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Signal peptide peptidase-like 2A (SPP-like 2A) (SPPL2a) (EC 3.4.23.-) (Intramembrane protease 3) (IMP-3) (Presenilin-like protein 2)

 SPP2A_HUMAN             Reviewed;         520 AA.
Q8TCT8; B2RDS0; Q8TAW1; Q96SZ8;
08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
08-NOV-2002, sequence version 2.
25-OCT-2017, entry version 135.
RecName: Full=Signal peptide peptidase-like 2A {ECO:0000303|PubMed:15385547, ECO:0000312|HGNC:HGNC:30227};
Short=SPP-like 2A {ECO:0000303|PubMed:15385547};
Short=SPPL2a {ECO:0000303|PubMed:15385547};
EC=3.4.23.-;
AltName: Full=Intramembrane protease 3 {ECO:0000303|PubMed:12139484};
Short=IMP-3 {ECO:0000303|PubMed:12139484};
AltName: Full=Presenilin-like protein 2;
Flags: Precursor;
Name=SPPL2A {ECO:0000303|PubMed:15385547,
ECO:0000312|HGNC:HGNC:30227};
Synonyms=IMP3 {ECO:0000303|PubMed:12139484}, PSL2; ORFNames=PSEC0147;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
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].
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Synovium, and Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 91-520.
TISSUE=Cervix carcinoma;
PubMed=12077416; DOI=10.1126/science.1070925;
Weihofen A., Binns K., Lemberg M.K., Ashman K., Martoglio B.;
"Identification of signal peptide peptidase, a presenilin-type
aspartic protease.";
Science 296:2215-2218(2002).
[8]
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).
[9]
FUNCTION IN CLEAVAGE OF TNF, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
ASP-412.
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).
[10]
FUNCTION IN CLEAVAGE OF TNF.
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).
[11]
FUNCTION IN CLEAVAGE OF FASLG, AND MUTAGENESIS OF ASP-412.
PubMed=17557115; DOI=10.1038/sj.cdd.4402175;
Kirkin V., Cahuzac N., Guardiola-Serrano F., Huault S., Luckerath K.,
Friedmann E., Novac N., Wels W.S., Martoglio B., Hueber A.O.,
Zornig M.;
"The Fas ligand intracellular domain is released by ADAM10 and SPPL2a
cleavage in T-cells.";
Cell Death Differ. 14:1678-1687(2007).
[12]
FUNCTION IN CLEAVAGE OF ITM2B, INTERACTION WITH ITM2B, AND MUTAGENESIS
OF ASP-412.
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).
[13]
GLYCOSYLATION AT ASN-155.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[14]
FUNCTION, AND MUTAGENESIS OF ASP-412.
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 FASLG, ITM2B and TNF processing
(PubMed:16829952, PubMed:16829951, PubMed:17557115,
PubMed:17965014). 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). Also responsible for the intramembrane
cleavage of Fas antigen ligand FASLG, which promotes the release
of the intracellular FasL domain (FasL ICD) (PubMed:17557115). May
play a role in the regulation of innate and adaptive immunity
(PubMed:16829952). Catalyzes the intramembrane cleavage of the
simian foamy virus envelope glycoprotein gp130 independently 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:17557115, ECO:0000269|PubMed:17965014,
ECO:0000269|PubMed:23132852}.
-!- SUBUNIT: Interacts with ITM2B (PubMed:17965014).
{ECO:0000269|PubMed:17965014}.
-!- INTERACTION:
O43765:SGTA; NbExp=6; IntAct=EBI-750784, EBI-347996;
-!- SUBCELLULAR LOCATION: Late endosome membrane
{ECO:0000269|PubMed:16829952}; Multi-pass membrane protein
{ECO:0000305}. Lysosome membrane {ECO:0000250|UniProtKB:Q9JJF9};
Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9JJF9}.
Membrane {ECO:0000269|PubMed:15385547}; Multi-pass membrane
protein {ECO:0000305}; Lumenal side {ECO:0000269|PubMed:15385547}.
