
MHTSTEARMG MRAALTGFAV LMLLQSCSAY KLVCYFTSWS QYREGVGSFL PDAIQPFLCT
HIIYSFANIS SDNMLSTWEW NDESNYDKLN KLKTRNTNLK TLLSVGGWKF GEKRFSEIAS
NTERRTAFVR SVAPFLRSYG FDGLDLAWLY PRLRDKQYFS TLIKELNAEF TKEVQPGREK
LLLSAALSAG KVAIDTGYDI AQIAQHLDFI NLMTYDFHGV WRQITGHHSP LFQGQKDTRF
DRYSNVNYAV QYMIRLGAQA SKLLMGIPTF GKSFTLASSE NQLGAPISGE GLPGRFTKEA
GTLAYYEICD FLKGAEVHRL SNEKVPFATK GNQWVGYEDK ESVKNKVGFL KEKKLAGAMV
WALDLDDFQG TCQPKEFFPL TNAIKDALA


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U1463b CLIA 39 kDa whey protein,Bos taurus,Bovine,Cartilage glycoprotein 39,CGP-39,CHI3L1,Chitinase-3-like protein 1,Chitinase-like protein 1,CLP-1,GP-39,Signal-processing protein,SPC-40 96T
E1463b ELISA kit 39 kDa whey protein,Bos taurus,Bovine,Cartilage glycoprotein 39,CGP-39,CHI3L1,Chitinase-3-like protein 1,Chitinase-like protein 1,CLP-1,GP-39,Signal-processing protein,SPC-40 96T
U1463h CLIA 39 kDa synovial protein,Cartilage glycoprotein 39,CGP-39,CHI3L1,Chitinase-3-like protein 1,GP-39,hCGP-39,Homo sapiens,Human,YKL-40 96T
E1463h ELISA 39 kDa synovial protein,Cartilage glycoprotein 39,CGP-39,CHI3L1,Chitinase-3-like protein 1,GP-39,hCGP-39,Homo sapiens,Human,YKL-40 96T
E1463h ELISA kit 39 kDa synovial protein,Cartilage glycoprotein 39,CGP-39,CHI3L1,Chitinase-3-like protein 1,GP-39,hCGP-39,Homo sapiens,Human,YKL-40 96T
U1463r CLIA Cartilage glycoprotein 39,CGP-39,Chi3l1,Chitinase-3-like protein 1,GP-39,Rat,Rattus norvegicus 96T
E1463r ELISA Cartilage glycoprotein 39,CGP-39,Chi3l1,Chitinase-3-like protein 1,GP-39,Rat,Rattus norvegicus 96T
E1463r ELISA kit Cartilage glycoprotein 39,CGP-39,Chi3l1,Chitinase-3-like protein 1,GP-39,Rat,Rattus norvegicus 96T
E1463p ELISA 38 kDa heparin-binding glycoprotein,CHI3L1,Chitinase-3-like protein 1,gp38k,Pig,Signal-processing protein,Sus scrofa 96T
E1463p ELISA kit 38 kDa heparin-binding glycoprotein,CHI3L1,Chitinase-3-like protein 1,gp38k,Pig,Signal-processing protein,Sus scrofa 96T
U1463p CLIA 38 kDa heparin-binding glycoprotein,CHI3L1,Chitinase-3-like protein 1,gp38k,Pig,Signal-processing protein,Sus scrofa 96T
CHIA CHI3L1 Gene chitinase 3-like 1 (cartilage glycoprotein-39)
EIAAB07164 CHID1,Chitinase domain-containing protein 1,GL008,Homo sapiens,Human,PSEC0104,SB139,SI-CLP,Stabilin-1-interacting chitinase-like protein
E1386099 Sheep Chitinase 3-Like 1 (Cartilage Glycoprotein-39) (CHI3L1) ELISA Kit 1
18-783-77701 SHEEP ANTI HUMAN ALPHA 1 ACID GLYCOPROTEIN HRP - Cartilage glycoprotein 39; GP-39; 39 kDa synovial protein; HCgp-39; YKL-40 Polyclonal 1 ml
18-783-77700 SHEEP ANTI HUMAN ALPHA 1 ACID GLYCOPROTEIN Alk. Phos. - Cartilage glycoprotein 39; GP-39; 39 kDa synovial protein; HCgp-39; YKL-40 Polyclonal 1 ml
CSB-EL005346RA Rat chitinase 3-like 1 (cartilage glycoprotein-39) (CHI3L1) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL005346PI Pig chitinase 3-like 1 (cartilage glycoprotein-39) (CHI3L1) ELISA kit, Species Pig, Sample Type serum, plasma 96T
EIAAB09398 32 kDa epididymal protein,Acidic epididymal glycoprotein,Aeg,Crisp1,Cysteine-rich secretory protein 1,Protein D,Protein E,Protein IV,Rat,Rattus norvegicus,SCP,Sialoprotein,Sperm-coating glycoprotein
EIAAB45178 Mouse,Mus musculus,Ucma,Unique cartilage matrix-associated protein,Upper zone of growth plate and cartilage matrix associated protein
CSB-EL005346GO Goat chitinase 3-like 1 (cartilage glycoprotein-39) (CHI3L1) ELISA kit, Species Goat, Sample Type serum, plasma 96T


 

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