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

S-adenosylhomocysteine hydrolase-like protein 1 (IP3R-binding protein released with inositol 1,4,5-trisphosphate) (Putative adenosylhomocysteinase 2) (S-adenosyl-L-homocysteine hydrolase 2) (AdoHcyase 2)

 SAHH2_MOUSE             Reviewed;         530 AA.
Q80SW1;
04-APR-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
07-JUN-2017, entry version 131.
RecName: Full=S-adenosylhomocysteine hydrolase-like protein 1;
AltName: Full=IP3R-binding protein released with inositol 1,4,5-trisphosphate;
AltName: Full=Putative adenosylhomocysteinase 2;
AltName: Full=S-adenosyl-L-homocysteine hydrolase 2;
Short=AdoHcyase 2;
Name=Ahcyl1; Synonyms=Irbit;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ITPR1, FUNCTION, TISSUE
SPECIFICITY, AND LACK OF S-ADENOSYLHOMOCYSTEINE HYDROLASE ACTIVITY.
TISSUE=Cerebellum;
PubMed=12525476; DOI=10.1074/jbc.M210119200;
Ando H., Mizutani A., Matsu-ura T., Mikoshiba K.;
"IRBIT, a novel inositol 1,4,5-trisphosphate (IP3) receptor-binding
protein, is released from the IP3 receptor upon IP3 binding to the
receptor.";
J. Biol. Chem. 278:10602-10612(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II; TISSUE=Mammary tumor;
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).
[3]
PROTEIN SEQUENCE OF 74-80, INTERACTION WITH ITPR1, MUTAGENESIS OF
70-SER--ASP-73; ASP-73; 82-THR--ASP-88 AND 86-ASP--GLU-88, AND
SUBCELLULAR LOCATION.
PubMed=16527252; DOI=10.1016/j.bbrc.2006.02.119;
Devogelaere B., Nadif Kasri N., Derua R., Waelkens E., Callewaert G.,
Missiaen L., Parys J.B., De Smedt H.;
"Binding of IRBIT to the IP3 receptor: determinants and functional
effects.";
Biochem. Biophys. Res. Commun. 343:49-56(2006).
[4]
PROTEIN SEQUENCE OF 479-486, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[5]
IDENTIFICATION.
PubMed=11904675; DOI=10.1007/s00251-001-0402-z;
Dekker J.W., Budhia S., Angel N.Z., Cooper B.J., Clark G.J.,
Hart D.N., Kato M.;
"Identification of an S-adenosylhomocysteine hydrolase-like transcript
induced during dendritic cell differentiation.";
Immunogenetics 53:993-1001(2002).
[6]
INTERACTION WITH SLC4A4.
PubMed=16769890; DOI=10.1073/pnas.0602250103;
Shirakabe K., Priori G., Yamada H., Ando H., Horita S., Fujita T.,
Fujimoto I., Mizutani A., Seki G., Mikoshiba K.;
"IRBIT, an inositol 1,4,5-trisphosphate receptor-binding protein,
specifically binds to and activates pancreas-type Na+/HCO3-
cotransporter 1 (pNBC1).";
Proc. Natl. Acad. Sci. U.S.A. 103:9542-9547(2006).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[8]
FUNCTION, AND INTERACTION WITH FIP1L1.
PubMed=19224921; DOI=10.1074/jbc.M807136200;
Kiefer H., Mizutani A., Iemura S., Natsume T., Ando H., Kuroda Y.,
Mikoshiba K.;
"Inositol 1,4,5-triphosphate receptor-binding protein released with
inositol 1,4,5-triphosphate (IRBIT) associates with components of the
mRNA 3' processing machinery in a phosphorylation-dependent manner and
inhibits polyadenylation.";
J. Biol. Chem. 284:10694-10705(2009).
[9]
FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH CFTR AND SLC4A4.