Note=Colocalizes with palmitoylated and myristoylated proteins at
the plasma membrane.
-!- TISSUE SPECIFICITY: Ubiquitous. {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. The C-
terminal tail is necessary for lysosomal transport.
{ECO:0000250|UniProtKB:P49768, ECO:0000250|UniProtKB:Q9JJF9}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:15385547,
ECO:0000269|PubMed:19139490}.
-!- SIMILARITY: Belongs to the peptidase A22B family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB55117.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAD13133.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AJ345028; CAC87789.1; -; mRNA.
EMBL; AY169314; AAO12539.1; -; mRNA.
EMBL; AK027446; BAB55117.1; ALT_INIT; mRNA.
EMBL; AK315651; BAG38017.1; -; mRNA.
EMBL; AK075454; BAC11630.1; -; mRNA.
EMBL; CH471082; EAW77410.1; -; Genomic_DNA.
EMBL; BC025740; AAH25740.1; -; mRNA.
EMBL; AJ420896; CAD13133.1; ALT_INIT; mRNA.
CCDS; CCDS10138.1; -.
RefSeq; NP_116191.2; NM_032802.3.
UniGene; Hs.401537; -.
ProteinModelPortal; Q8TCT8; -.
BioGrid; 124328; 3.
IntAct; Q8TCT8; 4.
MINT; MINT-1465822; -.
STRING; 9606.ENSP00000261854; -.
MEROPS; A22.007; -.
TCDB; 1.A.54.3.2; the presenilin er ca(2+) leak channel (presenilin) family.
iPTMnet; Q8TCT8; -.
PhosphoSitePlus; Q8TCT8; -.
SwissPalm; Q8TCT8; -.
BioMuta; SPPL2A; -.
DMDM; 25008981; -.
EPD; Q8TCT8; -.
MaxQB; Q8TCT8; -.
PaxDb; Q8TCT8; -.
PeptideAtlas; Q8TCT8; -.
PRIDE; Q8TCT8; -.
DNASU; 84888; -.
Ensembl; ENST00000261854; ENSP00000261854; ENSG00000138600.
GeneID; 84888; -.
KEGG; hsa:84888; -.
UCSC; uc001zyv.4; human.
CTD; 84888; -.
DisGeNET; 84888; -.
EuPathDB; HostDB:ENSG00000138600.9; -.
GeneCards; SPPL2A; -.
HGNC; HGNC:30227; SPPL2A.
HPA; HPA036062; -.
HPA; HPA067304; -.
MIM; 608238; gene.
neXtProt; NX_Q8TCT8; -.
OpenTargets; ENSG00000138600; -.
eggNOG; KOG2442; Eukaryota.
eggNOG; ENOG410ZP52; LUCA.
GeneTree; ENSGT00530000062920; -.
HOGENOM; HOG000231496; -.
HOVERGEN; HBG024193; -.
InParanoid; Q8TCT8; -.
KO; K09596; -.
OMA; KKFWKGS; -.
OrthoDB; EOG091G05NG; -.
PhylomeDB; Q8TCT8; -.
TreeFam; TF319186; -.
Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
GeneWiki; SPPL2A; -.
GenomeRNAi; 84888; -.
PRO; PR:Q8TCT8; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000138600; -.
ExpressionAtlas; Q8TCT8; baseline and differential.
Genevisible; Q8TCT8; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
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:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005770; C:late endosome; IDA:UniProtKB.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
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; IPR033151; SPPL2a.
PANTHER; PTHR12174; PTHR12174; 1.
PANTHER; PTHR12174:SF34; PTHR12174:SF34; 1.
Pfam; PF02225; PA; 1.
Pfam; PF04258; Peptidase_A22B; 1.
SMART; SM00730; PSN; 1.
1: Evidence at protein level;
Complete proteome; Endosome; Glycoprotein; Hydrolase; Lysosome;
Membrane; Polymorphism; Protease; Reference proteome; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 25 {ECO:0000269|PubMed:15385547}.
