GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

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

Phosphate-binding protein PstS 1 (PBP 1) (PhoS1) (PstS-1) (38-kDa glycolipoprotein) (38-kDa lipoprotein) (P38) (Antigen Ag78) (Protein antigen B) (Pab)

 PSTS1_MYCTU             Reviewed;         374 AA.
P9WGU1; L0T854; O05868; P15712;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
22-APR-2020, entry version 36.
RecName: Full=Phosphate-binding protein PstS 1;
Short=PBP 1;
Short=PhoS1 {ECO:0000303|PubMed:19362712};
Short=PstS-1;
AltName: Full=38-kDa glycolipoprotein {ECO:0000303|PubMed:16622205};
AltName: Full=38-kDa lipoprotein {ECO:0000303|PubMed:1906192};
Short=P38;
AltName: Full=Antigen Ag78;
AltName: Full=Protein antigen B {ECO:0000303|PubMed:2545626};
Short=Pab {ECO:0000303|PubMed:2545626};
Flags: Precursor;
Name=pstS1; Synonyms=phoS1; OrderedLocusNames=Rv0934;
ORFNames=MTCY08D9.05c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2545626;
Andersen A.B., Hansen E.B.;
"Structure and mapping of antigenic domains of protein antigen b, a 38,000-
molecular-weight protein of Mycobacterium tuberculosis.";
Infect. Immun. 57:2481-2488(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the complete
genome sequence.";
Nature 393:537-544(1998).
[3]
FUNCTION IN INFECTION, SUBCELLULAR LOCATION, AND PALMITOYLATION AT CYS-24.
STRAIN=H37Rv;
PubMed=1906192; DOI=10.1016/0923-2508(91)90097-t;
Young D.B., Garbe T.R.;
"Lipoprotein antigens of Mycobacterium tuberculosis.";
Res. Microbiol. 142:55-65(1991).
[4]
FUNCTION, AND PHOSPHATE-BINDING.
STRAIN=H37Rv;
PubMed=8294447;
Chang Z., Choudhary A., Lathigra R., Quiocho F.A.;
"The immunodominant 38-kDa lipoprotein antigen of Mycobacterium
tuberculosis is a phosphate-binding protein.";
J. Biol. Chem. 269:1956-1958(1994).
[5]
SUBCELLULAR LOCATION, AND INDUCTION BY PHOSPHATE STARVATION.
STRAIN=H37Rv;
PubMed=1612766;
Espitia C., Elinos M., Hernandez-Pando R., Mancilla R.;
"Phosphate starvation enhances expression of the immunodominant 38-
kilodalton protein antigen of Mycobacterium tuberculosis: demonstration by
immunogold electron microscopy.";
Infect. Immun. 60:2998-3001(1992).
[6]
SUBCELLULAR LOCATION.
STRAIN=H37Rv;
PubMed=10426995; DOI=10.1126/science.285.5428.732;
Brightbill H.D., Libraty D.H., Krutzik S.R., Yang R.B., Belisle J.T.,
Bleharski J.R., Maitland M., Norgard M.V., Plevy S.E., Smale S.T.,
Brennan P.J., Bloom B.R., Godowski P.J., Modlin R.L.;
"Host defense mechanisms triggered by microbial lipoproteins through Toll-
like receptors.";
Science 285:732-736(1999).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=H37Rv;
PubMed=15731097; DOI=10.1128/iai.73.3.1898-1902.2005;
Peirs P., Lefevre P., Boarbi S., Wang X.M., Denis O., Braibant M.,
Pethe K., Locht C., Huygen K., Content J.;
"Mycobacterium tuberculosis with disruption in genes encoding the phosphate
binding proteins PstS1 and PstS2 is deficient in phosphate uptake and
demonstrates reduced in vivo virulence.";
Infect. Immun. 73:1898-1902(2005).
