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

Killer cell lectin-like receptor 3 (5E6) (Lymphocyte antigen 49c) (Ly-49c) (Nk2.1) (T-cell surface glycoprotein Ly-49C)

 KLRA3_MOUSE             Reviewed;         266 AA.
Q64329; Q3TWQ1; Q3ZB40; Q499I4; Q61154; Q61198; Q64257;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
31-OCT-2012, sequence version 2.
20-DEC-2017, entry version 149.
RecName: Full=Killer cell lectin-like receptor 3;
AltName: Full=5E6;
AltName: Full=Lymphocyte antigen 49c;
Short=Ly-49c;
AltName: Full=Nk2.1;
AltName: Full=T-cell surface glycoprotein Ly-49C;
Name=Klra3; Synonyms=Ly-49c, Ly49C;
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].
STRAIN=C57BL/6 X CBA; TISSUE=Lung;
PubMed=1869832;
Wong S., Freeman J.D., Kelleher C., Mager D., Takei F.;
"Ly-49 multigene family. New members of a superfamily of type II
membrane proteins with lectin-like domains.";
J. Immunol. 147:1417-1423(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ, C57BL/6 X BALB/c, C57BL/6J, CB-17/SCID, and NZB;
PubMed=7629496; DOI=10.1084/jem.182.2.305;
Stoneman E.R., Bennett M., An J., Chesnut K.A., Wakeland E.K.,
Scheerer J.B., Siciliano M.J., Kumar V., Mathew P.A.;
"Cloning and characterization of 5E6(Ly-49C), a receptor molecule
expressed on a subset of murine natural killer cells.";
J. Exp. Med. 182:305-313(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
STRAIN=C57BL/6J; TISSUE=Natural killer cell;
PubMed=8976165; DOI=10.1084/jem.184.6.2085;
Brennan J., Lemieux S., Freeman J.D., Mager D.L., Takei F.;
"Heterogeneity among Ly-49C natural killer (NK) cells:
characterization of highly related receptors with differing functions
and expression patterns.";
J. Exp. Med. 184:2085-2090(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=A/Sn, and C57BL/6J;
PubMed=8892625;
Sundbaeck J., Kaerre K., Sentman C.L.;
"Cloning of minimally divergent allelic forms of the natural killer
(NK) receptor Ly-49C, differentially controlled by host genes in the
MHC and NK gene complexes.";
J. Immunol. 157:3936-3942(1996).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
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).
[6]
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[8]
MUTAGENESIS OF ASN-160; LYS-161; THR-162; ALA-169; ASN-170; HIS-173;
TYR-174; ILE-195; PRO-196; LYS-225; ILE-226; ARG-234; ASP-248; ASN-250
AND ILE-251.
PubMed=11777974; DOI=10.4049/jimmunol.168.2.793;
Sundback J., Achour A., Michaelsson J., Lindstrom H., Karre K.;
"NK cell inhibitory receptor Ly-49C residues involved in MHC class I
binding.";
J. Immunol. 168:793-800(2002).
[9]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 142-263 OF WILD-TYPE AND
MUTANT ARG-121/SER-175/GLU-197/ARG-227 IN COMPLEX WITH H-2K, SUBUNIT,
DISULFIDE BONDS, AND MUTAGENESIS OF ARG-121; SER-175; GLU-197 AND
ARG-227.
PubMed=14595439; DOI=10.1038/ni1006;
Dam J., Guan R., Natarajan K., Dimasi N., Chlewicki L.K., Kranz D.M.,
Schuck P., Margulies D.H., Mariuzza R.A.;
"Variable MHC class I engagement by Ly49 natural killer cell receptors
demonstrated by the crystal structure of Ly49C bound to H-2K(b).";
Nat. Immunol. 4:1213-1222(2003).
[10]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 67-266 ALONE AND IN COMPLEX
WITH H-2K, SUBUNIT, AND DISULFIDE BONDS.
