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

Probable pectinesterase/pectinesterase inhibitor 32 [Includes: Pectinesterase inhibitor 32 (Pectin methylesterase inhibitor 32); Pectinesterase 32 (PE 32) (EC 3.1.1.11) (Pectin methylesterase 32) (AtPME32)]

 PME32_ARATH             Reviewed;         527 AA.
Q9LXK7; Q8VZ27;
05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
30-AUG-2017, entry version 106.
RecName: Full=Probable pectinesterase/pectinesterase inhibitor 32;
Includes:
RecName: Full=Pectinesterase inhibitor 32;
AltName: Full=Pectin methylesterase inhibitor 32;
Includes:
RecName: Full=Pectinesterase 32;
Short=PE 32;
EC=3.1.1.11;
AltName: Full=Pectin methylesterase 32;
Short=AtPME32;
Flags: Precursor;
Name=PME32; Synonyms=ARATH32; OrderedLocusNames=At3g43270;
ORFNames=F7K15.120;
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=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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]
GENE FAMILY, AND NOMENCLATURE.
PubMed=15337457; DOI=10.1016/j.carres.2004.06.023;
Markovic O., Janecek S.;
"Pectin methylesterases: sequence-structural features and phylogenetic
relationships.";
Carbohydr. Res. 339:2281-2295(2004).
[5]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=16622707; DOI=10.1007/s00425-006-0261-9;
Louvet R., Cavel E., Gutierrez L., Guenin S., Roger D., Gillet F.,
Guerineau F., Pelloux J.;
"Comprehensive expression profiling of the pectin methylesterase gene
family during silique development in Arabidopsis thaliana.";
Planta 224:782-791(2006).
-!- FUNCTION: Acts in the modification of cell walls via
demethylesterification of cell wall pectin. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Pectin + n H(2)O = n methanol + pectate.
-!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-
D-gluconate from pectin: step 1/5.
-!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9LXK7-1; Sequence=Displayed;
Name=2;
IsoId=Q9LXK7-2; Sequence=VSP_037089, VSP_037090;
-!- TISSUE SPECIFICITY: Expressed in siliques.
{ECO:0000269|PubMed:16622707}.
-!- DEVELOPMENTAL STAGE: Expressed during late developmental phases of
siliques. {ECO:0000269|PubMed:16622707}.
-!- MISCELLANEOUS: The PMEI region may act as an autoinhibitory domain
and prevent untimely PME activity during transport.
-!- SIMILARITY: In the N-terminal section; belongs to the PMEI family.
{ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the
pectinesterase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AL353871; CAB89048.1; -; Genomic_DNA.
EMBL; CP002686; AEE77781.1; -; Genomic_DNA.
EMBL; AY070071; AAL49828.1; -; mRNA.
EMBL; AY096694; AAM20328.1; -; mRNA.
EMBL; AY065349; AAL38790.1; -; mRNA.
EMBL; AY096720; AAM20354.1; -; mRNA.
PIR; T49241; T49241.
RefSeq; NP_189913.3; NM_114195.4. [Q9LXK7-1]
UniGene; At.28622; -.
ProteinModelPortal; Q9LXK7; -.
SMR; Q9LXK7; -.
STRING; 3702.AT3G43270.1; -.
iPTMnet; Q9LXK7; -.
PaxDb; Q9LXK7; -.
PRIDE; Q9LXK7; -.
EnsemblPlants; AT3G43270.1; AT3G43270.1; AT3G43270. [Q9LXK7-1]
GeneID; 823402; -.
Gramene; AT3G43270.1; AT3G43270.1; AT3G43270.
KEGG; ath:AT3G43270; -.
Araport; AT3G43270; -.
TAIR; locus:2084751; AT3G43270.
eggNOG; ENOG410IGVA; Eukaryota.
eggNOG; COG4677; LUCA.
HOGENOM; HOG000217409; -.
InParanoid; Q9LXK7; -.
KO; K01051; -.
OMA; APDYSTK; -.
OrthoDB; EOG093607M8; -.