[8]
FUNCTION IN INFECTION, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 27294 / TMC 102 / H37Rv;
PubMed=16622205; DOI=10.1128/iai.74.5.2686-2696.2006;
Jung S.B., Yang C.S., Lee J.S., Shin A.R., Jung S.S., Son J.W.,
Harding C.V., Kim H.J., Park J.K., Paik T.H., Song C.H., Jo E.K.;
"The mycobacterial 38-kilodalton glycolipoprotein antigen activates the
mitogen-activated protein kinase pathway and release of proinflammatory
cytokines through Toll-like receptors 2 and 4 in human monocytes.";
Infect. Immun. 74:2686-2696(2006).
[9]
FUNCTION IN INFECTION.
STRAIN=H37Rv;
PubMed=19140873; DOI=10.1111/j.1365-3083.2008.02193.x;
Sanchez A., Espinosa P., Esparza M.A., Colon M., Bernal G., Mancilla R.;
"Mycobacterium tuberculosis 38-kDa lipoprotein is apoptogenic for human
monocyte-derived macrophages.";
Scand. J. Immunol. 69:20-28(2009).
[10]
FUNCTION IN INFECTION.
STRAIN=H37Rv;
PubMed=19362712; DOI=10.1016/j.cellimm.2009.03.008;
Drage M.G., Pecora N.D., Hise A.G., Febbraio M., Silverstein R.L.,
Golenbock D.T., Boom W.H., Harding C.V.;
"TLR2 and its co-receptors determine responses of macrophages and dendritic
cells to lipoproteins of Mycobacterium tuberculosis.";
Cell. Immunol. 258:29-37(2009).
[11]
FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
STRAIN=H37Rv;
PubMed=20933472; DOI=10.1016/j.tube.2010.09.004;
Vanzembergh F., Peirs P., Lefevre P., Celio N., Mathys V., Content J.,
Kalai M.;
"Effect of PstS sub-units or PknD deficiency on the survival of
Mycobacterium tuberculosis.";
Tuberculosis 90:338-345(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.m111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[13]
BIOTECHNOLOGY.
PubMed=23719937; DOI=10.1002/eji.201243245;
Palma C., Schiavoni G., Abalsamo L., Mattei F., Piccaro G., Sanchez M.,
Fernandez C., Singh M., Gabriele L.;
"Mycobacterium tuberculosis PstS1 amplifies IFN-gamma and induces IL-17/IL-
22 responses by unrelated memory CD4+ T cells via dendritic cell
activation.";
Eur. J. Immunol. 43:2386-2397(2013).
[14]
FUNCTION IN INFECTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
STRAIN=H37Rv;
PubMed=25359607; DOI=10.1111/sji.12249;
Esparza M., Palomares B., Garcia T., Espinosa P., Zenteno E., Mancilla R.;
"PstS-1, the 38-kDa Mycobacterium tuberculosis glycoprotein, is an adhesin,
which binds the macrophage mannose receptor and promotes phagocytosis.";
Scand. J. Immunol. 81:46-55(2015).
[15]
FUNCTION IN INFECTION.
STRAIN=ATCC 27294 / TMC 102 / H37Rv;
PubMed=25544271; DOI=10.1007/s10495-014-1080-2;
Lim Y.J., Choi J.A., Lee J.H., Choi C.H., Kim H.J., Song C.H.;
"Mycobacterium tuberculosis 38-kDa antigen induces endoplasmic reticulum
stress-mediated apoptosis via toll-like receptor 2/4.";
Apoptosis 20:358-370(2015).
[16]
REVIEW.
PubMed=20234378; DOI=10.1038/nrmicro2321;
Harding C.V., Boom W.H.;
"Regulation of antigen presentation by Mycobacterium tuberculosis: a role
for Toll-like receptors.";
Nat. Rev. Microbiol. 8:296-307(2010).
[17]
X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 25-374 IN COMPLEX WITH PHOSPHATE.
STRAIN=H37Rv;
PubMed=12842040; DOI=10.1016/s0969-2126(03)00109-6;
Vyas N.K., Vyas M.N., Quiocho F.A.;
"Crystal structure of M tuberculosis ABC phosphate transport receptor:
specificity and charge compensation dominated by ion-dipole interactions.";
Structure 11:765-774(2003).
