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

Salivary cystatin-L (Sialostatin-L) (SialoL)

 CYTL_IXOSC              Reviewed;         133 AA.
Q8MVB6;
13-APR-2016, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
12-APR-2017, entry version 59.
RecName: Full=Salivary cystatin-L {ECO:0000305};
AltName: Full=Sialostatin-L {ECO:0000303|PubMed:16772304, ECO:0000303|PubMed:20545851, ECO:0000303|PubMed:26078269};
Short=SialoL {ECO:0000303|PubMed:19494265};
Flags: Precursor;
Ixodes scapularis (Black-legged tick) (Deer tick).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
Acari; Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
NCBI_TaxID=6945 {ECO:0000312|EMBL:AAM93646.1};
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Rhode Island {ECO:0000312|EMBL:AAM93646.1};
TISSUE=Salivary gland {ECO:0000312|EMBL:AAM93646.1};
PubMed=12177149;
Valenzuela J.G., Francischetti I.M., Pham V.M., Garfield M.K.,
Mather T.N., Ribeiro J.M.;
"Exploring the sialome of the tick Ixodes scapularis.";
J. Exp. Biol. 205:2843-2864(2002).
[2]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16772304; DOI=10.1074/jbc.M513010200;
Kotsyfakis M., Sa-Nunes A., Francischetti I.M., Mather T.N.,
Andersen J.F., Ribeiro J.M.;
"Antiinflammatory and immunosuppressive activity of sialostatin L, a
salivary cystatin from the tick Ixodes scapularis.";
J. Biol. Chem. 281:26298-26307(2006).
[3]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=17698852; DOI=10.1074/jbc.M703143200;
Kotsyfakis M., Karim S., Andersen J.F., Mather T.N., Ribeiro J.M.;
"Selective cysteine protease inhibition contributes to blood-feeding
success of the tick Ixodes scapularis.";
J. Biol. Chem. 282:29256-29263(2007).
[4]
FUNCTION.
PubMed=19494265; DOI=10.4049/jimmunol.0900075;
Sa-Nunes A., Bafica A., Antonelli L.R., Choi E.Y., Francischetti I.M.,
Andersen J.F., Shi G.P., Chavakis T., Ribeiro J.M., Kotsyfakis M.;
"The immunomodulatory action of sialostatin L on dendritic cells
reveals its potential to interfere with autoimmunity.";
J. Immunol. 182:7422-7429(2009).
[5]
FUNCTION.
PubMed=26078269; DOI=10.4049/jimmunol.1401823;
Klein M., Bruehl T.J., Staudt V., Reuter S., Grebe N., Gerlitzki B.,
Hoffmann M., Bohn T., Ulges A., Stergiou N., de Graaf J., Loewer M.,
Taube C., Becker M., Hain T., Dietzen S., Stassen M., Huber M.,
Lohoff M., Campos Chagas A., Andersen J., Kotal J., Langhansova H.,
Kopecky J., Schild H., Kotsyfakis M., Schmitt E., Bopp T.;
"Tick salivary sialostatin L represses the initiation of immune
responses by targeting IRF4-dependent transcription in murine mast
cells.";
J. Immunol. 195:621-631(2015).
[6]
FUNCTION.
PubMed=25975355; DOI=10.1186/s13071-015-0887-1;
Lieskovska J., Palenikova J., Langhansova H., Campos Chagas A.,
Calvo E., Kotsyfakis M., Kopecky J.;
"Tick sialostatins L and L2 differentially influence dendritic cell
responses to Borrelia spirochetes.";
Parasit. Vectors 8:275-275(2015).
[7] {ECO:0000244|PDB:4ZM8}
X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS) OF 20-133, FUNCTION, SUBUNIT,
AND DISULFIDE BONDS.
PubMed=20545851; DOI=10.1111/j.1365-2958.2010.07220.x;
Kotsyfakis M., Horka H., Salat J., Andersen J.F.;
"The crystal structures of two salivary cystatins from the tick Ixodes
scapularis and the effect of these inhibitors on the establishment of
Borrelia burgdorferi infection in a murine model.";
Mol. Microbiol. 77:456-470(2010).
-!- FUNCTION: Inhibitor of cysteine proteinases. Inhibits host immune
responses via its inhibition of host cathepsins (PubMed:19494265).
Contributes to the suppression of the host's immune response to
tick salivary proteins and is important for successful feeding on
