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Signal peptide peptidase-like 2B (SPP-like 2B) (SPPL2b) (EC 3.4.23.-) (Intramembrane protease 4) (IMP-4) (Presenilin homologous protein 4) (PSH4) (Presenilin-like protein 1)

 SPP2B_HUMAN             Reviewed;         592 AA.
Q8TCT7; D6W609; O60365; Q567S3; Q8IUH9; Q9BUY6; Q9H3M4; Q9NPN2;
Q9P1Z6;
08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
16-MAY-2006, sequence version 2.
25-OCT-2017, entry version 144.
RecName: Full=Signal peptide peptidase-like 2B {ECO:0000303|PubMed:15385547, ECO:0000312|HGNC:HGNC:30627};
Short=SPP-like 2B {ECO:0000303|PubMed:15385547};
Short=SPPL2b {ECO:0000303|PubMed:15385547};
EC=3.4.23.-;
AltName: Full=Intramembrane protease 4 {ECO:0000303|PubMed:12139484};
Short=IMP-4 {ECO:0000303|PubMed:12139484};
AltName: Full=Presenilin homologous protein 4;
Short=PSH4;
AltName: Full=Presenilin-like protein 1;
Flags: Precursor;
Name=SPPL2B {ECO:0000303|PubMed:15385547,
ECO:0000312|HGNC:HGNC:30627};
Synonyms=IMP4 {ECO:0000303|PubMed:12139484}, KIAA1532, PSL1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Irmler M., Tomiuk S., Korner M.R., Hofmann K., Conradt M.;
"Characterization of a new protein family with homology to
presenilins.";
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Martoglio B.;
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Blood;
PubMed=12139484; DOI=10.1023/A:1016365227942;
Grigorenko A.P., Moliaka Y.K., Korovaitseva G.I., Rogaev E.I.;
"Novel class of polytopic proteins with domains associated with
putative protease activity.";
Biochemistry (Mosc.) 67:826-834(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10819331; DOI=10.1093/dnares/7.2.143;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:143-150(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
TISSUE=Brain, Eye, and Testis;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 201-279 (ISOFORM 1).
The European IMAGE consortium;
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[9]
GLYCOSYLATION, TOPOLOGY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15385547; DOI=10.1074/jbc.M407898200;
Friedmann E., Lemberg M.K., Weihofen A., Dev K.K., Dengler U.,
Rovelli G., Martoglio B.;
"Consensus analysis of signal peptide peptidase and homologous human
aspartic proteases reveals opposite topology of catalytic domains
compared with presenilins.";
J. Biol. Chem. 279:50790-50798(2004).
[10]
SUBUNIT, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
PubMed=15998642; DOI=10.1074/jbc.M501645200;
Krawitz P., Haffner C., Fluhrer R., Steiner H., Schmid B., Haass C.;
"Differential localization and identification of a critical aspartate
suggest non-redundant proteolytic functions of the presenilin
homologues SPPL2b and SPPL3.";
J. Biol. Chem. 280:39515-39523(2005).
[11]
SUBUNIT.
PubMed=16873890; DOI=10.1096/fj.06-5762com;
Nyborg A.C., Ladd T.B., Jansen K., Kukar T., Golde T.E.;
"Intramembrane proteolytic cleavage by human signal peptide peptidase
like 3 and malaria signal peptide peptidase.";
FASEB J. 20:1671-1679(2006).
[12]
FUNCTION IN CLEAVAGE OF TNF, AND SUBCELLULAR LOCATION.
PubMed=16829952; DOI=10.1038/ncb1440;
Friedmann E., Hauben E., Maylandt K., Schleeger S., Vreugde S.,
Lichtenthaler S.F., Kuhn P.H., Stauffer D., Rovelli G., Martoglio B.;
"SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in
activated dendritic cells to trigger IL-12 production.";
Nat. Cell Biol. 8:843-848(2006).
[13]
FUNCTION IN CLEAVAGE OF TNF, INTERACTION WITH TNF, AND MUTAGENESIS OF
ASP-421.
PubMed=16829951; DOI=10.1038/ncb1450;
Fluhrer R., Grammer G., Israel L., Condron M.M., Haffner C.,
Friedmann E., Bohland C., Imhof A., Martoglio B., Teplow D.B.,
Haass C.;
"A gamma-secretase-like intramembrane cleavage of TNFalpha by the GxGD
aspartyl protease SPPL2b.";
Nat. Cell Biol. 8:894-896(2006).