PubMed=19033647; DOI=10.1172/JCI37914;
Yang D., Shcheynikov N., Zeng W., Ohana E., So I., Ando H.,
Mizutani A., Mikoshiba K., Muallem S.;
"IRBIT coordinates epithelial fluid and HCO3- secretion by stimulating
the transporters pNBC1 and CFTR in the murine pancreatic duct.";
J. Clin. Invest. 119:193-202(2009).
[10]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=19220705; DOI=10.1111/j.1471-4159.2009.05979.x;
Ando H., Mizutani A., Mikoshiba K.;
"An IRBIT homologue lacks binding activity to inositol 1,4,5-
trisphosphate receptor due to the unique N-terminal appendage.";
J. Neurochem. 109:539-550(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[12]
FUNCTION, INTERACTION WITH SLC4A4, AND MUTAGENESIS OF 42-ILE--PHE-44.
PubMed=21317537; DOI=10.1172/JCI43475;
Yang D., Li Q., So I., Huang C.L., Ando H., Mizutani A., Seki G.,
Mikoshiba K., Thomas P.J., Muallem S.;
"IRBIT governs epithelial secretion in mice by antagonizing the
WNK/SPAK kinase pathway.";
J. Clin. Invest. 121:956-965(2011).
[13]
FUNCTION, AND INTERACTION WITH CFTR; ITPR1 AND SLC26A6.
PubMed=23542070; DOI=10.1053/j.gastro.2013.03.047;
Park S., Shcheynikov N., Hong J.H., Zheng C., Suh S.H., Kawaai K.,
Ando H., Mizutani A., Abe T., Kiyonari H., Seki G., Yule D.,
Mikoshiba K., Muallem S.;
"Irbit mediates synergy between ca(2+) and cAMP signaling pathways
during epithelial transport in mice.";
Gastroenterology 145:232-241(2013).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-40, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Multifaceted cellular regulator which coordinates
several essential cellular functions including regulation of
epithelial HCO3(-) and fluid secretion, mRNA processing and DNA
replication. Regulates ITPR1 sensitivity to inositol 1,4,5-
trisphosphate competing for the common binding site and acting as
endogenous 'pseudoligand' whose inhibitory activity can be
modulated by its phosphorylation status. In the pancreatic and
salivary ducts, at resting state, attenuates inositol 1,4,5-
trisphosphate-induced calcium release by interacting with ITPR1
(By similarity). When extracellular stimuli induce ITPR1
phosphorylation or inositol 1,4,5-trisphosphate production,
dissociates of ITPR1 to interact with CFTR and SLC26A6 mediating
their synergistic activation by calcium and cAMP that stimulates
the epithelial secretion of electrolytes and fluid
(PubMed:12525476, PubMed:23542070). Also activates basolateral
SLC4A4 isoform 1 to coordinate fluid and HCO3(-) secretion
(PubMed:19224921). Inhibits the effect of STK39 on SLC4A4 and CFTR
by recruiting PP1 phosphatase which activates SLC4A4, SLC26A6 and
CFTR through dephosphorylation (PubMed:19033647, PubMed:21317537).
Mediates the induction of SLC9A3 surface expression produced by
Angiotensin-2. Depending on the cell type, activates SLC9A3 in
response to calcium or reverses SLC9A3R2-dependent calcium
inhibition. May modulate the polyadenylation state of specific
mRNAs, both by controlling the subcellular location of FIP1L1 and
by inhibiting PAPOLA activity, in response to a stimulus that
alters its phosphorylation state. Acts as a (dATP)-dependent
inhibitor of ribonucleotide reductase large subunit RRM1,
controlling the endogenous dNTP pool and ensuring normal cell
cycle progression (By similarity). In vitro does not exhibit any
S-adenosyl-L-homocysteine hydrolase activity (PubMed:12525476).
{ECO:0000250|UniProtKB:B5DFN2, ECO:0000250|UniProtKB:O43865,
ECO:0000269|PubMed:12525476, ECO:0000269|PubMed:16769890,
ECO:0000269|PubMed:19033647, ECO:0000269|PubMed:19224921,
ECO:0000269|PubMed:21317537, ECO:0000269|PubMed:23542070}.