-!- FUNCTION: Functions in inorganic phosphate uptake, although probably
not the main uptake protein under phosphate starvation
(PubMed:15731097, PubMed:20933472). Binds phosphate; probably able to
bind both H(2)PO(4)(-) and HPO(4)(2-) (PubMed:8294447,
PubMed:12842040). Part of the ABC transporter complex PstSACB involved
in phosphate import (Probable). {ECO:0000269|PubMed:12842040,
ECO:0000269|PubMed:15731097, ECO:0000269|PubMed:20933472,
ECO:0000269|PubMed:8294447, ECO:0000305}.
-!- FUNCTION: A host TLR2 agonist (toll-like receptor), shown
experimentally for human and mouse (PubMed:1906192, PubMed:19362712).
Requires both host TLR1 and TLR2 as coreceptors to elicit host response
in mouse (TLR6 may also play a role) neither CD14 or CD36 function as
accessory receptors (PubMed:19362712). Protein purified from culture
filtrate induces host (human) monocytes to produce TNF-alpha, IL-6 and
IL-12 p40 (IL12B) via ERK1/2 (MAPK3 and MAPK1) and p38 MAPK pathways;
MEK inhibitors U0126 and PD98059 and p38 inhibitor SB203580 block most
cytokine production (PubMed:16622205). Host ERK1/2 and p38 MAPK
activation is mediated mainly by TLR2, but also partially by TLR4, and
unlike the case for lipoprotein LpqH the protein moiety of PstS1 seems
to be the antigenic agent (PubMed:16622205). Greater activation of
ERK1/2 and p38 MAPK is seen in patients with active pulmonary
tuberculosis than in tuberculin-negative patients (PubMed:16622205).
Induces apoptosis when incubated with human monocyte-derived
macrophages via TLR2 (PubMed:19140873). Protein purified from culture
filtrate acts via TLR2 and TLR4 to induce host macrophage (shown for
mouse) endoplasmic reticulum stress-mediated apoptosis via MAPK (at
least JNK), C-C motif chemokine 2 (MCP-1, Ccl2) and ZC3H12
endoribonucleases (MCPIP, Zc3h12) (PubMed:25544271). Functions as an
adhesin, binds to human and mouse macrophages via mannose residues,
binds to the mouse macrophage mannose receptor (possibly Mrc1) and
mediates bacterial phagocytosis (PubMed:25359607).
{ECO:0000269|PubMed:16622205, ECO:0000269|PubMed:1906192,
ECO:0000269|PubMed:19140873, ECO:0000269|PubMed:19362712,
ECO:0000269|PubMed:25359607, ECO:0000269|PubMed:25544271}.
-!- SUBUNIT: The ABC transporter complex is composed of two ATP-binding
proteins (PstB), two transmembrane proteins (PstC and PstA) and a
solute-binding protein (PstS). {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
{ECO:0000305|PubMed:1906192}. Cell surface {ECO:0000269|PubMed:1612766,
ECO:0000269|PubMed:25359607}. Secreted, cell wall
{ECO:0000269|PubMed:10426995}. Secreted {ECO:0000305|PubMed:16622205,
ECO:0000305|PubMed:1906192}. Note=A soluble cell wall-associated
protein (PubMed:10426995). Also found in culture filtrate in increasing
quantities during growth (PubMed:1906192, PubMed:16622205).
{ECO:0000269|PubMed:10426995, ECO:0000269|PubMed:16622205,
ECO:0000269|PubMed:1906192}.
-!- INDUCTION: Transcription slightly induced by phosphate starvation, part
of the pstB3-pstS2-pstC1-pstA2 operon (PubMed:20933472). Strongly
induced by phosphate starvation (at protein level) (PubMed:1612766).
Also shown to be only slightly induced by phosphate starvation; results
may depend on growth media (at protein level) (PubMed:20933472).