[14]
FUNCTION IN CLEAVAGE OF ITM2B, SUBCELLULAR LOCATION, INTERACTION WITH
ITM2B, AND MUTAGENESIS OF ASP-421.
PubMed=17965014; DOI=10.1074/jbc.M706661200;
Martin L., Fluhrer R., Reiss K., Kremmer E., Saftig P., Haass C.;
"Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and
SPPL2a/SPPL2b.";
J. Biol. Chem. 283:1644-1652(2008).
[15]
FUNCTION IN CLEAVAGE OF ITM2B, AND MUTAGENESIS OF ASP-421.
PubMed=19114711; DOI=10.1074/jbc.M807485200;
Martin L., Fluhrer R., Haass C.;
"Substrate requirements for SPPL2b-dependent regulated intramembrane
proteolysis.";
J. Biol. Chem. 284:5662-5670(2009).
[16]
FUNCTION IN CLEAVAGE OF ITM2B, AND MUTAGENESIS OF ASP-421.
PubMed=22194595; DOI=10.1074/jbc.M111.328104;
Fluhrer R., Martin L., Klier B., Haug-Kroper M., Grammer G.,
Nuscher B., Haass C.;
"The alpha-helical content of the transmembrane domain of the British
dementia protein-2 (Bri2) determines its processing by signal peptide
peptidase-like 2b (SPPL2b).";
J. Biol. Chem. 287:5156-5163(2012).
[17]
FUNCTION, INTERACTION WITH SIMIAN FOAMY VIRUS ENVELOPE GLYCOPROTEIN
GP130, AND MUTAGENESIS OF ASP-421.
PubMed=23132852; DOI=10.1074/jbc.M112.371369;
Voss M., Fukumori A., Kuhn P.H., Kunzel U., Klier B., Grammer G.,
Haug-Kroper M., Kremmer E., Lichtenthaler S.F., Steiner H.,
Schroder B., Haass C., Fluhrer R.;
"Foamy virus envelope protein is a substrate for signal peptide
peptidase-like 3 (SPPL3).";
J. Biol. Chem. 287:43401-43409(2012).
-!- FUNCTION: Intramembrane-cleaving aspartic protease (I-CLiP) that
cleaves type II membrane signal peptides in the hydrophobic plane
of the membrane. Functions in ITM2B and TNF processing
(PubMed:16829952, PubMed:16829951, PubMed:17965014,
PubMed:19114711, PubMed:22194595). Catalyzes the intramembrane
cleavage of the anchored fragment of shed TNF-alpha (TNF), which
promotes the release of the intracellular domain (ICD) for
signaling to the nucleus (PubMed:16829952, PubMed:16829951). May
play a role in the regulation of innate and adaptive immunity
(PubMed:16829952). Catalyzes the intramembrane cleavage of the
simian foamy virus processed leader peptide gp18 of the envelope
glycoprotein gp130 dependently of prior ectodomain shedding by
furin or furin-like proprotein convertase (PC)-mediated cleavage
proteolysis (PubMed:23132852). {ECO:0000269|PubMed:16829951,
ECO:0000269|PubMed:16829952, ECO:0000269|PubMed:17965014,
ECO:0000269|PubMed:19114711, ECO:0000269|PubMed:22194595,
ECO:0000269|PubMed:23132852}.
-!- SUBUNIT: Monomer (PubMed:15998642, PubMed:16873890). Homodimer
(PubMed:15998642, PubMed:16873890). Interacts with ITM2B
(PubMed:17965014). Interacts with TNF (PubMed:16829951). Interacts
with the simian foamy virus envelope glycoprotein gp130 and its
processed leader peptide gp18LP; preferentially interacts with the
leader peptide gp18LP (PubMed:23132852).
{ECO:0000269|PubMed:15998642, ECO:0000269|PubMed:16829951,
ECO:0000269|PubMed:16873890, ECO:0000269|PubMed:17965014,
ECO:0000269|PubMed:23132852}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16829952};
Multi-pass membrane protein {ECO:0000305}. Golgi apparatus
membrane {ECO:0000269|PubMed:17965014}; Multi-pass membrane
protein {ECO:0000305}. Lysosome membrane
{ECO:0000269|PubMed:15998642}; Multi-pass membrane protein
{ECO:0000305}. Endosome membrane {ECO:0000269|PubMed:15998642};
Multi-pass membrane protein {ECO:0000305}. Membrane
{ECO:0000269|PubMed:15385547}; Multi-pass membrane protein
{ECO:0000305}; Lumenal side {ECO:0000269|PubMed:15385547}.