-!- COFACTOR:
Name=NAD(+); Xref=ChEBI:CHEBI:57540;
Evidence={ECO:0000250|UniProtKB:O43865};
Note=Binds 1 NAD(+) per subunit. {ECO:0000250|UniProtKB:O43865};
-!- SUBUNIT: Forms multimers (By similarity). Forms heteromultimers
with AHCYL2 (via the C-terminal region) (PubMed:19220705).
Interacts (when phosphorylated) with ITPR1 (when not
phosphorylated); the interaction suppresses inositol 1,4,5-
trisphosphate binding to ITPR1 (PubMed:23542070). Interacts with
CFTR and SLC26A6; the interactions take place once AHCYL1 is
released from ITPR1 and increase CFTR and SLC26A6 activities
(PubMed:19033647, PubMed:21317537, PubMed:23542070). Interacts
with RRM1; in a phosphorylation- and (dATP)-dependent manner.
Interacts (via PEST domain when phosphorylated) with SLC4A4
isoform 1 but not isoform 2; the interaction increases SLC4A4
isoform 1 activity (PubMed:16769890, PubMed:19033647,
PubMed:21317537). Interacts (when phosphorylated) with SLC9A3; the
interaction is required for SLC9A3 apical location and activity
(PubMed:19224921). Interacts (when phosphorylated) with FIP1L1;
the interaction is direct and associates AHCYL1 with the CPSF
complex and RNA Interacts with PAPOLA (By similarity).
{ECO:0000250|UniProtKB:O43865, ECO:0000269|PubMed:12525476,
ECO:0000269|PubMed:16527252, ECO:0000269|PubMed:16769890,
ECO:0000269|PubMed:19033647, ECO:0000269|PubMed:19220705,
ECO:0000269|PubMed:19224921, ECO:0000269|PubMed:21317537,
ECO:0000269|PubMed:23542070}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum
{ECO:0000269|PubMed:16527252}. Cytoplasm, cytosol
{ECO:0000269|PubMed:19220705}. Microsome
{ECO:0000269|PubMed:19220705}. Apical cell membrane
{ECO:0000250|UniProtKB:B5DFN2}. Note=Associates with membranes
when phosphorylated, probably through interaction with ITPR1.
{ECO:0000269|PubMed:19220705}.
-!- TISSUE SPECIFICITY: Widely expressed (at protein level). Expressed
in the lateral and luminal poles of the pancreatic duct (at
protein level). {ECO:0000269|PubMed:12525476,
ECO:0000269|PubMed:19033647, ECO:0000269|PubMed:19220705}.
-!- DOMAIN: The PEST region is essential for the interaction with
ITPR1, and, when phosphorylated, is also the RRM1-binding region.
The PDZ-binding region is required for maximal interaction with
ITPR1 and is also responsible for the IP3-insensitive interaction
with ITPR1. {ECO:0000250|UniProtKB:O43865,
ECO:0000269|PubMed:12525476}.
-!- PTM: Phosphorylated at Ser/Thr residues between Ser-68 and Thr-72
in the PEST region: required for interaction with dATP-bound RRM1
and ITPR1. Phosphorylation at Ser-68 by PRKD1 and CAMK4 is
required for further phosphorylations by CSNK1A1. Phosphorylation
is induced by oxidative stress. Probably phosphorylated by CAMK2A;
phosphorylation at Ser-68 may be required for interaction with
SLC9A3. {ECO:0000250|UniProtKB:O43865}.
-!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
{ECO:0000305}.
-!- CAUTION: In spite of its similarity with AHCY, which catalyzes the
reversible hydrolysis of S-adenosyl-L-homocysteine to adenosine
and homocysteine, recombinant AHCYL1 expressed in bacteria shows
no hydrolysase activity, nor does it affect the enzyme activity of
AHCY. {ECO:0000269|PubMed:12525476}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB092504; BAC65166.1; -; mRNA.
EMBL; BC018218; AAH18218.2; -; mRNA.
EMBL; BK000547; DAA00059.1; -; mRNA.
CCDS; CCDS38593.1; -.