{ECO:0000269|PubMed:1612766, ECO:0000269|PubMed:20933472}.
-!- PTM: Glycosylated, probably with mannose residues; treatment with
alpha-D-mannosidase abolishes its interaction with concanavalin A.
{ECO:0000269|PubMed:25359607}.
-!- DISRUPTION PHENOTYPE: No growth phenotype in phosphate-rich medium (3.6
mM Pi), decreased phosphate uptake in phosphate-depleted medium
(PubMed:15731097). Grows faster than wild-type in restricted (Sauton)
phosphate-free medium, even after nutrient starvation
(PubMed:20933472). Decreased growth in infected BALB/c and C57BL/6 mice
for up to 5 months after infection (PubMed:15731097).
{ECO:0000269|PubMed:15731097, ECO:0000269|PubMed:20933472}.
-!- BIOTECHNOLOGY: When used as a vaccine has immunostimulatory properties;
it stimulates the differentiation of unrelated antigen memory CD4+ T-
cells to produce IFN-gamma, IL-17 and IL-22.
{ECO:0000269|PubMed:23719937}.
-!- SIMILARITY: Belongs to the PstS family. {ECO:0000305}.
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; M30046; AAA25374.1; -; Genomic_DNA.
EMBL; AL123456; CCP43682.1; -; Genomic_DNA.
PIR; F70584; F70584.
RefSeq; WP_003900236.1; NZ_NVQJ01000001.1.
RefSeq; YP_177770.1; NC_000962.3.
PDB; 1PC3; X-ray; 2.16 A; A/B=25-374.
PDBsum; 1PC3; -.
SMR; P9WGU1; -.
STRING; 83332.Rv0934; -.
PaxDb; P9WGU1; -.
PRIDE; P9WGU1; -.
EnsemblBacteria; CCP43682; CCP43682; Rv0934.
GeneID; 885724; -.
KEGG; mtu:Rv0934; -.
KEGG; mtv:RVBD_0934; -.
TubercuList; Rv0934; -.
eggNOG; ENOG4107RBH; Bacteria.
eggNOG; COG0226; LUCA.
KO; K02040; -.
OMA; DNIGGEG; -.
PhylomeDB; P9WGU1; -.
BioCyc; MTBH37RV:G185E-5089-MONOMER; -.
Reactome; R-HSA-9637628; Modulation by Mtb of host immune system.
Proteomes; UP000001584; Chromosome.
GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005829; C:cytosol; HDA:MTBBASE.
GO; GO:0005576; C:extracellular region; IGI:MTBBASE.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0042301; F:phosphate ion binding; IDA:MTBBASE.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0016036; P:cellular response to phosphate starvation; IEP:MTBBASE.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0035435; P:phosphate ion transmembrane transport; IEA:InterPro.
GO; GO:0006817; P:phosphate ion transport; IMP:MTBBASE.
InterPro; IPR005673; ABC_phos-bd_PstS.
InterPro; IPR024370; PBP_domain.
Pfam; PF12849; PBP_like_2; 1.
PIRSF; PIRSF002756; PstS; 1.
TIGRFAMs; TIGR00975; 3a0107s03; 1.
PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
1: Evidence at protein level;
3D-structure; Cell adhesion; Cell membrane; Cell wall; Glycoprotein;
Lipoprotein; Membrane; Palmitate; Phosphate transport; Reference proteome;
Secreted; Signal; Transport; Virulence.
