Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Chitinase-3-like protein 1 (BP40) (Mammary gland protein 40) (MGP-40)

 CH3L1_CAPHI             Reviewed;         383 AA.
Q8SPQ0;
23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
10-MAY-2017, entry version 87.
RecName: Full=Chitinase-3-like protein 1;
AltName: Full=BP40;
AltName: Full=Mammary gland protein 40;
Short=MGP-40;
Flags: Precursor;
Name=CHI3L1;
Capra hircus (Goat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Capra.
NCBI_TaxID=9925;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, AND X-RAY
CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 22-383 IN COMPLEX WITH CHITIN
OLIGOMERS.
TISSUE=Mammary gland;
PubMed=12529329; DOI=10.1074/jbc.M208967200;
Mohanty A.K., Singh G., Paramasivam M., Saravanan K., Jabeen T.,
Sharma S., Yadav S., Kaur P., Kumar P., Srinivasan A., Singh T.P.;
"Crystal structure of a novel regulatory 40-kDa mammary gland protein
(MGP-40) secreted during involution.";
J. Biol. Chem. 278:14451-14460(2003).
[2]
X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 22-381 IN COMPLEXES WITH
OLIGOSACCHARIDES, GLYCOSYLATION AT ASN-60, AND DISULFIDE BONDS.
PubMed=17372347; DOI=10.1107/S0907444907001631;
Kumar J., Ethayathulla A.S., Srivastava D.B., Singh N., Sharma S.,
Kaur P., Srinivasan A., Singh T.P.;
"Carbohydrate-binding properties of goat secretory glycoprotein (SPG-
40) and its functional implications: structures of the native
glycoprotein and its four complexes with chitin-like
oligosaccharides.";
Acta Crystallogr. D 63:437-446(2007).
-!- 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 (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12529329}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space. Cytoplasm
{ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.
Endoplasmic reticulum {ECO:0000250}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family.
{ECO:0000305}.
-!- CAUTION: Although it belongs to the glycosyl hydrolase 18 family,
Leu-140 is present instead of the conserved Glu which is an active
site residue. Therefore this protein lacks chitinase activity.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY081150; AAL87007.1; -; mRNA.
RefSeq; NP_001272618.1; NM_001285689.1.
UniGene; Chi.18273; -.
PDB; 1LJY; X-ray; 2.90 A; A=22-383.
PDB; 1SYT; X-ray; 2.60 A; A=22-381.
PDB; 1ZBV; X-ray; 3.21 A; A=22-381.
PDB; 1ZBW; X-ray; 2.80 A; A=22-381.
PDB; 1ZU8; X-ray; 3.05 A; A=22-383.
PDB; 2AOS; X-ray; 2.90 A; A=22-381.
PDB; 2B31; X-ray; 3.10 A; A=22-381.
PDB; 2DSZ; X-ray; 2.35 A; A=22-381.
PDB; 2DT0; X-ray; 2.45 A; A=22-381.
PDB; 2DT1; X-ray; 2.09 A; A=22-381.
PDB; 2DT2; X-ray; 2.90 A; A=22-381.
PDB; 2DT3; X-ray; 2.28 A; A=22-381.
PDB; 2O92; X-ray; 3.00 A; A=22-381.
PDB; 2OLH; X-ray; 2.78 A; A=22-381.
PDBsum; 1LJY; -.
PDBsum; 1SYT; -.
PDBsum; 1ZBV; -.
PDBsum; 1ZBW; -.
PDBsum; 1ZU8; -.
PDBsum; 2AOS; -.
PDBsum; 2B31; -.
PDBsum; 2DSZ; -.
PDBsum; 2DT0; -.
PDBsum; 2DT1; -.
PDBsum; 2DT2; -.
PDBsum; 2DT3; -.
PDBsum; 2O92; -.
PDBsum; 2OLH; -.
ProteinModelPortal; Q8SPQ0; -.
SMR; Q8SPQ0; -.
CAZy; GH18; Glycoside Hydrolase Family 18.
GeneID; 100860825; -.
KEGG; chx:100860825; -.
CTD; 1116; -.
HOVERGEN; HBG011684; -.
KO; K17523; -.
OrthoDB; EOG091G014W; -.