hosts (PubMed:17698852). Inhibits differentiation of host
dendritic cells (PubMed:19494265, PubMed:25975355). Inhibits
proliferation of host T-cells in response to antigen stimulus
(PubMed:19494265). Down-regulates TLR2-mediated host responses to
infection by B.burgdorferi and the production of the chemokine
CCL3 by host dendritic cells (PubMed:25975355). Down-regulates
host responses to infection by B.burgdorferi and the production of
IFNB1 by host dendritic cells (PubMed:25975355). Down-regulates
IL1B production by host mast cells, and this then leads to
impaired activation of IL1R1, resulting in decreased IL9
production (PubMed:26078269). Inhibits host inflammatory reactions
and recruitment of host neutrophils (PubMed:16772304). Inhibits
papain and cathepsin-L (CTSL) (in vitro) (PubMed:16772304,
PubMed:17698852, PubMed:20545851). Inhibits cathepsin-S (CTSS) (in
vitro) (PubMed:17698852, PubMed:20545851). Inhibits CTSV and CTSC,
but to a lesser degree (in vitro) (PubMed:16772304,
PubMed:17698852). {ECO:0000269|PubMed:16772304,
ECO:0000269|PubMed:17698852, ECO:0000269|PubMed:19494265,
ECO:0000269|PubMed:20545851, ECO:0000269|PubMed:25975355,
ECO:0000269|PubMed:26078269}.
-!- SUBUNIT: Monomer. Can form homodimers in vitro, but probably not
in vivo. Homodimers are predicted to be inactive; dimerization
disrupts the interaction with target proteases.
{ECO:0000269|PubMed:20545851}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16772304}.
-!- TISSUE SPECIFICITY: Detected in saliva (at protein level)
(PubMed:16772304). Detected in salivary gland and midgut
(PubMed:17698852). {ECO:0000269|PubMed:16772304,
ECO:0000269|PubMed:17698852}.
-!- DISRUPTION PHENOTYPE: Combined, RNAi-mediated down-regulation of
Salivary cystatin-L and Salivary cystatin-L2 in salivary glands
strongly impairs the tick's ability to feed on hosts. About 40% of
the ticks cannot feed and die. The remainder show much reduced
blood intake, appear unhealthy and display strongly reduced egg
laying. RNAi-treated ticks show an impaired ability to suppress
the host's immune response to tick salivary proteins.
{ECO:0000269|PubMed:17698852}.
-!- SIMILARITY: Belongs to the cystatin family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF483724; AAM93646.1; -; mRNA.
PDB; 4ZM8; X-ray; 2.68 A; A/B/C/D=20-133.
PDBsum; 4ZM8; -.
ProteinModelPortal; Q8MVB6; -.
SMR; Q8MVB6; -.
MEROPS; I25.049; -.
OrthoDB; EOG091G0TP1; -.
EvolutionaryTrace; Q8MVB6; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
CDD; cd00042; CY; 1.
InterPro; IPR027214; Cystatin.
InterPro; IPR000010; Cystatin_dom.
InterPro; IPR018073; Prot_inh_cystat_CS.
PANTHER; PTHR11413; PTHR11413; 1.
Pfam; PF00031; Cystatin; 1.
SMART; SM00043; CY; 1.
PROSITE; PS00287; CYSTATIN; 1.
1: Evidence at protein level;
3D-structure; Disulfide bond; Protease inhibitor; Secreted; Signal;
Thiol protease inhibitor.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 133 Salivary cystatin-L.
{ECO:0000255|RuleBase:RU362130}.
/FTId=PRO_5005401154.
DOMAIN 30 118 Cystatin. {ECO:0000255}.
SITE 24 24 Reactive site.
{ECO:0000250|UniProtKB:P01040}.
DISULFID 89 100 {ECO:0000244|PDB:4ZM8,
ECO:0000269|PubMed:20545851}.
DISULFID 111 130 {ECO:0000244|PDB:4ZM8,
ECO:0000269|PubMed:20545851}.
HELIX 36 51 {ECO:0000244|PDB:4ZM8}.
STRAND 58 90 {ECO:0000244|PDB:4ZM8}.
TURN 97 99 {ECO:0000244|PDB:4ZM8}.
STRAND 109 118 {ECO:0000244|PDB:4ZM8}.
STRAND 123 125 {ECO:0000244|PDB:4ZM8}.
SEQUENCE 133 AA; 14282 MW; F07CF496B55995B7 CRC64;
MTSTFALVLL LGGMAVCVAT GVFGGYSERA NHQANPEFLN LAHYATSTWS AQQPGKTHFD
TVAEVVKVET QVVAGTNYRL TLKVAESTCE LTSTYNKDTC LPKADAAHRT CTTVVFENLQ
GDKSVSPFEC EAA