PubMed=18426793; DOI=10.1074/jbc.M801526200;
Deng L., Cho S., Malchiodi E.L., Kerzic M.C., Dam J., Mariuzza R.A.;
"Molecular architecture of the major histocompatibility complex class
I-binding site of Ly49 natural killer cell receptors.";
J. Biol. Chem. 283:16840-16849(2008).
-!- FUNCTION: Receptor on natural killer (NK) cells for class I MHC.
{ECO:0000269|PubMed:8976165}.
-!- SUBUNIT: Homodimer; disulfide-linked.
{ECO:0000269|PubMed:14595439, ECO:0000269|PubMed:18426793}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane
protein.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U10305; AAA19053.1; -; mRNA.
EMBL; U09739; AAA86873.1; -; mRNA.
EMBL; U49865; AAA92951.1; -; mRNA.
EMBL; U49866; AAA92952.1; -; mRNA.
EMBL; U49867; AAA92953.1; -; mRNA.
EMBL; U49868; AAA92954.1; -; mRNA.
EMBL; U56404; AAB19100.1; -; mRNA.
EMBL; U56405; AAB19101.1; -; mRNA.
EMBL; AK159595; BAE35215.1; -; mRNA.
EMBL; AC087336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC099867; AAH99867.1; -; mRNA.
EMBL; BC099878; AAH99878.1; -; mRNA.
EMBL; BC099879; AAH99879.1; -; mRNA.
EMBL; BC099880; AAH99880.1; -; mRNA.
EMBL; BC101952; AAI01953.1; -; mRNA.
EMBL; BC103543; AAI03544.1; -; mRNA.
EMBL; BC103544; AAI03545.1; -; mRNA.
EMBL; BC103545; AAI03546.1; -; mRNA.
EMBL; BC132524; AAI32525.1; -; mRNA.
EMBL; BC132526; AAI32527.1; -; mRNA.
EMBL; BC145192; AAI45193.1; -; mRNA.
EMBL; BC145193; AAI45194.1; -; mRNA.
CCDS; CCDS20601.1; -.
PIR; I49059; I49059.
PIR; I49363; I49363.
RefSeq; NP_001276533.1; NM_001289604.1.
RefSeq; NP_001276534.1; NM_001289605.1.
RefSeq; NP_034778.2; NM_010648.3.
RefSeq; NP_034781.2; NM_010651.3.
RefSeq; XP_011239535.1; XM_011241233.1.
RefSeq; XP_011239537.1; XM_011241235.1.
UniGene; Mm.425338; -.
UniGene; Mm.439698; -.
UniGene; Mm.457996; -.
PDB; 1P1Z; X-ray; 3.26 A; D=143-262.
PDB; 1P4L; X-ray; 2.90 A; D=142-263.
PDB; 3C8J; X-ray; 2.60 A; A/B/C/D=67-266.
PDB; 3C8K; X-ray; 2.90 A; D=142-266.
PDB; 5J6G; X-ray; 3.30 A; G/H=136-266.
PDBsum; 1P1Z; -.
PDBsum; 1P4L; -.
PDBsum; 3C8J; -.
PDBsum; 3C8K; -.
PDBsum; 5J6G; -.
ProteinModelPortal; Q64329; -.
SMR; Q64329; -.
BioGrid; 200995; 1.
STRING; 10090.ENSMUSP00000085333; -.
EPD; Q64329; -.
PaxDb; Q64329; -.
PRIDE; Q64329; -.
DNASU; 16640; -.
Ensembl; ENSMUST00000088017; ENSMUSP00000085333; ENSMUSG00000067591.
Ensembl; ENSMUST00000111998; ENSMUSP00000107629; ENSMUSG00000067591.
GeneID; 16634; -.
GeneID; 16640; -.
KEGG; mmu:16634; -.
KEGG; mmu:16640; -.
UCSC; uc009eik.2; mouse.
CTD; 16634; -.
CTD; 16640; -.
MGI; MGI:101905; Klra3.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
GeneTree; ENSGT00390000008117; -.
HOGENOM; HOG000113237; -.
HOVERGEN; HBG053176; -.
InParanoid; Q64329; -.
OMA; HEKHEPA; -.
OrthoDB; EOG091G0TU6; -.
TreeFam; TF336674; -.