PhylomeDB; Q9LXK7; -.
BioCyc; ARA:AT3G43270-MONOMER; -.
UniPathway; UPA00545; UER00823.
PRO; PR:Q9LXK7; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9LXK7; baseline and differential.
Genevisible; Q9LXK7; AT.
GO; GO:0071944; C:cell periphery; IBA:GO_Central.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
GO; GO:0030599; F:pectinesterase activity; IBA:GO_Central.
GO; GO:0046910; F:pectinesterase inhibitor activity; IBA:GO_Central.
GO; GO:0042545; P:cell wall modification; IEA:InterPro.
GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
Gene3D; 2.160.20.10; -; 1.
InterPro; IPR012334; Pectin_lyas_fold.
InterPro; IPR011050; Pectin_lyase_fold/virulence.
InterPro; IPR033131; Pectinesterase_Asp_AS.
InterPro; IPR000070; Pectinesterase_cat.
InterPro; IPR006501; Pectinesterase_inhib_dom.
InterPro; IPR018040; Pectinesterase_Tyr_AS.
Pfam; PF01095; Pectinesterase; 1.
Pfam; PF04043; PMEI; 1.
SMART; SM00856; PMEI; 1.
SUPFAM; SSF101148; SSF101148; 1.
SUPFAM; SSF51126; SSF51126; 1.
TIGRFAMs; TIGR01614; PME_inhib; 1.
PROSITE; PS00800; PECTINESTERASE_1; 1.
PROSITE; PS00503; PECTINESTERASE_2; 1.
2: Evidence at transcript level;
Alternative splicing; Aspartyl esterase; Cell wall;
Cell wall biogenesis/degradation; Complete proteome; Disulfide bond;
Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 527 Probable pectinesterase/pectinesterase
inhibitor 32.
/FTId=PRO_0000371684.
REGION 25 165 Pectinesterase inhibitor 32.
REGION 214 511 Pectinesterase 32.
COMPBIAS 259 262 Poly-Lys.
ACT_SITE 342 342 Proton donor; for pectinesterase
activity. {ECO:0000255|PROSITE-
ProRule:PRU10040}.
ACT_SITE 363 363 Nucleophile; for pectinesterase activity.
{ECO:0000255|PROSITE-ProRule:PRU10040}.
BINDING 289 289 Substrate; for pectinesterase activity.
{ECO:0000250}.
BINDING 319 319 Substrate; for pectinesterase activity.
{ECO:0000250}.
BINDING 431 431 Substrate; for pectinesterase activity.
{ECO:0000250}.
BINDING 433 433 Substrate; for pectinesterase activity.
{ECO:0000250}.
SITE 341 341 Transition state stabilizer.
{ECO:0000250}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 209 209 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 224 224 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 280 280 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 423 423 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 494 494 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 501 501 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 356 376 {ECO:0000250}.
VAR_SEQ 296 305 AVSGRGFIAR -> GKSKFIISFT (in isoform 2).
{ECO:0000303|PubMed:14593172}.
/FTId=VSP_037089.
VAR_SEQ 306 527 Missing (in isoform 2).
{ECO:0000303|PubMed:14593172}.
/FTId=VSP_037090.
SEQUENCE 527 AA; 57636 MW; CBC47903AB23A29C CRC64;
MAKFRQMGSS IFFLFLIIIS LCSAHKEAFS STDLVQMECL RVPPLEFAEA AKTVVDAITK
AVAIVSKFDK KAGKSRVSNA IVDCVDLLDS AAEELSWIIS ASQSPNGKDN STGDVGSDLR
TWISAALSNQ DTCLDGFEGT NGIIKKIVAG GLSKVGTTVR NLLTMVHSPP SKPKPKPIKA
QTMTKAHSGF SKFPSWVKPG DRKLLQTDNI TVADAVVAAD GTGNFTTISD AVLAAPDYST
KRYVIHVKRG VYVENVEIKK KKWNIMMVGD GIDATVITGN RSFIDGWTTF RSATFAVSGR
GFIARDITFQ NTAGPEKHQA VAIRSDTDLG VFYRCAMRGY QDTLYAHSMR QFFRECIITG
TVDFIFGDAT AVFQSCQIKA KQGLPNQKNS ITAQGRKDPN EPTGFTIQFS NIAADTDLLL
NLNTTATYLG RPWKLYSRTV FMQNYMSDAI NPVGWLEWNG NFALDTLYYG EYMNSGPGAS
LDRRVKWPGY HVLNTSAEAN NFTVSQLIQG NLWLPSTGIT FIAGLVS