Note=targeted through the entire secretory pathway to
endosomes/lysosomes (PubMed:15998642).
{ECO:0000269|PubMed:15998642}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Experimental confirmation may be lacking for some
isoforms.;
Name=1;
IsoId=Q8TCT7-1; Sequence=Displayed;
Name=2;
IsoId=Q8TCT7-2; Sequence=VSP_005204;
Name=4;
IsoId=Q8TCT7-4; Sequence=VSP_009221, VSP_009222;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed predominantly in adrenal cortex and
mammary gland. {ECO:0000269|PubMed:15385547}.
-!- DOMAIN: The PAL motif is required for normal active site
conformation. The catalytic domains embedded in the membrane are
in the opposite orientation to that of the presenilin protein
family; therefore, it is predicted to cleave type II-oriented
substrate peptides like the prototypic protease SPP.
{ECO:0000250|UniProtKB:P49768}.
-!- PTM: Glycosylated (PubMed:15385547, PubMed:15998642).
{ECO:0000269|PubMed:15385547, ECO:0000269|PubMed:15998642}.
-!- SIMILARITY: Belongs to the peptidase A22B family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC05601.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAG45441.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAA96056.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAB96951.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
Sequence=CAB96951.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AJ345027; CAC87788.1; -; mRNA.
EMBL; AJ420897; CAD13134.1; -; mRNA.
EMBL; AY169315; AAO12540.1; -; mRNA.
EMBL; AB040965; BAA96056.1; ALT_INIT; mRNA.
EMBL; AC004410; AAC05601.1; ALT_SEQ; Genomic_DNA.
EMBL; AC005258; AAG45441.1; ALT_INIT; Genomic_DNA.
EMBL; CH471139; EAW69383.1; -; Genomic_DNA.
EMBL; CH471139; EAW69388.1; -; Genomic_DNA.
EMBL; BC001788; AAH01788.2; -; mRNA.
EMBL; BC028391; AAH28391.2; -; mRNA.
EMBL; BC093046; AAH93046.1; -; mRNA.
EMBL; AL365405; CAB96951.1; ALT_SEQ; mRNA.
CCDS; CCDS74252.1; -. [Q8TCT7-1]
CCDS; CCDS74253.1; -. [Q8TCT7-4]
RefSeq; NP_001070706.1; NM_001077238.1. [Q8TCT7-4]
RefSeq; NP_694533.1; NM_152988.2. [Q8TCT7-1]
UniGene; Hs.744026; -.
ProteinModelPortal; Q8TCT7; -.
BioGrid; 121255; 126.
IntAct; Q8TCT7; 3.
MEROPS; A22.004; -.
iPTMnet; Q8TCT7; -.
PhosphoSitePlus; Q8TCT7; -.
BioMuta; SPPL2B; -.
DMDM; 97537015; -.
EPD; Q8TCT7; -.
MaxQB; Q8TCT7; -.
PeptideAtlas; Q8TCT7; -.
PRIDE; Q8TCT7; -.
TopDownProteomics; Q8TCT7-4; -. [Q8TCT7-4]
DNASU; 56928; -.
Ensembl; ENST00000610743; ENSP00000478510; ENSG00000005206. [Q8TCT7-4]
Ensembl; ENST00000613503; ENSP00000478298; ENSG00000005206. [Q8TCT7-1]
Ensembl; ENST00000618220; ENSP00000480813; ENSG00000005206. [Q8TCT7-2]
GeneID; 56928; -.
KEGG; hsa:56928; -.
UCSC; uc032hjm.2; human. [Q8TCT7-1]
CTD; 56928; -.
DisGeNET; 56928; -.
EuPathDB; HostDB:ENSG00000005206.16; -.
GeneCards; SPPL2B; -.
H-InvDB; HIX0158528; -.
HGNC; HGNC:30627; SPPL2B.
HPA; HPA039292; -.
MIM; 608239; gene.
neXtProt; NX_Q8TCT7; -.
OpenTargets; ENSG00000005206; -.
GeneTree; ENSGT00530000062920; -.
HOVERGEN; HBG024193; -.
InParanoid; Q8TCT7; -.
KO; K09597; -.
OMA; FSNQIPL; -.
OrthoDB; EOG091G05NG; -.