RefSeq; NP_663517.2; NM_145542.3.
UniGene; Mm.220328; -.
ProteinModelPortal; Q80SW1; -.
SMR; Q80SW1; -.
IntAct; Q80SW1; 1.
MINT; MINT-4437427; -.
STRING; 10090.ENSMUSP00000029490; -.
iPTMnet; Q80SW1; -.
PhosphoSitePlus; Q80SW1; -.
SwissPalm; Q80SW1; -.
EPD; Q80SW1; -.
MaxQB; Q80SW1; -.
PaxDb; Q80SW1; -.
PeptideAtlas; Q80SW1; -.
PRIDE; Q80SW1; -.
Ensembl; ENSMUST00000029490; ENSMUSP00000029490; ENSMUSG00000027893.
GeneID; 229709; -.
KEGG; mmu:229709; -.
UCSC; uc008qxi.1; mouse.
CTD; 10768; -.
MGI; MGI:2385184; Ahcyl1.
eggNOG; KOG1370; Eukaryota.
eggNOG; COG0499; LUCA.
GeneTree; ENSGT00390000003626; -.
HOGENOM; HOG000227986; -.
HOVERGEN; HBG005041; -.
InParanoid; Q80SW1; -.
KO; K01251; -.
OMA; PVKKQIQ; -.
OrthoDB; EOG091G06EB; -.
PhylomeDB; Q80SW1; -.
TreeFam; TF300415; -.
Reactome; R-MMU-5578775; Ion homeostasis.
PRO; PR:Q80SW1; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000027893; -.
CleanEx; MM_AHCYL1; -.
ExpressionAtlas; Q80SW1; baseline and differential.
Genevisible; Q80SW1; MM.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0038166; P:angiotensin-activated signaling pathway; ISS:UniProtKB.
GO; GO:0042045; P:epithelial fluid transport; IDA:UniProtKB.
GO; GO:0006378; P:mRNA polyadenylation; IDA:MGI.
GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
GO; GO:0010765; P:positive regulation of sodium ion transport; IGI:MGI.
GO; GO:0006611; P:protein export from nucleus; IDA:MGI.
GO; GO:0044070; P:regulation of anion transport; IGI:MGI.
GO; GO:0032412; P:regulation of ion transmembrane transporter activity; IGI:MGI.
GO; GO:0031440; P:regulation of mRNA 3'-end processing; IDA:MGI.
GO; GO:0051592; P:response to calcium ion; ISO:MGI.
GO; GO:0033353; P:S-adenosylmethionine cycle; IBA:GO_Central.
CDD; cd00401; SAHH; 1.
InterPro; IPR000043; Adenosylhomocysteinase-like.
InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
InterPro; IPR016040; NAD(P)-bd_dom.
InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS.
PANTHER; PTHR23420; PTHR23420; 1.
Pfam; PF05221; AdoHcyase; 1.
Pfam; PF00670; AdoHcyase_NAD; 1.
PIRSF; PIRSF001109; Ad_hcy_hydrolase; 1.
SMART; SM00996; AdoHcyase; 1.
SMART; SM00997; AdoHcyase_NAD; 1.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR00936; ahcY; 1.
PROSITE; PS00738; ADOHCYASE_1; 1.
PROSITE; PS00739; ADOHCYASE_2; 1.
1: Evidence at protein level;
Acetylation; Cell membrane; Complete proteome; Cytoplasm;
Direct protein sequencing; Endoplasmic reticulum; Membrane; Microsome;
NAD; One-carbon metabolism; Phosphoprotein; Reference proteome;
RNA-binding.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O43865}.
CHAIN 2 530 S-adenosylhomocysteine hydrolase-like
protein 1.
/FTId=PRO_0000230300.
NP_BIND 318 322 NAD. {ECO:0000250|UniProtKB:O43865}.
NP_BIND 397 399 NAD. {ECO:0000250|UniProtKB:O43865}.
REGION 65 92 PEST. {ECO:0000269|PubMed:12525476}.
