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

Presequence protease 1, chloroplastic/mitochondrial (AtPreP1) (PreP 1) (EC 3.4.24.-) (Zinc metalloprotease 1) (AtZnMP1)

 PREP1_ARATH             Reviewed;        1080 AA.
Q9LJL3; Q8RUN6;
19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
19-SEP-2006, sequence version 2.
25-APR-2018, entry version 122.
RecName: Full=Presequence protease 1, chloroplastic/mitochondrial;
Short=AtPreP1;
Short=PreP 1;
EC=3.4.24.-;
AltName: Full=Zinc metalloprotease 1;
Short=AtZnMP1;
Flags: Precursor;
Name=PREP1; Synonyms=ZNMP1; OrderedLocusNames=At3g19170;
ORFNames=MVI11.6, MVI11.7, MVI11_8;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10907853; DOI=10.1093/dnares/7.3.217;
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 3. II.
Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC
and BAC clones.";
DNA Res. 7:217-221(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
PubMed=12138166; DOI=10.1074/jbc.M205500200;
Staahl A., Moberg P., Ytterberg J., Panfilov O.,
Brockenhuus Von Lowenhielm H., Nilsson F., Glaser E.;
"Isolation and identification of a novel mitochondrial metalloprotease
(PreP) that degrades targeting presequences in plants.";
J. Biol. Chem. 277:41931-41939(2002).
[5]
CHARACTERIZATION, MUTAGENESIS OF HIS-162; GLU-165; HIS-166; GLU-240
AND GLU-245, AND SUBCELLULAR LOCATION.
PubMed=14617063; DOI=10.1046/j.1365-313X.2003.01904.x;
Moberg P., Staahl A., Bhushan S., Wright S.J., Eriksson A.,
Bruce B.D., Glaser E.;
"Characterization of a novel zinc metalloprotease involved in
degrading targeting peptides in mitochondria and chloroplasts.";
Plant J. 36:616-628(2003).
[6]
CHARACTERIZATION, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE
SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=15827031; DOI=10.1093/pcp/pci107;
Bhushan S., Staahl A., Nilsson S., Lefebvre B., Seki M., Roth C.,
McWilliam D., Wright S.J., Liberles D.A., Shinozaki K., Bruce B.D.,
Boutry M., Glaser E.;
"Catalysis, subcellular localization, expression and evolution of the
targeting peptides degrading protease, AtPreP2.";
Plant Cell Physiol. 46:985-996(2005).
[7]
CLEAVAGE SPECIFICITY.
PubMed=15893767; DOI=10.1016/j.jmb.2005.04.023;
Staahl A., Nilsson S., Lundberg P., Bhushan S., Biverstaahl H.,
Moberg P., Morisset M., Vener A., Maeler L., Langel U., Glaser E.;
"Two novel targeting peptide degrading proteases, PrePs, in
mitochondria and chloroplasts, so similar and still different.";
J. Mol. Biol. 349:847-860(2005).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-86, CLEAVAGE OF TRANSIT
PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-85, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[9]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 86-1080, AND MUTAGENESIS OF
GLU-179; ASN-194; LYS-256; GLU-262; LYS-264; ALA-416; GLU-430;
ASN-700; SER-767; GLN-895; ARG-933; GLY-937 AND TYR-939.
PubMed=16601675; DOI=10.1038/sj.emboj.7601080;
Johnson K.A., Bhushan S., Staahl A., Hallberg B.M., Frohn A.,
Glaser E., Eneqvist T.;
"The closed structure of presequence protease PreP forms a unique
10,000 Angstroms3 chamber for proteolysis.";
EMBO J. 25:1977-1986(2006).
-!- FUNCTION: ATP-independent protease that degrades both
mitochondrial and chloroplastic transit peptides after their
cleavage. Also degrades other unstructured peptides. Specific for
peptides in the range of 10 to 65 residues. Shows a preference for
cleavage after small polar residues and before basic residues,
with a bias for positively charged amino acid residues.
{ECO:0000269|PubMed:12138166}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 1 zinc ion per subunit.;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Binds 2 Magnesium ions per subunit.;
-!- ENZYME REGULATION: Inactive in the absence of MgCl(2) and CaCl(2)
and full activation at 10 mM concentrations of either ion.