Related products :

Catalog number Product name Quantity
EIAAB10314 CST4,Cystatin-4,Cystatin-S,Cystatin-SA-III,Homo sapiens,Human,Salivary acidic protein 1
EIAAB10312 CST1,Cystain-SA-I,Cystatin-1,Cystatin-SN,Homo sapiens,Human,Salivary cystatin-SA-1
18-003-44276 Cystatin-S - Cystatin-4; Salivary acidic protein 1; Cystatin-SA-III Polyclonal 0.1 mg Protein A
EIAAB10305 CMAP,CST7,Cystatin-7,Cystatin-F,Cystatin-like metastasis-associated protein,Homo sapiens,Human,Leukocystatin
EIAAB10306 CMAP,Cst7,Cystatin-7,Cystatin-F,Cystatin-like metastasis-associated protein,Leukocystatin,Mouse,Mus musculus
EIAAB10322 CST2,Cystatin-2,Cystatin-S5,Cystatin-SA,Homo sapiens,Human
EIAAB10311 CST6,Cystatin-6,Cystatin-E,Cystatin-M,Homo sapiens,Human
EIAAB32271 Basic salivary proline-rich protein 4,Homo sapiens,Human,Parotid o protein,PRB4,Salivary proline-rich protein II-1,Salivary proline-rich protein Po
CNB-2795580 Recombinant Proteins; Mouse Mouse Cystatin-E _ CST6 _ Cystatin-M _ Cystatin-6 Protein (His Tag) 20
orb81057 Human Cystatin-A protein Cystatin-A Human Recombinant full length protein expressed in E.coli, shows 37 kDa band on SDS-PAGE (including GST tag).The Cystatin-A is purified by proprietary chromatograph 2
20-272-190218 Cystatin A - Mouse monoclonal [WR - 23 _ 2 _ 3 _ 3] to Cystatin A; Stefin-A; Cystatin-AS Monoclonal 0.05 ml
EIAAB09670 Cres,Cst8,Cystatin-8,Cystatin-related epididymal spermatogenic protein,Cystatin-related epididymal-specific protein,Mouse,Mus musculus
EIAAB32270 Basic salivary proline-rich protein 3,Homo sapiens,Human,Parotid salivary glycoprotein G1,PRB3,Proline-rich protein G1
EIAAB32269 Basic salivary proline-rich protein 2,Con1 glycoprotein,Homo sapiens,Human,PRB2,Salivary proline-rich protein
E0476b ELISA kit Bos taurus,Bovine,CSTA,Cystatin-A,Cystatin-AS,Stefin-A,STF1 96T
E0476b ELISA Bos taurus,Bovine,CSTA,Cystatin-A,Cystatin-AS,Stefin-A,STF1 96T
orb81876 Human Cystatin C protein Cystatin C is a purified protein_bioactive peptide. For research use only. 1 mg
U0476b CLIA Bos taurus,Bovine,CSTA,Cystatin-A,Cystatin-AS,Stefin-A,STF1 96T
orb81874 Cystatin C Antigen protein Cystatin C is a purified protein_bioactive peptide. For research use only. 1 mg
U0896Rb CLIA CST3,Cystatin-3,Cystatin-C,Oryctolagus cuniculus,Rabbit 96T
CNB-2795585 Recombinant Proteins; Human CST2 _ Cystatin-2 _ Cystatin-SA Protein (His Tag) 20
CNB-2795575 Recombinant Proteins; Human CST3 _ Cystatin-C _ Cystatin-3 Protein (His Tag) 20
CNB-2795584 Recombinant Proteins; Human CST4 _ Cystatin-4 _ Cystatin-S Protein (His Tag) 100
CNB-2795586 Recombinant Proteins; Human CST1 _ Cystatin-1 _ Cystatin-SN Protein (His Tag) 100
EIAAB09673 CLM,CST9,Cystatin-9,Cystatin-like molecule,Homo sapiens,Human


 

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