Related products :

Catalog number Product name Quantity
bs-2219R Rabbit Anti-Pectinesterase inhibitor 18 Polyclonal Antibody 100ul
bs-2219R-Cy7 Rabbit Anti-Pectinesterase inhibitor 18 Polyclonal Antibody, Cy7 Conjugated 100ul
bs-2219R-Cy3 Rabbit Anti-Pectinesterase inhibitor 18 Polyclonal Antibody, Cy3 Conjugated 100ul
bs-2219R-Cy5 Rabbit Anti-Pectinesterase inhibitor 18 Polyclonal Antibody, Cy5 Conjugated 100ul
bs-2219R-Cy5.5 Rabbit Anti-Pectinesterase inhibitor 18 Polyclonal Antibody, Cy5.5 Conjugated 100ul
bs-2219P Peptides: pectinesterase inhibitor 18 peptide Protein Length:12-25 amino acids. 200ug lyophilized
bs-2219R-A555 Rabbit Anti-Pectinesterase inhibitor 18 Polyclonal Antibody, ALEXA FLUOR 555 Conjugated 100ul
bs-2219R-A350 Rabbit Anti-Pectinesterase inhibitor 18 Polyclonal Antibody, ALEXA FLUOR 350 Conjugated 100ul
bs-2219R-A488 Rabbit Anti-Pectinesterase inhibitor 18 Polyclonal Antibody, ALEXA FLUOR 488 Conjugated 100ul
bs-2219R-A647 Rabbit Anti-Pectinesterase inhibitor 18 Polyclonal Antibody, ALEXA FLUOR 647 Conjugated 100ul
bs-2219R-FITC Rabbit Anti-Pectinesterase inhibitor 18 Polyclonal Antibody, FITC Conjugated 100ul
bs-2219R-Biotin Rabbit Anti-Pectinesterase inhibitor 18 Polyclonal Antibody, Biotin Conjugated 100ul
orb1408 Pectinesterase antibody 200 ug
orb1408 Pectinesterase antibody 100 ug
orb3438 Pectinesterase antibody (FITC) 100 ug
A025543 Rabbit Anti-Pectinesterase Ab 100ul
orb9534 Pectinesterase antibody (FITC) 100 ug
bs-4550R Rabbit Anti-Pectinesterase Polyclonal Antibody 100ug Lyophilized
bs-2219R Rabbit Anti-Pectinesterase Polyclonal Antibody 100ug Lyophilized
bs-2219R-Cy3 Rabbit Anti-Pectinesterase Polyclonal Antibody, Cy3 Conjugated 100ug
bs-2219R-PE-Cy3 Rabbit Anti-Pectinesterase Polyclonal Antibody, PE-Cy3 Conjugated 100ug
bs-2219R-PE Rabbit Anti-Pectinesterase Polyclonal Antibody, PE Conjugated 100ug
bs-2219R-HRP Rabbit Anti-Pectinesterase Polyclonal Antibody, HRP Conjugated 100ug
bs-2219R-Cy7 Rabbit Anti-Pectinesterase Polyclonal Antibody, Cy7 Conjugated 100ug
bs-2219R-PE-Cy7 Rabbit Anti-Pectinesterase Polyclonal Antibody, PE-Cy7 Conjugated 100ug


 

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