PhylomeDB; Q8TCT7; -.
Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
ChiTaRS; SPPL2B; human.
GeneWiki; SPPL2B; -.
GenomeRNAi; 56928; -.
PRO; PR:Q8TCT7; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000005206; -.
ExpressionAtlas; Q8TCT7; baseline and differential.
Genevisible; Q8TCT7; HS.
GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
GO; GO:0005813; C:centrosome; IDA:HPA.
GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0030660; C:Golgi-associated vesicle membrane; IDA:UniProtKB.
GO; GO:0071458; C:integral component of cytoplasmic side of endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0006509; P:membrane protein ectodomain proteolysis; IDA:UniProtKB.
GO; GO:0031293; P:membrane protein intracellular domain proteolysis; IDA:UniProtKB.
GO; GO:0033619; P:membrane protein proteolysis; IDA:UniProtKB.
GO; GO:0050776; P:regulation of immune response; IMP:UniProtKB.
GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
InterPro; IPR003137; PA_domain.
InterPro; IPR007369; Peptidase_A22B_SPP.
InterPro; IPR006639; Preselin/SPP.
InterPro; IPR033149; SPPL2B.
PANTHER; PTHR12174; PTHR12174; 1.
PANTHER; PTHR12174:SF39; PTHR12174:SF39; 1.
Pfam; PF02225; PA; 1.
Pfam; PF04258; Peptidase_A22B; 1.
SMART; SM00730; PSN; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Endosome;
Glycoprotein; Golgi apparatus; Hydrolase; Lysosome; Membrane;
Polymorphism; Protease; Reference proteome; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 25 {ECO:0000269|PubMed:15385547}.
CHAIN 26 592 Signal peptide peptidase-like 2B.
/FTId=PRO_0000073909.
TOPO_DOM 26 174 Lumenal. {ECO:0000269|PubMed:15385547}.
TRANSMEM 175 195 Helical. {ECO:0000255}.
TOPO_DOM 196 221 Cytoplasmic. {ECO:0000255}.
TRANSMEM 222 244 Helical. {ECO:0000255}.
TOPO_DOM 245 248 Lumenal. {ECO:0000255}.
TRANSMEM 249 271 Helical. {ECO:0000255}.
TOPO_DOM 272 293 Cytoplasmic. {ECO:0000255}.
TRANSMEM 294 314 Helical. {ECO:0000255}.
TOPO_DOM 315 319 Lumenal. {ECO:0000255}.
TRANSMEM 320 340 Helical. {ECO:0000255}.
TOPO_DOM 341 348 Cytoplasmic. {ECO:0000255}.
TRANSMEM 349 369 Helical. {ECO:0000255}.
TOPO_DOM 370 412 Lumenal. {ECO:0000269|PubMed:15385547}.
TRANSMEM 413 433 Helical. {ECO:0000255}.
TOPO_DOM 434 445 Cytoplasmic. {ECO:0000255}.
TRANSMEM 446 466 Helical. {ECO:0000255}.
TOPO_DOM 467 470 Lumenal. {ECO:0000255}.
TRANSMEM 471 491 Helical. {ECO:0000255}.
TOPO_DOM 492 592 Cytoplasmic.
{ECO:0000269|PubMed:15385547}.
DOMAIN 71 149 PA.
MOTIF 472 474 PAL.
COMPBIAS 350 357 Poly-Leu.
COMPBIAS 509 551 Pro-rich.
ACT_SITE 359 359 {ECO:0000250|UniProtKB:P49810}.
ACT_SITE 421 421 {ECO:0000250|UniProtKB:P49810}.
CARBOHYD 97 97 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 129 129 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 320 592 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_005204.
VAR_SEQ 506 511 KVLPPS -> VNTSLL (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_009221.
VAR_SEQ 512 592 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_009222.
VARIANT 574 574 S -> P (in dbSNP:rs10402284).
/FTId=VAR_059780.
MUTAGEN 421 421 D->A: Loss of intramembrane-cleaving
activity toward ITM2B, TNF and the simian
foamy virus envelope glycoprotein gp130.
{ECO:0000269|PubMed:16829951,
ECO:0000269|PubMed:17965014,
ECO:0000269|PubMed:19114711,
ECO:0000269|PubMed:22194595}.