SIGNAL 1..23
/evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
CHAIN 24..374
/note="Phosphate-binding protein PstS 1"
/id="PRO_0000031854"
REGION 58..60
/note="Phosphate binding"
/evidence="ECO:0000269|PubMed:12842040"
REGION 185..191
/note="Phosphate binding"
/evidence="ECO:0000269|PubMed:12842040"
BINDING 88
/note="Phosphate"
/evidence="ECO:0000269|PubMed:12842040"
BINDING 106
/note="Phosphate"
/evidence="ECO:0000269|PubMed:12842040"
LIPID 24
/note="N-palmitoyl cysteine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
ECO:0000305|PubMed:1906192"
LIPID 24
/note="S-diacylglycerol cysteine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
STRAND 51..57
/evidence="ECO:0000244|PDB:1PC3"
TURN 59..61
/evidence="ECO:0000244|PDB:1PC3"
HELIX 62..75
/evidence="ECO:0000244|PDB:1PC3"
STRAND 79..82
/evidence="ECO:0000244|PDB:1PC3"
HELIX 88..96
/evidence="ECO:0000244|PDB:1PC3"
STRAND 101..107
/evidence="ECO:0000244|PDB:1PC3"
HELIX 111..116
/evidence="ECO:0000244|PDB:1PC3"
STRAND 120..134
/evidence="ECO:0000244|PDB:1PC3"
HELIX 147..154
/evidence="ECO:0000244|PDB:1PC3"
HELIX 164..169
/evidence="ECO:0000244|PDB:1PC3"
STRAND 184..187
/evidence="ECO:0000244|PDB:1PC3"
HELIX 190..202
/evidence="ECO:0000244|PDB:1PC3"
TURN 204..211
/evidence="ECO:0000244|PDB:1PC3"
STRAND 214..216
/evidence="ECO:0000244|PDB:1PC3"
HELIX 230..240
/evidence="ECO:0000244|PDB:1PC3"
STRAND 244..249
/evidence="ECO:0000244|PDB:1PC3"
HELIX 250..252
/evidence="ECO:0000244|PDB:1PC3"
HELIX 253..258
/evidence="ECO:0000244|PDB:1PC3"
STRAND 265..267
/evidence="ECO:0000244|PDB:1PC3"
HELIX 278..285
/evidence="ECO:0000244|PDB:1PC3"
TURN 286..290
/evidence="ECO:0000244|PDB:1PC3"
STRAND 312..322
/evidence="ECO:0000244|PDB:1PC3"
HELIX 326..339
/evidence="ECO:0000244|PDB:1PC3"
HELIX 342..344
/evidence="ECO:0000244|PDB:1PC3"
HELIX 346..349
/evidence="ECO:0000244|PDB:1PC3"
TURN 350..353
/evidence="ECO:0000244|PDB:1PC3"
HELIX 359..369
/evidence="ECO:0000244|PDB:1PC3"
SEQUENCE 374 AA; 38243 MW; 6334968191FF38AA CRC64;
MKIRLHTLLA VLTAAPLLLA AAGCGSKPPS GSPETGAGAG TVATTPASSP VTLAETGSTL
LYPLFNLWGP AFHERYPNVT ITAQGTGSGA GIAQAAAGTV NIGASDAYLS EGDMAAHKGL
MNIALAISAQ QVNYNLPGVS EHLKLNGKVL AAMYQGTIKT WDDPQIAALN PGVNLPGTAV
VPLHRSDGSG DTFLFTQYLS KQDPEGWGKS PGFGTTVDFP AVPGALGENG NGGMVTGCAE
TPGCVAYIGI SFLDQASQRG LGEAQLGNSS GNFLLPDAQS IQAAAAGFAS KTPANQAISM
IDGPAPDGYP IINYEYAIVN NRQKDAATAQ TLQAFLHWAI TDGNKASFLD QVHFQPLPPA
VVKLSDALIA TISS


Related products :

Catalog number Product name Quantity
abx109230 Polyclonal Rabbit Phosphate-binding protein PstS 1 Antibody (HRP) 100 μg
CSB-RP149194Ba Recombinant Ba(Mycobacterium tuberculosis) Phosphate-binding protein PstS 1 500ug
abx106401 Polyclonal Rabbit Phosphate-binding protein PstS 1 Antibody (Biotin) 100 μg
abx107813 Polyclonal Rabbit Phosphate-binding protein PstS 1 Antibody (FITC) 100 μg
CSB-RP149194Ba Recombinant Ba(Mycobacterium tuberculosis) Phosphate-binding protein PstS 1 Source: E.coli 1mg
101-M531 Kallikrein 4 Anti-Human Host: Mouse KLK4; ARM1; EMSP; PSTS; AI2A1; EMSP1; KLK-L1; PRSS17; kallikrein 100