EvolutionaryTrace; Q64329; -.
PRO; PR:Q64329; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000067591; -.
Genevisible; Q64329; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:MGI.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
CDD; cd03593; CLECT_NK_receptors_like; 1.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR013600; Ly49_N.
InterPro; IPR033992; NKR-like_CTLD.
Pfam; PF00059; Lectin_C; 1.
Pfam; PF08391; Ly49; 1.
SMART; SM00034; CLECT; 1.
SUPFAM; SSF56436; SSF56436; 1.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
1: Evidence at protein level;
3D-structure; Cell adhesion; Complete proteome; Disulfide bond;
Glycoprotein; Lectin; Membrane; Receptor; Reference proteome;
Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 266 Killer cell lectin-like receptor 3.
/FTId=PRO_0000046681.
TOPO_DOM 1 48 Cytoplasmic. {ECO:0000255}.
TRANSMEM 49 69 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 70 266 Extracellular. {ECO:0000255}.
DOMAIN 150 258 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
REGION 147 151 Involved in dimerization.
REGION 160 162 Implicated in MHC class I binding.
REGION 195 196 Implicated in MHC class I binding.
REGION 207 208 Implicated in MHC class I binding.
REGION 224 233 Implicated in MHC class I binding.
REGION 240 245 Implicated in MHC class I binding.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 87 87 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 113 113 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 160 160 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 149 154
DISULFID 167 255
DISULFID 171 257
DISULFID 236 249
VARIANT 2 2 S -> N (in strain: C57BL/6 and C57BL/6 X
BALB/c).
VARIANT 22 22 L -> Q (in strain: A/Sn, BALB/c, C57BL/6,
C57BL/6 X BALB/c, C57BL/6 X CBA, CB-17/
SCID and NZB).
VARIANT 34 34 V -> A (in strain: C57BL/6, C57BL/6 X
BALB/c and NZB).
VARIANT 41 42 AP -> VS (in strain: C57BL/6 X BALB/c,
NZB and C57BL/6).
VARIANT 60 60 T -> I (in strain: C57BL/6, C57BL/6 X
BALB/c and NZB).
VARIANT 65 66 AV -> TI (in strain: C57BL/6, C57BL/6 X
BALB/c and NZB).
VARIANT 72 72 N -> S (in strain: C57BL/6, C57BL/6 X
BALB/c and NZB).
VARIANT 85 85 H -> Y (in strain: C57BL/6, C57BL/6 X
BALB/c and NZB).
VARIANT 93 94 RA -> SD (in strain: A/Sn, BALB/c, C57BL/
6, C57BL/6 X BALB/c, C57BL/6 X CBA, CB-
17/SCID and NZB).
VARIANT 115 115 T -> L (in strain: C57BL/6, C57BL/6 X
BALB/c and NZB; requires 2 nucleotide
substitutions).
VARIANT 117 117 E -> D (in strain: C57BL/6 and C57BL/6 X
BALB/c).
VARIANT 127 127 D -> N (in strain: C57BL/6 and C57BL/6 X
BALB/c).
VARIANT 129 129 K -> E (in strain: C57BL/6, C57BL/6 X
BALB/c and NZB).
VARIANT 131 131 K -> N (in strain: NZB).
VARIANT 133 133 V -> I (in strain: NZB).
VARIANT 146 146 Y -> H (in strain: C57BL/6 and C57BL/6 X
BALB/c).
VARIANT 151 151 S -> G (in strain: C57BL/6, C57BL/6 X
BALB/c and NZB).
VARIANT 174 174 Y -> F (in strain: A/Sn, BALB/c, C57BL/6,
C57BL/6 X BALB/c, C57BL/6 X CBA, CB-17/
SCID and NZB).
VARIANT 179 179 L -> V (in strain: C57BL/6, C57BL/6 X
BALB/c and NZB).
VARIANT 189 189 F -> S (in strain: NZB).
VARIANT 198 198 N -> S (in strain: C57BL/6, C57BL/6 X
BALB/c and NZB).
VARIANT 219 219 P -> Q (in strain: C57BL/6, C57BL/6 X
BALB/c and NZB).