Completely inhibited by the metal chelator orthophenanthroline,
but not affected by phenylmethylsulfonyl fluoride (PMSF) or N-
ethylmaleimide (NEM).
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Active from pH 4 to 10.;
Temperature dependence:
Optimum temperature is 28 degrees Celsius. Active from 4 to 40
degrees Celsius.;
-!- SUBUNIT: Homodimer.
-!- INTERACTION:
P17614:ATPB (xeno); NbExp=6; IntAct=EBI-7143359, EBI-7143406;
-!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Mitochondrion
matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=Q9LJL3-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Expressed only in siliques and flowers.
{ECO:0000269|PubMed:15827031}.
-!- MISCELLANEOUS: The 2 enzymes halves enclose a large proteolytic
chamber spacious enough to hold peptide substrates, but
sufficiently small to exclude larger, folded proteins. Since the
active site includes residues from both the N- and C-terminal part
of the protein, proteolysis can occur only when the chamber is
closed. Covalently locking the 2 halves of the protease with
disulfide bonds induces a loss of activity.
-!- SIMILARITY: Belongs to the peptidase M16 family. PreP subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB02957.1; Type=Erroneous initiation; Evidence={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; AP000419; BAB02957.1; ALT_INIT; Genomic_DNA.
EMBL; CP002686; AEE76201.1; -; Genomic_DNA.
EMBL; AY090240; AAL90904.1; -; mRNA.
EMBL; AY091051; AAM13872.1; -; mRNA.
EMBL; BT006362; AAP21170.1; -; mRNA.
EMBL; BT002372; AAN86205.1; -; mRNA.
RefSeq; NP_188548.2; NM_112804.5. [Q9LJL3-1]
UniGene; At.27915; -.
PDB; 2FGE; X-ray; 2.10 A; A/B=86-1080.
PDBsum; 2FGE; -.
ProteinModelPortal; Q9LJL3; -.
SMR; Q9LJL3; -.
BioGrid; 6784; 1.
IntAct; Q9LJL3; 4.
MINT; Q9LJL3; -.
STRING; 3702.AT3G19170.1; -.
MEROPS; M16.012; -.
iPTMnet; Q9LJL3; -.
PaxDb; Q9LJL3; -.
PRIDE; Q9LJL3; -.
EnsemblPlants; AT3G19170.1; AT3G19170.1; AT3G19170. [Q9LJL3-1]
GeneID; 821451; -.
Gramene; AT3G19170.1; AT3G19170.1; AT3G19170. [Q9LJL3-1]
KEGG; ath:AT3G19170; -.
Araport; AT3G19170; -.
TAIR; locus:2094138; AT3G19170.
eggNOG; KOG2019; Eukaryota.
eggNOG; COG1026; LUCA.
HOGENOM; HOG000008829; -.
InParanoid; Q9LJL3; -.
KO; K06972; -.
OMA; FTYGNFP; -.
OrthoDB; EOG093600W5; -.
PhylomeDB; Q9LJL3; -.
Reactome; R-ATH-1268020; Mitochondrial protein import.
EvolutionaryTrace; Q9LJL3; -.
PRO; PR:Q9LJL3; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9LJL3; baseline and differential.
Genevisible; Q9LJL3; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IDA:TAIR.
GO; GO:0016485; P:protein processing; IDA:TAIR.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
InterPro; IPR011249; Metalloenz_LuxS/M16.
InterPro; IPR011765; Pept_M16_N.
InterPro; IPR007863; Peptidase_M16_C.
InterPro; IPR013578; Peptidase_M16C_assoc.
Pfam; PF08367; M16C_assoc; 1.
Pfam; PF00675; Peptidase_M16; 1.
Pfam; PF05193; Peptidase_M16_C; 1.
SMART; SM01264; M16C_associated; 1.
SUPFAM; SSF63411; SSF63411; 4.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Chloroplast;
Coiled coil; Complete proteome; Hydrolase; Magnesium; Metal-binding;
Metalloprotease; Mitochondrion; Plastid; Protease; Reference proteome;
Transit peptide; Zinc.