SEQUENCE 592 AA; 64644 MW; 0F49370F16D36AA0 CRC64;
MAAAVAAALA RLLAAFLLLA AQVACEYGMV HVVSQAGGPE GKDYCILYNP QWAHLPHDLS
KASFLQLRNW TASLLCSAAD LPARGFSNQI PLVARGNCTF YEKVRLAQGS GARGLLIVSR
ERLVPPGGNK TQYDEIGIPV ALLSYKDMLD IFTRFGRTVR AALYAPKEPV LDYNMVIIFI
MAVGTVAIGG YWAGSRDVKK RYMKHKRDDG PEKQEDEAVD VTPVMTCVFV VMCCSMLVLL
YYFYDLLVYV VIGIFCLASA TGLYSCLAPC VRRLPFGKCR IPNNSLPYFH KRPQARMLLL
ALFCVAVSVV WGVFRNEDQW AWVLQDALGI AFCLYMLKTI RLPTFKACTL LLLVLFLYDI
FFVFITPFLT KSGSSIMVEV ATGPSDSATR EKLPMVLKVP RLNSSPLALC DRPFSLLGFG
DILVPGLLVA YCHRFDIQVQ SSRVYFVACT IAYGVGLLVT FVALALMQRG QPALLYLVPC
TLVTSCAVAL WRRELGVFWT GSGFAKVLPP SPWAPAPADG PQPPKDSATP LSPQPPSEEP
ATSPWPAEQS PKSRTSEEMG AGAPMREPGS PAESEGRDQA QPSPVTQPGA SA


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EIAAB32832 Rat,Rattus norvegicus,Signal peptide peptidase-like 2B,SPPL2b,Sppl2b,SPP-like 2B
EIAAB32834 Chicken,Gallus gallus,RCJMB04_29c5,Signal peptide peptidase-like 2B,SPPL2b,SPPL2B,SPP-like 2B
18-783-75579 RABBIT ANTI HUMAN PEN2 (N-TERMINAL) - PRESENILIN ENHANCER PROTEIN 2; Presenilin enhancer protein 2 Polyclonal 0.1 mg
18-783-75578 RABBIT ANTI HUMAN PEN2 (C-TERMINAL) - PRESENILIN ENHANCER PROTEIN 2; Presenilin enhancer protein 2 Polyclonal 0.1 mg
GWB-BAB23A Anti- SPPL2B (signal peptide peptidase-like 2B) Antibody
AP6311a Signal peptide peptidase-like 2B (SPPL2b) Antibody (N-term)
PSL1_RAT ELISA Kit FOR Signal peptide peptidase-like 2B; organism: Rat; gene name: Sppl2b 96T
PSL1_MOUSE ELISA Kit FOR Signal peptide peptidase-like 2B; organism: Mouse; gene name: Sppl2b 96T
AP6311a Signal peptide peptidase-like 2B (SPPL2b) Antibody (N-term) Purified Rabbit Polyclonal Antibody (Pab) Applications WB, E 0.1 mg
orb72134 Presenilin 1 peptide This is Presenilin 1 peptide. For research use only. 1 mg
LF-PA50211 anti-Presenilin 2, Rabbit polyclonal to Presenilin 2, Isotype IgG, Host Rabbit 200 ul
20-272-190981 Presenilin 2 - Mouse monoclonal [198C679.2.1] to Presenilin 2 Monoclonal 0.2 ml
AS10 1614 Antibody: SppA1 | signal peptide peptidase (cyanobacterial) (200 ul), Immunogen: synthetic peptide (amino acids 305 - 320) specific for SppA1 protease from Synechocystis sp. PCC 6803, P73689, Hos 200 ul
EIAAB11657 Dedicator of cytokinesis protein 3,Dock3,Moca,Modifier of cell adhesion,Mouse,Mus musculus,PBP,Presenilin-binding protein
4761 Presenilin-associated rhomboid-like protein 0.1 mg
4761 Presenilin-associated rhomboid-like protein 0.5 mg
EIAAB30547 Gamma-secretase subunit PEN-2,Liver regeneration-related protein LRRGT00140,Presenilin enhancer protein 2,Psenen,Rat,Rattus norvegicus
LF-PA40949 anti-Presenilin 1 (PSEN1) , Rabbit polyclonal to Presenilin 1 (PSEN1) , Isotype IgG, Host Rabbit 50 ug
LF-PA42514 Anti-Presenilin (PSEN1_PSEN2), Rabbit Polyclonal to Presenilin (PSEN1_PSEN2), Isotype , Host Rabbit 50


 

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