EvolutionaryTrace; Q8SPQ0; -.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0008061; F:chitin binding; ISS:UniProtKB.
GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; ISS: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; ISS: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; ISS:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS: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.
InterPro; IPR028538; CHI3L1.
InterPro; IPR011583; Chitinase_II.
InterPro; IPR029070; Chitinase_insertion.
InterPro; IPR001223; Glyco_hydro18_cat.
InterPro; IPR017853; Glycoside_hydrolase_SF.
PANTHER; PTHR11177:SF249; PTHR11177:SF249; 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; Antimicrobial; Apoptosis; Cytoplasm;
Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
Glycoprotein; Inflammatory response; Lectin; Secreted; Signal.
SIGNAL 1 21 {ECO:0000269|PubMed:12529329}.
CHAIN 22 383 Chitinase-3-like protein 1.
/FTId=PRO_0000011964.
REGION 70 71 Chitooligosaccharide binding.
REGION 97 100 Chitooligosaccharide binding.
REGION 204 207 Chitooligosaccharide binding.
REGION 324 338 Important for AKT1 activation and IL8
production. {ECO:0000250}.
BINDING 141 141 Chitooligosaccharide.
BINDING 263 263 Chitooligosaccharide.
BINDING 352 352 Chitooligosaccharide.
CARBOHYD 60 60 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17372347}.
CARBOHYD 367 367 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 26 51 {ECO:0000269|PubMed:17372347}.
DISULFID 300 364 {ECO:0000269|PubMed:17372347}.
STRAND 23 29 {ECO:0000244|PDB:2DT1}.
HELIX 30 34 {ECO:0000244|PDB:2DT1}.
HELIX 37 39 {ECO:0000244|PDB:2DT1}.
HELIX 43 45 {ECO:0000244|PDB:2DT1}.
TURN 48 50 {ECO:0000244|PDB:2DT1}.
STRAND 52 62 {ECO:0000244|PDB:2DT1}.
STRAND 65 67 {ECO:0000244|PDB:2DT1}.
HELIX 73 81 {ECO:0000244|PDB:2DT1}.
HELIX 82 85 {ECO:0000244|PDB:2DT1}.
STRAND 91 97 {ECO:0000244|PDB:2DT1}.
STRAND 99 101 {ECO:0000244|PDB:2DT3}.
HELIX 103 111 {ECO:0000244|PDB:2DT1}.
HELIX 113 130 {ECO:0000244|PDB:2DT1}.
STRAND 133 138 {ECO:0000244|PDB:2DT1}.
TURN 144 146 {ECO:0000244|PDB:2DT1}.
HELIX 147 164 {ECO:0000244|PDB:2DT1}.
HELIX 165 167 {ECO:0000244|PDB:2DT1}.
STRAND 173 178 {ECO:0000244|PDB:2DT1}.
HELIX 182 188 {ECO:0000244|PDB:2DT1}.
HELIX 191 195 {ECO:0000244|PDB:2DT1}.
STRAND 199 203 {ECO:0000244|PDB:2DT1}.
STRAND 213 215 {ECO:0000244|PDB:2DT1}.
STRAND 229 231 {ECO:0000244|PDB:2OLH}.
STRAND 234 236 {ECO:0000244|PDB:1LJY}.
HELIX 237 247 {ECO:0000244|PDB:2DT1}.
HELIX 251 253 {ECO:0000244|PDB:2DT1}.
STRAND 254 270 {ECO:0000244|PDB:2DT1}.
STRAND 277 281 {ECO:0000244|PDB:2DT1}.
TURN 286 288 {ECO:0000244|PDB:2DT1}.
STRAND 293 295 {ECO:0000244|PDB:2DT1}.
HELIX 296 302 {ECO:0000244|PDB:2DT1}.
TURN 303 305 {ECO:0000244|PDB:2DT1}.
STRAND 307 311 {ECO:0000244|PDB:2DT1}.
TURN 312 315 {ECO:0000244|PDB:2DT1}.
STRAND 316 321 {ECO:0000244|PDB:2DT1}.
STRAND 324 327 {ECO:0000244|PDB:2DT1}.
HELIX 331 343 {ECO:0000244|PDB:2DT1}.
STRAND 347 352 {ECO:0000244|PDB:2DT1}.