TRANSIT 1 85 Chloroplast and mitochondrion.
{ECO:0000244|PubMed:22223895}.
CHAIN 86 1080 Presequence protease 1,
chloroplastic/mitochondrial.
/FTId=PRO_0000249938.
COILED 571 612 {ECO:0000255}.
ACT_SITE 165 165 Proton acceptor.
{ECO:0000269|PubMed:16601675}.
ACT_SITE 240 240 {ECO:0000305}.
METAL 162 162 Zinc; catalytic.
{ECO:0000269|PubMed:16601675}.
METAL 166 166 Zinc; catalytic.
{ECO:0000269|PubMed:16601675}.
METAL 262 262 Zinc; catalytic.
{ECO:0000269|PubMed:16601675}.
MOD_RES 86 86 N-acetylvaline.
{ECO:0000244|PubMed:22223895}.
MUTAGEN 162 162 H->L: Loss of activity.
{ECO:0000269|PubMed:14617063}.
MUTAGEN 165 165 E->Q: Loss of activity.
{ECO:0000269|PubMed:14617063}.
MUTAGEN 166 166 H->L: Loss of activity.
{ECO:0000269|PubMed:14617063}.
MUTAGEN 179 179 E->Q: Decreased activity toward some
substrates.
{ECO:0000269|PubMed:16601675}.
MUTAGEN 194 194 N->A: Reduced activity.
{ECO:0000269|PubMed:16601675}.
MUTAGEN 240 240 E->Q: Decreased activity toward some
substrates.
{ECO:0000269|PubMed:14617063}.
MUTAGEN 245 245 E->Q: No loss of activity.
{ECO:0000269|PubMed:14617063}.
MUTAGEN 256 256 K->C: Inactive under oxidizing conditions
and fully active under reducing
conditions; when associated with C-937.
{ECO:0000269|PubMed:16601675}.
MUTAGEN 262 262 E->Q: Loss of activity.
{ECO:0000269|PubMed:16601675}.
MUTAGEN 264 264 K->C: Inactive under oxidizing conditions
and fully active under reducing
conditions; when associated with C-895.
{ECO:0000269|PubMed:16601675}.
MUTAGEN 416 416 A->C: Little or no effect; when
associated with C-700.
{ECO:0000269|PubMed:16601675}.
MUTAGEN 430 430 E->C: Inactive under oxidizing conditions
and fully active under reducing
conditions; when associated with C-767.
{ECO:0000269|PubMed:16601675}.
MUTAGEN 700 700 N->C: Little or no effect; when
associated with C-416.
{ECO:0000269|PubMed:16601675}.
MUTAGEN 767 767 S->C: Inactive under oxidizing conditions
and fully active under reducing
conditions; when associated with C-430.
{ECO:0000269|PubMed:16601675}.
MUTAGEN 895 895 Q->C: Inactive under oxidizing conditions
and fully active under reducing
conditions; when associated with C-264.
{ECO:0000269|PubMed:16601675}.
MUTAGEN 933 933 R->A,K: Loss of activity.
{ECO:0000269|PubMed:16601675}.
MUTAGEN 937 937 G->C: Inactive under oxidizing conditions
and fully active under reducing
conditions; when associated with C-256.
{ECO:0000269|PubMed:16601675}.
MUTAGEN 939 939 Y->F: Loss of activity.
{ECO:0000269|PubMed:16601675}.
HELIX 101 104 {ECO:0000244|PDB:2FGE}.
STRAND 107 115 {ECO:0000244|PDB:2FGE}.
TURN 116 119 {ECO:0000244|PDB:2FGE}.
STRAND 120 127 {ECO:0000244|PDB:2FGE}.
TURN 128 130 {ECO:0000244|PDB:2FGE}.
STRAND 133 138 {ECO:0000244|PDB:2FGE}.
STRAND 142 151 {ECO:0000244|PDB:2FGE}.
STRAND 155 158 {ECO:0000244|PDB:2FGE}.
HELIX 160 167 {ECO:0000244|PDB:2FGE}.
HELIX 180 187 {ECO:0000244|PDB:2FGE}.
STRAND 190 193 {ECO:0000244|PDB:2FGE}.