CHAIN 26 520 Signal peptide peptidase-like 2A.
/FTId=PRO_0000073910.
TOPO_DOM 26 172 Lumenal. {ECO:0000269|PubMed:15385547}.
TRANSMEM 173 193 Helical. {ECO:0000255}.
TOPO_DOM 194 220 Cytoplasmic. {ECO:0000255}.
TRANSMEM 221 241 Helical. {ECO:0000255}.
TOPO_DOM 242 247 Lumenal. {ECO:0000255}.
TRANSMEM 248 268 Helical. {ECO:0000255}.
TOPO_DOM 269 285 Cytoplasmic. {ECO:0000255}.
TRANSMEM 286 306 Helical. {ECO:0000255}.
TOPO_DOM 307 311 Lumenal. {ECO:0000255}.
TRANSMEM 312 332 Helical. {ECO:0000255}.
TOPO_DOM 333 340 Cytoplasmic. {ECO:0000255}.
TRANSMEM 341 361 Helical. {ECO:0000255}.
TOPO_DOM 362 399 Lumenal. {ECO:0000269|PubMed:15385547}.
TRANSMEM 400 420 Helical. {ECO:0000255}.
TOPO_DOM 421 437 Cytoplasmic. {ECO:0000255}.
TRANSMEM 438 458 Helical. {ECO:0000255}.
TOPO_DOM 459 460 Lumenal. {ECO:0000255}.
TRANSMEM 461 481 Helical. {ECO:0000255}.
TOPO_DOM 482 520 Cytoplasmic.
{ECO:0000269|PubMed:15385547}.
DOMAIN 63 151 PA.
MOTIF 463 465 PAL.
MOTIF 495 498 YXXo lysosomal targeting motif.
ACT_SITE 351 351 {ECO:0000250|UniProtKB:P49810}.
ACT_SITE 412 412 {ECO:0000250|UniProtKB:P49810}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 66 66 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 126 126 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 149 149 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 155 155 N-linked (GlcNAc...) (complex)
asparagine.
{ECO:0000269|PubMed:19139490}.
VARIANT 90 90 V -> I (in dbSNP:rs8034443).
/FTId=VAR_051790.
MUTAGEN 412 412 D->A: Loss of intramembrane-cleaving
activity toward FASLG, ITM2B, TNF and the
simian foamy virus envelope glycoprotein
gp130. {ECO:0000269|PubMed:16829952,
ECO:0000269|PubMed:17557115,
ECO:0000269|PubMed:17965014,
ECO:0000269|PubMed:23132852}.
CONFLICT 126 126 N -> D (in Ref. 3; BAB55117).
{ECO:0000305}.
CONFLICT 271 271 I -> T (in Ref. 4; BAC11630).
{ECO:0000305}.
CONFLICT 406 406 S -> L (in Ref. 4; BAC11630).
{ECO:0000305}.
CONFLICT 446 446 I -> F (in Ref. 4; BAC11630).
{ECO:0000305}.
CONFLICT 511 511 V -> E (in Ref. 3; BAB55117).
{ECO:0000305}.