VARIANT 226 226 I -> T (in strain: C57BL/6, C57BL/6 X
BALB/c and NZB).
VARIANT 232 232 K -> T (in strain: NZB).
VARIANT 247 247 I -> T (in strain: C57BL/6, C57BL/6 X
BALB/c and NZB).
VARIANT 251 251 I -> T (in strain: NZB).
VARIANT 260 260 K -> R (in strain: NZB).
MUTAGEN 121 121 R->G: Increases stability and improves
binding to MHC I class ligand; when
associated with G-175; G-197 and K-227.
{ECO:0000269|PubMed:14595439}.
MUTAGEN 160 160 N->D: Greatly reduces MHC class I peptide
tetramer binding; when associated with L-
162. {ECO:0000269|PubMed:11777974}.
MUTAGEN 161 161 K->R: No effect on MHC class I peptide
tetramer binding.
{ECO:0000269|PubMed:11777974}.
MUTAGEN 162 162 T->K: Greatly reduces MHC class I peptide
tetramer binding; when associated with D-
160. {ECO:0000269|PubMed:11777974}.
MUTAGEN 169 169 A->Q: No effect on MHC class I peptide
tetramer binding; when associated with T-
170. {ECO:0000269|PubMed:11777974}.
MUTAGEN 170 170 N->T: No effect on MHC class I peptide
tetramer binding; when associated with Q-
169. {ECO:0000269|PubMed:11777974}.
MUTAGEN 173 173 H->S: No effect on MHC class I peptide
tetramer binding; when associated with S-
174. {ECO:0000269|PubMed:11777974}.
MUTAGEN 174 174 Y->S: No effect on MHC class I binding;
when associated with S-173.
{ECO:0000269|PubMed:11777974}.
MUTAGEN 175 175 S->G: Increases stability. Increases
stability and improves binding to MHC I
class ligand; when associated with G-121;
G-197 and K-227.
{ECO:0000269|PubMed:14595439}.
MUTAGEN 195 195 I->P: Greatly reduces MHC class I peptide
tetramer binding; when associated with S-
196. {ECO:0000269|PubMed:11777974}.
MUTAGEN 196 196 P->S: Greatly reduces MHC class I peptide
tetramer binding; when associated with P-
195. {ECO:0000269|PubMed:11777974}.
MUTAGEN 197 197 E->G: Increases stability and improves
binding to MHC I class ligand; when
associated with G-121; G-175 and K-227.
{ECO:0000269|PubMed:14595439}.
MUTAGEN 225 225 K->N: Greatly reduces MHC class I peptide
tetramer binding; when associated with T-
226. {ECO:0000269|PubMed:11777974}.
MUTAGEN 226 226 I->T: Greatly reduces MHC class I peptide
tetramer binding; when associated with N-
225. {ECO:0000269|PubMed:11777974}.
MUTAGEN 227 227 R->K: Increases stability and improves
binding to MHC I class ligand; when
associated with G-121; G-175 and G-197.
{ECO:0000269|PubMed:14595439}.
MUTAGEN 234 234 R->G: No effect on MHC class I peptide
tetramer binding.
{ECO:0000269|PubMed:11777974}.
MUTAGEN 248 248 D->N: No effect on MHC class I peptide
tetramer binding; when associated with D-
250. {ECO:0000269|PubMed:11777974}.
MUTAGEN 250 250 N->D: No effect on MHC class I peptide
tetramer binding; when associated with N-
248. {ECO:0000269|PubMed:11777974}.
MUTAGEN 251 251 I->Q: No effect on MHC class I peptide
tetramer binding.
{ECO:0000269|PubMed:11777974}.
CONFLICT 4 4 P -> L (in Ref. 7; AAH99880/AAH99879/
AAH99878/AAH99867). {ECO:0000305}.
CONFLICT 162 162 T -> M (in Ref. 5; BAE35215).
{ECO:0000305}.
STRAND 145 151 {ECO:0000244|PDB:3C8J}.
STRAND 153 162 {ECO:0000244|PDB:3C8J}.
HELIX 164 173 {ECO:0000244|PDB:3C8J}.