REGION 281 448 NAD binding. {ECO:0000250}.
REGION 520 530 PDZ-binding.
BINDING 155 155 Substrate. {ECO:0000250}.
BINDING 229 229 Substrate. {ECO:0000250}.
BINDING 254 254 Substrate. {ECO:0000250}.
BINDING 284 284 Substrate. {ECO:0000250}.
BINDING 288 288 Substrate. {ECO:0000250}.
BINDING 341 341 NAD. {ECO:0000250|UniProtKB:O43865}.
BINDING 376 376 NAD. {ECO:0000250|UniProtKB:O43865}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:O43865}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000250|UniProtKB:O43865}.
MOD_RES 40 40 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 68 68 Phosphoserine; by PKD.
{ECO:0000250|UniProtKB:O43865}.
MOD_RES 84 84 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 391 391 Phosphoserine.
{ECO:0000250|UniProtKB:O43865}.
MUTAGEN 42 44 IQF->AQA: Inhibits SLC4A4
dephosphorylation by PP1 phosphatase and
activity. {ECO:0000269|PubMed:21317537}.
MUTAGEN 70 73 Missing: Inhibits interaction with ITPR1.
{ECO:0000269|PubMed:16527252}.
MUTAGEN 73 73 D->R: Inhibits interaction with ITPR1.
{ECO:0000269|PubMed:16527252}.
MUTAGEN 82 88 Missing: Inhibits interaction with ITPR1.
{ECO:0000269|PubMed:16527252}.
MUTAGEN 86 88 DDE->KKK: Does not inhibits interaction
with ITPR1.
{ECO:0000269|PubMed:16527252}.
SEQUENCE 530 AA; 58951 MW; 974D23361A245D04 CRC64;
MSMPDAMPLP GVGEELKQAK EIEDAEKYSF MATVTKAPKK QIQFADDMQE FTKFPTKTGR
RSLSRSISQS STDSYSSAAS YTDSSDDEVS PREKQQTNSK GSSNFCVKNI KQAEFGRREI
EIAEQDMSAL ISLRKRAQGE KPLAGAKIVG CTHITAQTAV LIETLCALGA QCRWSACNIY
STQNEVAAAL AEAGVAVFAW KGESEDDFWW CIDRCVNMDG WQANMILDDG GDLTHWVYKK
YPNVFKKIRG IVEESVTGVH RLYQLSKAGK LCVPAMNVND SVTKQKFDNL YCCRESILDG
LKRTTDVMFG GKQVVVCGYG EVGKGCCAAL KALGAIVYIT EIDPICALQA CMDGFRVVKL
NEVIRQVDVV ITCTGNKNVV TREHLDRMKN SCIVCNMGHS NTEIDVTSLR TPELTWERVR
SQVDHVIWPD GKRVVLLAEG RLLNLSCSTV PTFVLSITAT TQALALIELY NAPEGRYKQD
VYLLPKKMDE YVASLHLPSF DAHLTELTDD QAKYLGLNKN GPFKPNYYRY


Related products :

Catalog number Product name Quantity
EIAAB37213 AdoHcyase 2,Ahcyl1,IP3R-binding protein released with inositol 1,4,5-trisphosphate,Irbit,Mouse,Mus musculus,Putative adenosylhomocysteinase 2,S-adenosylhomocysteine hydrolase-like protein 1,S-adenosyl
EIAAB37215 AdoHcyase 3,Ahcyl2,Mouse,Mus musculus,Putative adenosylhomocysteinase 3,S-adenosylhomocysteine hydrolase-like protein 2,S-adenosyl-L-homocysteine hydrolase 3
EIAAB37214 AdoHcyase 3,AHCYL2,Homo sapiens,Human,KIAA0828,Putative adenosylhomocysteinase 3,S-adenosylhomocysteine hydrolase-like protein 2,S-adenosyl-L-homocysteine hydrolase 3
EIAAB37212 AdoHcyase 2,AHCYL1,DCAL,DC-expressed AHCY-like molecule,Homo sapiens,Human,Putative adenosylhomocysteinase 2,S-adenosylhomocysteine hydrolase-like protein 1,S-adenosyl-L-homocysteine hydrolase 2,XPVKO