101-M531 Kallikrein 4, Host: Mouse, Species: Anti-Human, Synonyms: KLK4; ARM1; EMSP; PSTS; AI2A1; EMSP1; KLK-L1; PRSS17; kallikrein 100 ug
EIAAB27565 Homo sapiens,Human,Neuro-oncological ventral antigen 1,NOVA1,Onconeural ventral antigen 1,Paraneoplastic Ri antigen,RNA-binding protein Nova-1,Ventral neuron-specific protein 1
18-003-43641 RNA-binding protein 38 - RNA-binding motif protein 38; RNA-binding region-containing protein 1; HSRNASEB; ssDNA-binding protein SEB4; CLL-associated antigen KW-5 Polyclonal 0.05 mg Aff Pur
E1257h ELISA kit DEF3,Homo sapiens,Human,Lung cancer antigen NY-LU-12,Protein G16,RBM6,RNA-binding motif protein 6,RNA-binding protein 6,RNA-binding protein DEF-3 96T
U1257h CLIA DEF3,Homo sapiens,Human,Lung cancer antigen NY-LU-12,Protein G16,RBM6,RNA-binding motif protein 6,RNA-binding protein 6,RNA-binding protein DEF-3 96T
E1257h ELISA DEF3,Homo sapiens,Human,Lung cancer antigen NY-LU-12,Protein G16,RBM6,RNA-binding motif protein 6,RNA-binding protein 6,RNA-binding protein DEF-3 96T
18-003-43228 Apoptosis-stimulating of p53 protein 2 - Tumor suppressor p53-binding protein 2; p53-binding protein 2; p53BP2; 53BP2; Bcl2-binding protein; Bbp; NY-REN-51 antigen Polyclonal 0.05 mg Aff Pur
EIAAB33981 CLL-associated antigen KW-5,Homo sapiens,HSRNASEB,Human,RBM38,RNA-binding motif protein 38,RNA-binding protein 38,RNA-binding region-containing protein 1,RNPC1,SEB4,ssDNA-binding protein SEB4
10-288-22418F Galectin-3-binding protein - Lectin galactoside-binding soluble 3-binding protein; Mac-2-binding protein; Mac-2 BP; MAC2BP; Tumor-associated antigen 90K 0.05 mg
10-288-22418F Galectin-3-binding protein - Lectin galactoside-binding soluble 3-binding protein; Mac-2-binding protein; Mac-2 BP; MAC2BP; Tumor-associated antigen 90K 0.1 mg
EIAAB31521 47 kDa mannose 6-phosphate receptor-binding protein,47 kDa MPR-binding protein,Cargo selection protein TIP47,Homo sapiens,Human,M6PRBP1,Mannose-6-phosphate receptor-binding protein 1,Perilipin-3,Place
15-288-22299F Mannose-6-phosphate receptor-binding protein 1 - Cargo selection protein TIP47; 47 kDa mannose 6-phosphate receptor-binding protein; 47 kDa MPR-binding protein; Placental protein 17; PP17 Polyclonal 0.1 mg
15-288-22299F Mannose-6-phosphate receptor-binding protein 1 - Cargo selection protein TIP47; 47 kDa mannose 6-phosphate receptor-binding protein; 47 kDa MPR-binding protein; Placental protein 17; PP17 Polyclonal 0.05 mg
10-288-22299F Mannose-6-phosphate receptor-binding protein 1 - Cargo selection protein TIP47; 47 kDa mannose 6-phosphate receptor-binding protein; 47 kDa MPR-binding protein; Placental protein 17; PP17 0.1 mg
10-288-22299F Mannose-6-phosphate receptor-binding protein 1 - Cargo selection protein TIP47; 47 kDa mannose 6-phosphate receptor-binding protein; 47 kDa MPR-binding protein; Placental protein 17; PP17 0.05 mg
EIAAB06261 150 kDa TGF-beta-1-binding protein,C3 and PZP-like alpha-2-macroglobulin domain-containing protein 7,CD109,CD109 antigen,CPAMD7,Homo sapiens,Human,p180,Platelet-specific Gov antigen,r150