HELIX 184 193 {ECO:0000244|PDB:3C8J}.
STRAND 199 206 {ECO:0000244|PDB:3C8J}.
TURN 207 210 {ECO:0000244|PDB:3C8J}.
STRAND 211 214 {ECO:0000244|PDB:3C8J}.
HELIX 223 227 {ECO:0000244|PDB:3C8J}.
STRAND 233 239 {ECO:0000244|PDB:3C8J}.
STRAND 244 247 {ECO:0000244|PDB:3C8J}.
STRAND 253 260 {ECO:0000244|PDB:3C8J}.
STRAND 262 264 {ECO:0000244|PDB:3C8J}.
SEQUENCE 266 AA; 31311 MW; BF9B10D9B6EFD628 CRC64;
MSEPEVTYST VRLHKSSGLQ KLVRHEETQG PREVGNRKCS APWQLIVKAL GILCFLLLVT
VAVLAVKIFQ YNQHKQEINE TLNHHHNCSN MQRAFNLKEE MLTNKSIDCR PSNETLEYIK
REQDRWDSKT KTVLDSSRDT GRGVKYWFCY STKCYYFIMN KTTWSGCKAN CQHYSVPILK
IEDEDELKFL QRHVIPENYW IGLSYDKKKK EWAWIDNGPS KLDMKIRKMN FKSRGCVFLS
KARIEDIDCN IPYYCICGKK LDKFPD


Related products :

Catalog number Product name Quantity
EIAAB06400 Cd8b,Cd8b1,Ly-3,Lymphocyte antigen 3,Lyt3,Lyt-3,Mouse,Mus musculus,T-cell membrane glycoprotein Ly-3,T-cell surface glycoprotein CD8 beta chain,T-cell surface glycoprotein Lyt-3
EIAAB25056 CD200 cell surface glycoprotein receptor,Cd200r1,Cell surface glycoprotein CD200 receptor 1,Cell surface glycoprotein OX2 receptor 1,Mox2r,OX102 antigen,Ox2r,Rat,Rattus norvegicus
U1513m CLIA B-cell receptor CD22,BL-CAM,B-lymphocyte cell adhesion molecule,Cd22,Lyb-8,Mouse,Mus musculus,Sialic acid-binding Ig-like lectin 2,Siglec2,Siglec-2,T-cell surface antigen Leu-14 96T
E1513m ELISA kit B-cell receptor CD22,BL-CAM,B-lymphocyte cell adhesion molecule,Cd22,Lyb-8,Mouse,Mus musculus,Sialic acid-binding Ig-like lectin 2,Siglec2,Siglec-2,T-cell surface antigen Leu-14 96T
E1513m ELISA B-cell receptor CD22,BL-CAM,B-lymphocyte cell adhesion molecule,Cd22,Lyb-8,Mouse,Mus musculus,Sialic acid-binding Ig-like lectin 2,Siglec2,Siglec-2,T-cell surface antigen Leu-14 96T
U1513h CLIA B-cell receptor CD22,BL-CAM,B-lymphocyte cell adhesion molecule,CD22,Homo sapiens,Human,Sialic acid-binding Ig-like lectin 2,SIGLEC2,Siglec-2,T-cell surface antigen Leu-14 96T
E1513h ELISA B-cell receptor CD22,BL-CAM,B-lymphocyte cell adhesion molecule,CD22,Homo sapiens,Human,Sialic acid-binding Ig-like lectin 2,SIGLEC2,Siglec-2,T-cell surface antigen Leu-14 96T
E1513h ELISA kit B-cell receptor CD22,BL-CAM,B-lymphocyte cell adhesion molecule,CD22,Homo sapiens,Human,Sialic acid-binding Ig-like lectin 2,SIGLEC2,Siglec-2,T-cell surface antigen Leu-14 96T
20-783-70379 MOUSE ANTI FELINE CD8 ALPHA_BETA - T-cell surface glycoprotein Lyt-3; T-cell membrane glycoprotein Ly-3; Lymphocyte antigen 3; CD8b antigen Monoclonal 0.25 mg
20-783-73907 MOUSE ANTI LAPINE CD8 FITC - T-cell surface glycoprotein Lyt-3; T-cell membrane glycoprotein Ly-3; Lymphocyte antigen 3; CD8b antigen Monoclonal 0.1 mg