STRAND 199 210 {ECO:0000244|PDB:2FGE}.
HELIX 211 226 {ECO:0000244|PDB:2FGE}.
HELIX 229 231 {ECO:0000244|PDB:2FGE}.
HELIX 235 240 {ECO:0000244|PDB:2FGE}.
STRAND 243 245 {ECO:0000244|PDB:2FGE}.
STRAND 254 256 {ECO:0000244|PDB:2FGE}.
HELIX 258 266 {ECO:0000244|PDB:2FGE}.
HELIX 270 282 {ECO:0000244|PDB:2FGE}.
HELIX 287 289 {ECO:0000244|PDB:2FGE}.
TURN 296 298 {ECO:0000244|PDB:2FGE}.
HELIX 299 301 {ECO:0000244|PDB:2FGE}.
HELIX 304 314 {ECO:0000244|PDB:2FGE}.
HELIX 317 319 {ECO:0000244|PDB:2FGE}.
STRAND 320 328 {ECO:0000244|PDB:2FGE}.
HELIX 330 341 {ECO:0000244|PDB:2FGE}.
HELIX 349 352 {ECO:0000244|PDB:2FGE}.
STRAND 365 372 {ECO:0000244|PDB:2FGE}.
STRAND 375 377 {ECO:0000244|PDB:2FGE}.
HELIX 379 381 {ECO:0000244|PDB:2FGE}.
STRAND 383 390 {ECO:0000244|PDB:2FGE}.
HELIX 398 412 {ECO:0000244|PDB:2FGE}.
HELIX 418 425 {ECO:0000244|PDB:2FGE}.
STRAND 430 432 {ECO:0000244|PDB:2FGE}.
STRAND 436 438 {ECO:0000244|PDB:2FGE}.
STRAND 440 443 {ECO:0000244|PDB:2FGE}.
STRAND 445 453 {ECO:0000244|PDB:2FGE}.
HELIX 455 457 {ECO:0000244|PDB:2FGE}.
HELIX 458 475 {ECO:0000244|PDB:2FGE}.
HELIX 479 495 {ECO:0000244|PDB:2FGE}.
HELIX 503 515 {ECO:0000244|PDB:2FGE}.
TURN 516 518 {ECO:0000244|PDB:2FGE}.
HELIX 523 525 {ECO:0000244|PDB:2FGE}.
HELIX 528 541 {ECO:0000244|PDB:2FGE}.
HELIX 543 554 {ECO:0000244|PDB:2FGE}.
TURN 555 557 {ECO:0000244|PDB:2FGE}.
STRAND 561 569 {ECO:0000244|PDB:2FGE}.
HELIX 572 589 {ECO:0000244|PDB:2FGE}.
HELIX 593 610 {ECO:0000244|PDB:2FGE}.
HELIX 616 619 {ECO:0000244|PDB:2FGE}.
HELIX 627 629 {ECO:0000244|PDB:2FGE}.
STRAND 640 653 {ECO:0000244|PDB:2FGE}.
STRAND 657 667 {ECO:0000244|PDB:2FGE}.
TURN 673 675 {ECO:0000244|PDB:2FGE}.
HELIX 676 678 {ECO:0000244|PDB:2FGE}.
HELIX 679 688 {ECO:0000244|PDB:2FGE}.
STRAND 692 694 {ECO:0000244|PDB:2FGE}.
HELIX 696 706 {ECO:0000244|PDB:2FGE}.
STRAND 707 719 {ECO:0000244|PDB:2FGE}.
STRAND 722 736 {ECO:0000244|PDB:2FGE}.
HELIX 737 739 {ECO:0000244|PDB:2FGE}.
HELIX 740 753 {ECO:0000244|PDB:2FGE}.
HELIX 759 779 {ECO:0000244|PDB:2FGE}.
HELIX 781 791 {ECO:0000244|PDB:2FGE}.
HELIX 795 804 {ECO:0000244|PDB:2FGE}.
HELIX 806 821 {ECO:0000244|PDB:2FGE}.
HELIX 823 837 {ECO:0000244|PDB:2FGE}.
STRAND 844 849 {ECO:0000244|PDB:2FGE}.