EIAAB37211 Adenosylhomocysteinase,AdoHcyase,Ahcy,CUBP,Liver copper-binding protein,Mouse,Mus musculus,S-adenosyl-L-homocysteine hydrolase
EIAAB37210 Adenosylhomocysteinase,AdoHcyase,AHCY,Pig,S-adenosyl-L-homocysteine hydrolase,Sus scrofa
EIAAB37208 Adenosylhomocysteinase,AdoHcyase,AHCY,Bos taurus,Bovine,S-adenosyl-L-homocysteine hydrolase
EIAAB37207 Adenosylhomocysteinase,AdoHcyase,Ahcy,Rat,Rattus norvegicus,S-adenosyl-L-homocysteine hydrolase
EIAAB37209 Adenosylhomocysteinase,AdoHcyase,AHCY,Homo sapiens,Human,S-adenosyl-L-homocysteine hydrolase,SAHH
25-118 AHCYL1 belongs to the adenosylhomocysteinase family.The protein, an inositol 1,4,5-trisphosphate receptor-binding protein, specifically binds to and activates pancreas-type Na+_HCO3- cotransporter 1 ( 0.05 mg
EIAAB33919 B5T-overexpressed gene protein,Bog,Protein BOG,Putative hydrolase RBBP9,Rat,Rattus norvegicus,Rbbp9,RBBP-9,Retinoblastoma-binding protein 9
EIAAB33920 B5T-overexpressed gene protein,Bog,Mouse,Mus musculus,Protein BOG,Putative hydrolase RBBP9,Rbbp9,RBBP-9,Retinoblastoma-binding protein 9
EIAAB38290 AblSH3-binding protein,Inositol polyphosphate phosphatase-like protein 1,Inppl1,INPPL-1,Mouse,Mus musculus,Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2,SH2 domain-containing inositol phosp
EIAAB33918 B5T-overexpressed gene protein,BOG,Homo sapiens,Human,Protein BOG,Putative hydrolase RBBP9,RBBP10,RBBP-10,RBBP9,RBBP-9,Retinoblastoma-binding protein 10,Retinoblastoma-binding protein 9
EIAAB33127 C2orf79,Homo sapiens,Human,Peptidyl-tRNA hydrolase domain-containing protein 1,PTRHD1,Putative peptidyl-tRNA hydrolase PTRHD1
EIAAB33125 Bos taurus,Bovine,Peptidyl-tRNA hydrolase domain-containing protein 1,PTRHD1,Putative peptidyl-tRNA hydrolase PTRHD1
EIAAB33126 Mouse,Mus musculus,Peptidyl-tRNA hydrolase domain-containing protein 1,Ptrhd1,Putative peptidyl-tRNA hydrolase PTRHD1
GGH-1399H Protein Recombinant Human Gamma-Glutamyl Hydrolase (conjugase, folylpolygammaglutamyl hydrolase), His-tagged 0.5mg
GGH-1399H Protein: Recombinant Human Gamma-Glutamyl Hydrolase (conjugase, folylpolygammaglutamyl hydrolase), His-tagged 0.5mg
EIAAB13118 ABHD7,Abhydrolase domain-containing protein 7,EPHX4,EPHXRP,Epoxide hydrolase 4,Epoxide hydrolase-related protein,Homo sapiens,Human
EIAAB13117 Abhd7,Abhydrolase domain-containing protein 7,Ephx4,Ephxrp,Epoxide hydrolase 4,Epoxide hydrolase-related protein,Mouse,Mus musculus
YF-MA11856 anti-S adenosylhomocysteine hydrolase (M1) 200 uL
orb34028 S adenosylhomocysteine hydrolase antibody 5 ug(Trial size)
orb34028 S adenosylhomocysteine hydrolase antibody 20 ug(Trial size)
orb34029 S adenosylhomocysteine hydrolase antibody 100 ug


 

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