15-288-22813 Antigen 85-A - 85A; Antigen 85 complex A; Ag85A; Mycolyl transferase 85A; EC 2.3.1.-; Fibronectin-binding protein A Polyclonal 0.1 mg
15-288-22813 Antigen 85-A - 85A; Antigen 85 complex A; Ag85A; Mycolyl transferase 85A; EC 2.3.1.-; Fibronectin-binding protein A Polyclonal 0.05 mg
EIAAB45453 AIE75,Antigen NY-CO-38_NY-CO-37,Autoimmune enteropathy-related antigen AIE-75,Harmonin,Homo sapiens,Human,Protein PDZ-73,Renal carcinoma antigen NY-REN-3,USH1C,Usher syndrome type-1C protein
Pathways :
WP1531: Vitamin D synthesis
WP1616: ABC transporters
WP1657: Glycerolipid metabolism
WP731: Sterol regulatory element binding protein related
WP2292: Chemokine signaling pathway
WP1493: Carbon assimilation C4 pathway
WP1678: Nucleotide excision repair
WP2324: AGE/RAGE pathway
WP1624: Bacterial secretion system
WP1689: Porphyrin and chlorophyll metabolism
WP1650: Fluorobenzoate degradation
WP2032: TSH signaling pathway
WP1165: G Protein Signaling Pathways
WP1693: Purine metabolism
WP346: Protein Modifications
WP1663: Homologous recombination
WP2203: TSLP Signaling Pathway
WP931: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1713: Two-component system
WP1672: Mismatch repair
WP2272: Pathogenic Escherichia coli infection
WP1676: Non-homologous end-joining
WP232: G Protein Signaling Pathways
WP1892: Protein folding

Related Genes :
[pstS1 phoS1 Rv0934 MTCY08D9.05c] Phosphate-binding protein PstS 1 (PBP 1) (PhoS1) (PstS-1) (38-kDa glycolipoprotein) (38-kDa lipoprotein) (P38) (Antigen Ag78) (Protein antigen B) (Pab)
[lpqH Rv3763 MTV025.111] Lipoprotein LpqH (19 kDa lipoprotein antigen) (Putative transporter LpqH) (p19)
[MAPK14 CSBP CSBP1 CSBP2 CSPB1 MXI2 SAPK2A] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Cytokine suppressive anti-inflammatory drug-binding protein) (CSAID-binding protein) (CSBP) (MAP kinase MXI2) (MAX-interacting protein 2) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha) (Stress-activated protein kinase 2a) (SAPK2a)
[C PreC preC PreC-C preC-C PreC/C precore precore+core] Capsid protein (Core antigen) (Core protein) (HBcAg) (p21.5)
[Pa2g4 Ebp1 Plfap] Proliferation-associated protein 2G4 (IRES-specific cellular trans-acting factor 45 kDa) (ITAF45) (Mpp1) (Proliferation-associated protein 1) (Protein p38-2G4)
[pstS3 phoS2 Rv0928 MTCY21C12.22] Phosphate-binding protein PstS 3 (PBP 3) (PstS-3) (Antigen Ag88)
[Mapk14 Crk1 Csbp1 Csbp2] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (CRK1) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[S Large S P PreS1 preS1 PreS1-S preS1-S preS2] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
[Mapk14 Csbp1 Csbp2] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (CRK1) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[MAPK11 PRKM11 SAPK2 SAPK2B] Mitogen-activated protein kinase 11 (MAP kinase 11) (MAPK 11) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 beta) (MAP kinase p38 beta) (p38b) (Stress-activated protein kinase 2b) (SAPK2b) (p38-2)
[pmk-1 B0218.3] Mitogen-activated protein kinase pmk-1 (EC 2.7.11.24) (Stress-activated protein kinase pmk-1) (p38 MAP kinase 1)