HELIX 851 866 {ECO:0000244|PDB:2FGE}.
STRAND 888 891 {ECO:0000244|PDB:2FGE}.
STRAND 895 904 {ECO:0000244|PDB:2FGE}.
HELIX 905 908 {ECO:0000244|PDB:2FGE}.
HELIX 915 925 {ECO:0000244|PDB:2FGE}.
HELIX 927 931 {ECO:0000244|PDB:2FGE}.
TURN 932 936 {ECO:0000244|PDB:2FGE}.
STRAND 939 946 {ECO:0000244|PDB:2FGE}.
TURN 947 950 {ECO:0000244|PDB:2FGE}.
STRAND 951 960 {ECO:0000244|PDB:2FGE}.
HELIX 963 970 {ECO:0000244|PDB:2FGE}.
HELIX 972 977 {ECO:0000244|PDB:2FGE}.
HELIX 983 997 {ECO:0000244|PDB:2FGE}.
HELIX 1003 1015 {ECO:0000244|PDB:2FGE}.
HELIX 1020 1031 {ECO:0000244|PDB:2FGE}.
HELIX 1035 1051 {ECO:0000244|PDB:2FGE}.
STRAND 1053 1058 {ECO:0000244|PDB:2FGE}.
HELIX 1060 1069 {ECO:0000244|PDB:2FGE}.
TURN 1070 1072 {ECO:0000244|PDB:2FGE}.
STRAND 1074 1077 {ECO:0000244|PDB:2FGE}.
SEQUENCE 1080 AA; 121015 MW; 9FD259970195B9FC CRC64;
MLRTVSCLAS RSSSSLFFRF FRQFPRSYMS LTSSTAALRV PSRNLRRISS PSVAGRRLLL
RRGLRIPSAA VRSVNGQFSR LSVRAVATQP APLYPDVGQD EAEKLGFEKV SEEFISECKS
KAILFKHKKT GCEVMSVSNE DENKVFGVVF RTPPKDSTGI PHILEHSVLC GSRKYPVKEP
FVELLKGSLH TFLNAFTYPD RTCYPVASTN TKDFYNLVDV YLDAVFFPKC VDDAHTFQQE
GWHYELNDPS EDISYKGVVF NEMKGVYSQP DNILGRIAQQ ALSPENTYGV DSGGDPKDIP
NLTFEEFKEF HRQYYHPSNA RIWFYGDDDP VHRLRVLSEY LDMFEASPSP NSSKIKFQKL
FSEPVRLVEK YPAGRDGDLK KKHMLCVNWL LSEKPLDLQT QLALGFLDHL MLGTPASPLR
KILLESGLGE ALVSSGLSDE LLQPQFGIGL KGVSEENVQK VEELIMDTLK KLAEEGFDND
AVEASMNTIE FSLRENNTGS FPRGLSLMLQ SISKWIYDMD PFEPLKYTEP LKALKTRIAE
EGSKAVFSPL IEKLILNNSH RVTIEMQPDP EKATQEEVEE KNILEKVKAA MTEEDLAELA
RATEELKLKQ ETPDPPEALR CVPSLNLGDI PKEPTYVPTE VGDINGVKVL RHDLFTNDII
YTEVVFDIGS LKHELLPLVP LFCQSLLEMG TKDLTFVQLN QLIGRKTGGI SVYPLTSSVR
GKDEPCSKII VRGKSMAGRA DDLFNLMNCL LQEVQFTDQQ RFKQFVSQSR ARMENRLRGS
GHGIAAARMD AMLNIAGWMS EQMGGLSYLE FLHTLEKKVD EDWEGISSSL EEIRRSLLAR
NGCIVNMTAD GKSLTNVEKS VAKFLDLLPE NPSGGLVTWD GRLPLRNEAI VIPTQVNYVG
KAGNIYSTGY ELDGSAYVIS KHISNTWLWD RVRVSGGAYG GFCDFDSHSG VFSYLSYRDP
NLLKTLDIYD GTGDFLRGLD VDQETLTKAI IGTIGDVDSY QLPDAKGYSS LLRHLLGVTD
EERQRKREEI LTTSLKDFKD FAQAIDVVRD KGVAVAVASA EDIDAANNER SNFFEVKKAL


Related products :

Catalog number Product name Quantity
EIAAB32337 hMP1,Homo sapiens,hPreP,Human,KIAA1104,Metalloprotease 1,MP1,Pitrilysin metalloproteinase 1,PITRM1,Presequence protease, mitochondrial
CSB-EL018041MO Mouse Presequence protease, mitochondrial(PITRM1) ELISA kit 96T
G0808 Presequence protease, mitochondrial (PITRM1), Mouse, ELISA Kit 96T
G0807 Presequence protease, mitochondrial (PITRM1), Human, ELISA Kit 96T
CSB-EL018041HU Human Presequence protease, mitochondrial(PITRM1) ELISA kit 96T
CSB-EL018041MO Mouse Presequence protease, mitochondrial(PITRM1) ELISA kit SpeciesMouse 96T