SEQUENCE 520 AA; 58143 MW; A7A933A6504507DC CRC64;
MGPQRRLSPA GAALLWGFLL QLTAAQEAIL HASGNGTTKD YCMLYNPYWT ALPSTLENAT
SISLMNLTST PLCNLSDIPP VGIKSKAVVV PWGSCHFLEK ARIAQKGGAE AMLVVNNSVL
FPPSGNRSEF PDVKILIAFI SYKDFRDMNQ TLGDNITVKM YSPSWPNFDY TMVVIFVIAV
FTVALGGYWS GLVELENLKA VTTEDREMRK KKEEYLTFSP LTVVIFVVIC CVMMVLLYFF
YKWLVYVMIA IFCIASAMSL YNCLAALIHK IPYGQCTIAC RGKNMEVRLI FLSGLCIAVA
VVWAVFRNED RWAWILQDIL GIAFCLNLIK TLKLPNFKSC VILLGLLLLY DVFFVFITPF
ITKNGESIMV ELAAGPFGNN EKLPVVIRVP KLIYFSVMSV CLMPVSILGF GDIIVPGLLI
AYCRRFDVQT GSSYIYYVSS TVAYAIGMIL TFVVLVLMKK GQPALLYLVP CTLITASVVA
WRRKEMKKFW KGNSYQMMDH LDCATNEENP VISGEQIVQQ


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AS10 1613 Antibody: SppA1 | signal peptide peptidase (higher plants) (100 ul), Immunogen: recombinant SppA1 protease from Arabidopsis thaliana, NP_565077.2, Host: rabbit, polyclonal, Confirmed reactivity: Ar 100 ul
201-20-2787 IMP5{intramembrane protease 5}rabbit.pAb 0.2ml
EIAAB37376 Endopeptidase SP18,Microsomal signal peptidase 18 kDa subunit,Rat,Rattus norvegicus,SEC11 homolog A,Sec11a,Sec11l1,SEC11-like protein 1,Signal peptidase complex catalytic subunit SEC11A,SPase 18 kDa s
EIAAB37375 Endopeptidase SP18,Microsomal signal peptidase 18 kDa subunit,Mouse,Mus musculus,SEC11 homolog A,Sec11a,Sec11l1,SEC11-like protein 1,Sid 2895,Sid2895,Signal peptidase complex catalytic subunit SEC11A,
EIAAB37373 Bos taurus,Bovine,Endopeptidase SP18,Microsomal signal peptidase 18 kDa subunit,SEC11 homolog A,SEC11A,SEC11L1,SEC11-like protein 1,Signal peptidase complex catalytic subunit SEC11A,SPase 18 kDa subun
EIAAB37372 Endopeptidase SP18,Homo sapiens,Human,Microsomal signal peptidase 18 kDa subunit,SEC11 homolog A,SEC11A,SEC11L1,SEC11-like protein 1,Signal peptidase complex catalytic subunit SEC11A,SPase 18 kDa subu
EIAAB37374 Canis familiaris,Canis lupus familiaris,Dog,Endopeptidase SP18,Microsomal signal peptidase 18 kDa subunit,SEC11 homolog A,SEC11A,SEC11L1,SEC11-like protein 1,Signal peptidase complex catalytic subunit
EIAAB29915 Mitochondrial intramembrane-cleaving protease PARL,Parl,Presenilins-associated rhomboid-like protein, mitochondrial,Psarl,Rat,Rattus norvegicus
EIAAB29913 Bos taurus,Bovine,Mitochondrial intramembrane cleaving protease PARL,PARL,Presenilins-associated rhomboid-like protein, mitochondrial,PSARL
EIAAB29916 Mitochondrial intramembrane-cleaving protease PARL,Mouse,Mus musculus,Parl,Presenilins-associated rhomboid-like protein, mitochondrial,Psarl
EIAAB29914 Homo sapiens,Human,Mitochondrial intramembrane cleaving protease PARL,PARL,Presenilins-associated rhomboid-like protein, mitochondrial,PRO2207,PSARL
EIAAB39462 Homo sapiens,Human,KIAA0102,Microsomal signal peptidase 25 kDa subunit,Signal peptidase complex subunit 2,SPase 25 kDa subunit,SPC25,SPCS2
EIAAB39460 Homo sapiens,HSPC033,Human,Microsomal signal peptidase 12 kDa subunit,Signal peptidase complex subunit 1,SPase 12 kDa subunit,SPC12,SPCS1
EIAAB37379 Homo sapiens,Human,Microsomal signal peptidase 21 kDa subunit,SEC11 homolog C,SEC11C,SEC11L3,SEC11-like protein 3,Signal peptidase complex catalytic subunit SEC11C,SPase 21 kDa subunit,SPC21,SPC21,SPC


 

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