20-783-70209 MOUSE ANTI HUMAN CD8 FITC - T8; T-cell surface glycoprotein Lyt-3; T-cell membrane glycoprotein Ly-3; Lymphocyte antigen 3; CD8b antigen Monoclonal 0.1 mg
20-783-70208 MOUSE ANTI HUMAN CD8 Biotin - T8; T-cell surface glycoprotein Lyt-3; T-cell membrane glycoprotein Ly-3; Lymphocyte antigen 3; CD8b antigen Monoclonal 0.1 mg
20-783-72711 MOUSE ANTI RAT CD8 BETA FITC - T-cell surface glycoprotein Lyt-3; T-cell membrane glycoprotein Ly-3; Lymphocyte antigen 3; CD8b antigen Monoclonal 0.1 mg
20-783-71692 MOUSE ANTI OVINE CD8 FITC - T-cell surface glycoprotein Lyt-3; T-cell membrane glycoprotein Ly-3; Lymphocyte antigen 3; CD8b antigen Monoclonal 0.1 mg
20-783-70111 RAT ANTI MOUSE CD8 Azide Free - LY-2; T-cell surface glycoprotein Lyt-3; T-cell membrane glycoprotein Ly-3; Lymphocyte antigen 3; CD8b antigen Monoclonal 1 mg
20-783-70212 MOUSE ANTI HUMAN CD8 Azide Free - T8; T-cell surface glycoprotein Lyt-3; T-cell membrane glycoprotein Ly-3; Lymphocyte antigen 3; CD8b antigen Monoclonal 1 mg
20-783-71988 MOUSE ANTI EQUINE CD8 - T-cell surface glycoprotein Lyt-3; T-cell membrane glycoprotein Ly-3; Lymphocyte antigen 3; CD8b antigen Monoclonal 2 ml
20-783-71002 MOUSE ANTI HUMAN CD8 - T8; T-cell surface glycoprotein Lyt-3; T-cell membrane glycoprotein Ly-3; Lymphocyte antigen 3; CD8b antigen Monoclonal 0.1 ml
20-783-71001 MOUSE ANTI HUMAN CD8 - T8; T-cell surface glycoprotein Lyt-3; T-cell membrane glycoprotein Ly-3; Lymphocyte antigen 3; CD8b antigen Monoclonal 1 ml
20-783-70211 MOUSE ANTI HUMAN CD8 RPE - T8; T-cell surface glycoprotein Lyt-3; T-cell membrane glycoprotein Ly-3; Lymphocyte antigen 3; CD8b antigen Monoclonal 100 TESTS
20-783-70206 MOUSE ANTI HUMAN CD8 - T8; T-cell surface glycoprotein Lyt-3; T-cell membrane glycoprotein Ly-3; Lymphocyte antigen 3; CD8b antigen Monoclonal 0.2 mg
20-783-72066 RAT ANTI HUMAN CD8 FITC - T8; T-cell surface glycoprotein Lyt-3; T-cell membrane glycoprotein Ly-3; Lymphocyte antigen 3; CD8b antigen Monoclonal 100 TESTS
20-783-72712 MOUSE ANTI RAT CD8 BETA - T-cell surface glycoprotein Lyt-3; T-cell membrane glycoprotein Ly-3; Lymphocyte antigen 3; CD8b antigen Monoclonal 0.1 mg
20-783-72710 MOUSE ANTI RAT CD8 BETA - T-cell surface glycoprotein Lyt-3; T-cell membrane glycoprotein Ly-3; Lymphocyte antigen 3; CD8b antigen Monoclonal 0.25 mg
20-783-70207 MOUSE ANTI HUMAN CD8 APC - T8; T-cell surface glycoprotein Lyt-3; T-cell membrane glycoprotein Ly-3; Lymphocyte antigen 3; CD8b antigen Monoclonal 100 TESTS


 

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