CSB-EL018041HU Human Presequence protease, mitochondrial(PITRM1) ELISA kit SpeciesHuman 96T
PREP_MOUSE ELISA Kit FOR Presequence protease, mitochondrial; organism: Mouse; gene name: Pitrm1 96T
EIAAB32338 Kiaa1104,Mouse,Mus musculus,Ntup1,Pitrilysin metalloproteinase 1,Pitrm1,Presequence protease, mitochondrial
EIAAB46691 ATP-dependent metalloprotease FtsH1,ATP-dependent zinc metalloprotease YME1L1,FTSH1,Homo sapiens,Human,Meg-4,PAMP,Presenilin-associated metalloprotease,UNQ1868_PRO4304,YME1L,YME1L1,YME1-like protein 1
AS10 1592 Antibody: sll0528 | putative zinc metalloprotease sII0528 (100 ul), Immunogen: synthetic peptide (amino acids 271 - 286) specific for protease Sll0528, Q55518 from Synechocystis sp. PCC 6803, Host: ra 100 ul
AS10 1623 Antibody: sll0528 | putative zinc metalloprotease sII0528 (300 ul), Immunogen: synthetic peptide (amino acids 271 - 286) specific for protease Sll0528, Q55518 from Synechocystis sp. PCC 6803, Host: ra 300 ul
20312409-1 Deg5 | protease Do-like 5, chloroplastic 200 uL
AS10 1596 Antibody: slr1821 | putative zinc metalloprotease slr1821 (100 ul), Immunogen: synthetic peptide (amino acids 216 – 230) specific for protease Slr1821 from Synechocystis sp. PCC 6803, P73714 100 ul
AS10 1621 Antibody: slr1821 | putative zinc metalloprotease slr1821 (300 ul), Immunogen: synthetic peptide (amino acids 216 – 230) specific for protease Slr1821 from Synechocystis sp. PCC 6803, P73714 300 ul
AS10703 Deg5 | protease Do_like 5, chloroplastic 200 ul
AS07246 Deg1 | chloroplastic DegP_type serine protease 1 360 ug
AS07 246 Deg1 | chloroplastic DegP_type serine protease 1 360 ug
AS10 703 rabbit polyclonal Deg5 | protease Do-like 5, chloroplastic 200
AS14 2767 rabbit polyclonal Deg8 | protease Do-like 8, chloroplastic 50
AS07 246 rabbit polyclonal Deg1 | chloroplastic DegP-type serine protease 1 360
AS10 1581 rabbit polyclonal Deg2 | chloroplastic DegP-type serine protease 2 200 ul
EIAAB42422 Magmas,Mitochondria-associated granulocyte macrophage CSF-signaling molecule,Mitochondrial import inner membrane translocase subunit TIM16,Mouse,Mus musculus,Pam16,Presequence translocated-associated
EIAAB42421 CGI-136,Homo sapiens,Human,MAGMAS,Mitochondria-associated granulocyte macrophage CSF-signaling molecule,Mitochondrial import inner membrane translocase subunit TIM16,PAM16,Presequence translocated-ass
EIAAB46692 ATP-dependent metalloprotease FtsH1,ATP-dependent zinc metalloprotease YME1L1,Mouse,Mus musculus,Yme1l1,YME1-like protein 1


 

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