[MAPK14 CSBP1 CSBP2] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[XRCC6 G22P1] X-ray repair cross-complementing protein 6 (EC 3.6.4.-) (EC 4.2.99.-) (5'-deoxyribose-5-phosphate lyase Ku70) (5'-dRP lyase Ku70) (70 kDa subunit of Ku antigen) (ATP-dependent DNA helicase 2 subunit 1) (ATP-dependent DNA helicase II 70 kDa subunit) (CTC box-binding factor 75 kDa subunit) (CTC75) (CTCBF) (DNA repair protein XRCC6) (Lupus Ku autoantigen protein p70) (Ku70) (Thyroid-lupus autoantigen) (TLAA) (X-ray repair complementing defective repair in Chinese hamster cells 6)
[apa modD Rv1860 MTCY359.13] Alanine and proline-rich secreted protein Apa (45 kDa glycoprotein) (45/47 kDa antigen) (Antigen MPT-32) (FAP-B) (Fibronectin attachment protein) (Immunogenic protein MPT32)
[Mapk11 Prkm11] Mitogen-activated protein kinase 11 (MAP kinase 11) (MAPK 11) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 beta) (MAP kinase p38 beta) (p38B)
[p38b CG7393] Mitogen-activated protein kinase p38b (MAP kinase p38b) (MAPK p38b) (EC 2.7.11.24)
[mapk14b mapk14] Mitogen-activated protein kinase 14B (MAP kinase 14B) (MAPK 14B) (EC 2.7.11.24) (Mitogen-activated protein kinase p38b) (MAP kinase p38b) (zp38b)
[AIMP2 JTV1 PRO0992] Aminoacyl tRNA synthase complex-interacting multifunctional protein 2 (Multisynthase complex auxiliary component p38) (Protein JTV-1)
[C c core PreC preC] Capsid protein (Core antigen) (Core protein) (HBcAg) (p21.5)
[mapk14b] Mitogen-activated protein kinase 14B (MAP kinase 14B) (MAPK 14B) (EC 2.7.11.24) (Mitogen-activated protein kinase p38b) (MAP kinase p38b) (cp38b)
[MAPK13 PRKM13 SAPK4] Mitogen-activated protein kinase 13 (MAP kinase 13) (MAPK 13) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 delta) (MAP kinase p38 delta) (Stress-activated protein kinase 4)
[MAPK12 ERK6 SAPK3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
[Mapk12 Sapk3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
[Mapk12 Sapk3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
[Mapk13] Mitogen-activated protein kinase 13 (MAP kinase 13) (MAPK 13) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 delta) (MAP kinase p38 delta) (Stress-activated protein kinase 4)
[Mapk13 Serk4] Mitogen-activated protein kinase 13 (MAP kinase 13) (MAPK 13) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 delta) (MAP kinase p38 delta) (Stress-activated protein kinase 4)
[HSP90AA1 HSP90A HSPC1 HSPCA] Heat shock protein HSP 90-alpha (Heat shock 86 kDa) (HSP 86) (HSP86) (Lipopolysaccharide-associated protein 2) (LAP-2) (LPS-associated protein 2) (Renal carcinoma antigen NY-REN-38)
[MAPKAPK5 PRAK] MAP kinase-activated protein kinase 5 (MAPK-activated protein kinase 5) (MAPKAP kinase 5) (MAPKAP-K5) (MAPKAPK-5) (MK-5) (MK5) (EC 2.7.11.1) (p38-regulated/activated protein kinase) (PRAK)
[PA2G4 EBP1] Proliferation-associated protein 2G4 (Cell cycle protein p38-2G4 homolog) (hG4-1) (ErbB3-binding protein 1)
[MAPK14 CSBP1] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha) (Stress-activated protein kinase 2a)

Bibliography :
No related Items