HELIX 354 356 {ECO:0000244|PDB:2DT1}.
STRAND 359 361 {ECO:0000244|PDB:2DT1}.
STRAND 363 367 {ECO:0000244|PDB:2DT1}.
HELIX 371 381 {ECO:0000244|PDB:2DT1}.
SEQUENCE 383 AA; 42894 MW; 17655ED4BE4E9F5F CRC64;
MGLRASGTGF VVLVLLQSCA AYKLICYYTS WSQYREGDGS CFPDAIDPFL CTHIIYSFAN
ISNNEIDTWE WNDVTLYDTL NTLKNRNPKL KTLLSVGGWN FGPERFSKIA SKTQSRRTFI
KSVPPFLRTH GFDGLDLAWL YPGRRDKRHL TGLVKEMKAE FAREAQAGTE RLLLSAAVSA
GKIAIDRGYD IAQISRHLDF ISLLTYDFHG AWRQTVGHHS PLFRGQEDAS SDRFSNADYA
VSYMLRLGAP ANKLVMGIPT FGRSFTLASS KTDVGAPISG PGIPGRFTKE KGILAYYEIC
DFLHGATTHR FRDQQVPYAT KGNQWVAYDD QESVKNKARY LKNRQLAGAM VWALDLDDFR
GTFCGQNLTF PLTSAVKDVL AEV


Related products :

Catalog number Product name Quantity
MT-414-10 Mouse Mammary Gland Total protein Mammary Gland, pregnant_E10   0.5mg
MT-414-12 Mouse Mammary Gland Total protein Mammary Gland, pregnant_E12 0.5mg
MT-414-11 Mouse Mammary Gland Total protein Mammary Gland, pregnant_E11  0.5mg
MT-414-13 Mouse Mammary Gland Total protein Mammary Gland, pregnant_E13 0.5mg
MT-414 Mouse Mammary Gland Total protein Mammary Gland, non pregnant 0.5mg
MT-414-14 Mouse Mammary Gland Total protein Mammary Gland, pregnant_E14 0.5mg
MT-414-15 Mouse Mammary Gland Total protein Mammary Gland, pregnant_E15 0.5mg
MT-414-17 Mouse Mammary Gland Total protein Mammary Gland, pregnant_E17  0.5mg
MT-414-18 Mouse Mammary Gland Total protein Mammary Gland, pregnant_E18  0.5mg
MT-414-L1 Mouse Mammary Gland Total protein Mammary Gland, Day 1 of Lactation  0.5mg
MT-414-L3 Mouse Mammary Gland Total protein Mammary Gland, Day 3 of Lactation  0.5mg
MT-414-N7 Mouse Mammary Gland Total protein Mammary Gland, Day 7 of involution  0.5mg
MT-414-16 Mouse Mammary Gland Total protein Mammary Gland, pregnant_E16  0.5mg
MT-414-N1 Mouse Mammary Gland Total protein Mammary Gland, Day 1 of involution  0.5mg
MT-414-L7 Mouse Mammary Gland Total protein Mammary Gland, Day 7 of Lactation  0.5mg
RT-414-13 Rat Mammary Gland Total protein Mammary Gland, pregnant_E13 0.5mg
RT-414-N7 Rat Mammary Gland Total protein Mammary Gland, Day 7 of involution  0.5mg
RT-414-L3 Rat Mammary Gland Total protein Mammary Gland, Day 3 of Lactation  0.5mg
RT-414-15 Rat Mammary Gland Total protein Mammary Gland, pregnant_E15 0.5mg
RT-414-N1 Rat Mammary Gland Total protein Mammary Gland, Day 1 of involution  0.5mg
RT-414-L7 Rat Mammary Gland Total protein Mammary Gland, Day 7 of Lactation  0.5mg
RT-414-17 Rat Mammary Gland Total protein Mammary Gland, pregnant_E17  0.5mg
RT-414-18 Rat Mammary Gland Total protein Mammary Gland, pregnant_E18  0.5mg
RT-414-20 Rat Mammary Gland Total protein Mammary Gland, pregnant_E20  0.5mg
RT-414-16 Rat Mammary Gland Total protein Mammary Gland, pregnant_E16  0.5mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur