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Glycogen phosphorylase, brain form (EC 2.4.1.1)

 PYGB_HUMAN              Reviewed;         843 AA.
P11216; Q96AK1; Q9NPX8;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 5.
25-OCT-2017, entry version 201.
RecName: Full=Glycogen phosphorylase, brain form {ECO:0000303|PubMed:3346228};
EC=2.4.1.1 {ECO:0000269|PubMed:27402852};
Name=PYGB {ECO:0000303|PubMed:3346228};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=3346228;
Newgard C.B., Littman D.R., van Genderen C., Smith M.,
Fletterick R.J.;
"Human brain glycogen phosphorylase. Cloning, sequence analysis,
chromosomal mapping, tissue expression, and comparison with the human
liver and muscle isozymes.";
J. Biol. Chem. 263:3850-3857(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=2615594; DOI=10.1016/0169-328X(89)90052-1;
Gelinas R.P., Froman B.E., McElroy F., Tait R.C., Gorin F.A.;
"Human brain glycogen phosphorylase: characterization of fetal cDNA
and genomic sequences.";
Brain Res. Mol. Brain Res. 6:177-185(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Skin;
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).
[5]
PROTEIN SEQUENCE OF 2-11.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[6]
PROTEIN SEQUENCE OF 2-11; 18-30; 51-61; 71-78; 193-206; 271-278;
353-359; 388-395; 400-425; 508-520; 522-533; 546-552; 558-569;
577-590; 623-640; 657-681; 731-754 AND 817-823, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Colon adenocarcinoma;
Bienvenut W.V., Murray L., Brunton V.G., Frame M.C.;
Submitted (JUL-2007) to UniProtKB.
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-843 IN COMPLEX WITH AMP,
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT, AND
PHOSPHORYLATION.
PubMed=27402852; DOI=10.1074/jbc.M116.738898;
Mathieu C., de la Sierra-Gallay I.L., Duval R., Xu X., Cocaign A.,
Leger T., Woffendin G., Camadro J.M., Etchebest C., Haouz A.,
Dupret J.M., Rodrigues-Lima F.;
"Insights into Brain Glycogen Metabolism: THE STRUCTURE OF HUMAN BRAIN
GLYCOGEN PHOSPHORYLASE.";
J. Biol. Chem. 291:18072-18083(2016).
-!- FUNCTION: Glycogen phosphorylase that regulates glycogen
mobilization (PubMed:27402852). Phosphorylase is an important
allosteric enzyme in carbohydrate metabolism (PubMed:3346228).
Enzymes from different sources differ in their regulatory
mechanisms and in their natural substrates (PubMed:3346228).
However, all known phosphorylases share catalytic and structural
properties (PubMed:3346228). {ECO:0000269|PubMed:27402852,
ECO:0000303|PubMed:3346228}.
-!- CATALYTIC ACTIVITY: ((1->4)-alpha-D-glucosyl)(n) + phosphate =
((1->4)-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate.
{ECO:0000269|PubMed:27402852}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
-!- ENZYME REGULATION: Activity of phosphorylase is controlled both by
allosteric means (through the non-covalent binding of metabolites)
and by covalent modification. Thus AMP allosterically activates,
whereas ATP, ADP, and glucose-6-phosphate allosterically inhibit,
phosphorylase B. Activated upon phosphorylation.
{ECO:0000269|PubMed:27402852}.
-!- SUBUNIT: Homodimer. Dimers associate into a tetramer to form the
enzymatically active phosphorylase A.
{ECO:0000269|PubMed:27402852}.
-!- INTERACTION:
P06737:PYGL; NbExp=8; IntAct=EBI-1047231, EBI-2511865;
Q8IUQ4:SIAH1; NbExp=3; IntAct=EBI-1047231, EBI-747107;
-!- PTM: Phosphorylated (PubMed:27402852). Phosphorylation of Ser-15
converts phosphorylase B (unphosphorylated) to phosphorylase A (By
similarity). {ECO:0000250|UniProtKB:P11217,
ECO:0000269|PubMed:27402852}.
-!- SIMILARITY: Belongs to the glycogen phosphorylase family.
{ECO:0000305}.
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EMBL; J03544; AAA59597.1; -; mRNA.
EMBL; U47025; AAB60395.1; -; mRNA.
EMBL; AL121772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC017045; AAH17045.1; -; mRNA.
EMBL; BC030795; AAH30795.1; -; mRNA.
CCDS; CCDS13171.1; -.
PIR; A40138; A40138.
RefSeq; NP_002853.2; NM_002862.3.
UniGene; Hs.368157; -.
PDB; 5IKO; X-ray; 2.50 A; A=1-843.
PDB; 5IKP; X-ray; 3.40 A; A=1-843.
PDBsum; 5IKO; -.
PDBsum; 5IKP; -.
ProteinModelPortal; P11216; -.
SMR; P11216; -.
BioGrid; 111792; 50.
IntAct; P11216; 7.
STRING; 9606.ENSP00000216962; -.
BindingDB; P11216; -.
ChEMBL; CHEMBL3856; -.
DrugBank; DB00114; Pyridoxal Phosphate.
CAZy; GT35; Glycosyltransferase Family 35.
iPTMnet; P11216; -.
PhosphoSitePlus; P11216; -.
SwissPalm; P11216; -.
BioMuta; PYGB; -.
DMDM; 20178317; -.
EPD; P11216; -.
MaxQB; P11216; -.
PaxDb; P11216; -.
PeptideAtlas; P11216; -.
PRIDE; P11216; -.
DNASU; 5834; -.
Ensembl; ENST00000216962; ENSP00000216962; ENSG00000100994.
GeneID; 5834; -.
KEGG; hsa:5834; -.
UCSC; uc002wup.4; human.
CTD; 5834; -.
DisGeNET; 5834; -.
EuPathDB; HostDB:ENSG00000100994.11; -.
GeneCards; PYGB; -.
HGNC; HGNC:9723; PYGB.
HPA; HPA031067; -.
MIM; 138550; gene.
neXtProt; NX_P11216; -.
OpenTargets; ENSG00000100994; -.
PharmGKB; PA34066; -.
eggNOG; KOG2099; Eukaryota.
eggNOG; COG0058; LUCA.
GeneTree; ENSGT00390000016886; -.
HOVERGEN; HBG006848; -.
InParanoid; P11216; -.
KO; K00688; -.
OMA; LHDFNVG; -.
OrthoDB; EOG091G03RB; -.
PhylomeDB; P11216; -.
TreeFam; TF300309; -.
BioCyc; MetaCyc:HS02178-MONOMER; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-70221; Glycogen breakdown (glycogenolysis).
ChiTaRS; PYGB; human.
GenomeRNAi; 5834; -.
PRO; PR:P11216; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000100994; -.
CleanEx; HS_PYGB; -.
ExpressionAtlas; P11216; baseline and differential.
Genevisible; P11216; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0008184; F:glycogen phosphorylase activity; IBA:GO_Central.
GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
GO; GO:0005980; P:glycogen catabolic process; IBA:GO_Central.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
CDD; cd04300; GT1_Glycogen_Phosphorylase; 1.
InterPro; IPR011833; Glycg_phsphrylas.
InterPro; IPR000811; Glyco_trans_35.
InterPro; IPR035090; Pyridoxal_P_attach_site.
PANTHER; PTHR11468; PTHR11468; 1.
Pfam; PF00343; Phosphorylase; 1.
PIRSF; PIRSF000460; Pprylas_GlgP; 1.
TIGRFAMs; TIGR02093; P_ylase; 1.
PROSITE; PS00102; PHOSPHORYLASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Allosteric enzyme; Carbohydrate metabolism;
Complete proteome; Direct protein sequencing; Glycogen metabolism;
Glycosyltransferase; Phosphoprotein; Polymorphism;
Pyridoxal phosphate; Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:12665801,
ECO:0000269|Ref.6}.
CHAIN 2 843 Glycogen phosphorylase, brain form.
/FTId=PRO_0000188535.
REGION 677 678 Pyridoxal 5'-phosphate.
{ECO:0000269|PubMed:27402852}.
BINDING 43 43 AMP; shared with dimeric partner.
{ECO:0000269|PubMed:27402852}.
BINDING 197 197 AMP. {ECO:0000269|PubMed:27402852}.
BINDING 310 310 AMP. {ECO:0000269|PubMed:27402852}.
BINDING 569 569 Pyridoxal 5'-phosphate.
{ECO:0000269|PubMed:27402852}.
SITE 76 76 Participates in a stacking interaction
with the adenine ring of AMP.
{ECO:0000269|PubMed:27402852}.
SITE 109 109 Involved in the association of subunits.
{ECO:0000250}.
SITE 143 143 Involved in the association of subunits.
{ECO:0000250}.
SITE 156 156 May be involved in allosteric control.
{ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.6}.
MOD_RES 15 15 Phosphoserine; by PHK; in form
phosphorylase A.
{ECO:0000250|UniProtKB:P53534}.
MOD_RES 197 197 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q8CI94}.
MOD_RES 473 473 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q8CI94}.
MOD_RES 681 681 N6-(pyridoxal phosphate)lysine.
{ECO:0000269|PubMed:27402852}.
VARIANT 303 303 A -> S (in dbSNP:rs2228976).
/FTId=VAR_034428.
VARIANT 502 502 D -> N (in dbSNP:rs2227891).
/FTId=VAR_020212.
CONFLICT 2 3 AK -> GE (in Ref. 1 and 2).
{ECO:0000305}.
CONFLICT 248 248 K -> R (in Ref. 1; AAA59597).
{ECO:0000305}.
CONFLICT 302 302 A -> G (in Ref. 1; AAA59597).
{ECO:0000305}.
CONFLICT 835 843 IPPPNIPRD -> LQHLPHPEWESGGATCWAPPELCTHLAM
Y (in Ref. 1; AAA59597). {ECO:0000305}.
HELIX 23 38 {ECO:0000244|PDB:5IKO}.
TURN 44 46 {ECO:0000244|PDB:5IKO}.
HELIX 49 78 {ECO:0000244|PDB:5IKO}.
STRAND 82 86 {ECO:0000244|PDB:5IKO}.
HELIX 96 102 {ECO:0000244|PDB:5IKO}.
HELIX 106 115 {ECO:0000244|PDB:5IKO}.
HELIX 120 126 {ECO:0000244|PDB:5IKO}.
STRAND 130 132 {ECO:0000244|PDB:5IKP}.
HELIX 136 150 {ECO:0000244|PDB:5IKO}.
STRAND 155 160 {ECO:0000244|PDB:5IKO}.
STRAND 168 172 {ECO:0000244|PDB:5IKO}.
STRAND 175 179 {ECO:0000244|PDB:5IKO}.
TURN 183 186 {ECO:0000244|PDB:5IKO}.
HELIX 195 197 {ECO:0000244|PDB:5IKO}.
STRAND 199 210 {ECO:0000244|PDB:5IKO}.
STRAND 213 232 {ECO:0000244|PDB:5IKO}.
STRAND 234 237 {ECO:0000244|PDB:5IKP}.
STRAND 239 248 {ECO:0000244|PDB:5IKO}.
HELIX 260 274 {ECO:0000244|PDB:5IKO}.
HELIX 275 277 {ECO:0000244|PDB:5IKO}.
STRAND 279 281 {ECO:0000244|PDB:5IKO}.
HELIX 290 313 {ECO:0000244|PDB:5IKO}.
HELIX 326 329 {ECO:0000244|PDB:5IKO}.
HELIX 330 333 {ECO:0000244|PDB:5IKO}.
STRAND 334 341 {ECO:0000244|PDB:5IKO}.
HELIX 342 345 {ECO:0000244|PDB:5IKO}.
HELIX 346 356 {ECO:0000244|PDB:5IKO}.
HELIX 362 372 {ECO:0000244|PDB:5IKO}.
STRAND 373 376 {ECO:0000244|PDB:5IKO}.
HELIX 382 384 {ECO:0000244|PDB:5IKO}.
STRAND 387 389 {ECO:0000244|PDB:5IKO}.
HELIX 390 396 {ECO:0000244|PDB:5IKO}.
HELIX 398 418 {ECO:0000244|PDB:5IKO}.
HELIX 423 429 {ECO:0000244|PDB:5IKO}.
STRAND 431 433 {ECO:0000244|PDB:5IKO}.
STRAND 435 437 {ECO:0000244|PDB:5IKO}.
STRAND 439 441 {ECO:0000244|PDB:5IKO}.
HELIX 442 448 {ECO:0000244|PDB:5IKO}.
STRAND 453 457 {ECO:0000244|PDB:5IKO}.
HELIX 458 466 {ECO:0000244|PDB:5IKO}.
TURN 467 469 {ECO:0000244|PDB:5IKO}.
HELIX 470 475 {ECO:0000244|PDB:5IKO}.
HELIX 477 479 {ECO:0000244|PDB:5IKO}.
STRAND 480 482 {ECO:0000244|PDB:5IKO}.
HELIX 490 495 {ECO:0000244|PDB:5IKO}.
HELIX 498 508 {ECO:0000244|PDB:5IKO}.
HELIX 511 513 {ECO:0000244|PDB:5IKO}.
HELIX 516 526 {ECO:0000244|PDB:5IKO}.
HELIX 529 554 {ECO:0000244|PDB:5IKO}.
STRAND 562 569 {ECO:0000244|PDB:5IKO}.
TURN 573 576 {ECO:0000244|PDB:5IKO}.
HELIX 577 593 {ECO:0000244|PDB:5IKO}.
STRAND 602 607 {ECO:0000244|PDB:5IKO}.
HELIX 615 632 {ECO:0000244|PDB:5IKO}.
TURN 635 637 {ECO:0000244|PDB:5IKO}.
HELIX 638 640 {ECO:0000244|PDB:5IKO}.
STRAND 641 648 {ECO:0000244|PDB:5IKO}.
HELIX 651 657 {ECO:0000244|PDB:5IKO}.
HELIX 658 660 {ECO:0000244|PDB:5IKP}.
STRAND 662 666 {ECO:0000244|PDB:5IKO}.
TURN 670 672 {ECO:0000244|PDB:5IKP}.
HELIX 678 684 {ECO:0000244|PDB:5IKO}.
STRAND 688 691 {ECO:0000244|PDB:5IKO}.
HELIX 696 704 {ECO:0000244|PDB:5IKO}.
HELIX 706 708 {ECO:0000244|PDB:5IKO}.
STRAND 709 711 {ECO:0000244|PDB:5IKO}.
HELIX 716 725 {ECO:0000244|PDB:5IKO}.
HELIX 730 734 {ECO:0000244|PDB:5IKO}.
HELIX 737 748 {ECO:0000244|PDB:5IKO}.
TURN 749 751 {ECO:0000244|PDB:5IKO}.
STRAND 753 755 {ECO:0000244|PDB:5IKP}.
TURN 756 759 {ECO:0000244|PDB:5IKO}.
HELIX 760 768 {ECO:0000244|PDB:5IKO}.
HELIX 774 792 {ECO:0000244|PDB:5IKO}.
HELIX 795 807 {ECO:0000244|PDB:5IKO}.
HELIX 810 812 {ECO:0000244|PDB:5IKO}.
HELIX 814 824 {ECO:0000244|PDB:5IKO}.
SEQUENCE 843 AA; 96696 MW; 810BFAD3002CACB0 CRC64;
MAKPLTDSEK RKQISVRGLA GLGDVAEVRK SFNRHLHFTL VKDRNVATPR DYFFALAHTV
RDHLVGRWIR TQQHYYERDP KRIYYLSLEF YMGRTLQNTM VNLGLQNACD EAIYQLGLDL
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK IVNGWQVEEA
DDWLRYGNPW EKARPEYMLP VHFYGRVEHT PDGVKWLDTQ VVLAMPYDTP VPGYKNNTVN
TMRLWSAKAP NDFKLQDFNV GDYIEAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
VAATLQDIIR RFKSSKFGCR DPVRTCFETF PDKVAIQLND THPALSIPEL MRILVDVEKV
DWDKAWEITK KTCAYTNHTV LPEALERWPV SMFEKLLPRH LEIIYAINQR HLDHVAALFP
GDVDRLRRMS VIEEGDCKRI NMAHLCVIGS HAVNGVARIH SEIVKQSVFK DFYELEPEKF
QNKTNGITPR RWLLLCNPGL ADTIVEKIGE EFLTDLSQLK KLLPLVSDEV FIRDVAKVKQ
ENKLKFSAFL EKEYKVKINP SSMFDVHVKR IHEYKRQLLN CLHVVTLYNR IKRDPAKAFV
PRTVMIGGKA APGYHMAKLI IKLVTSIGDV VNHDPVVGDR LKVIFLENYR VSLAEKVIPA
ADLSQQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGAENLF IFGLRVEDVE
ALDRKGYNAR EYYDHLPELK QAVDQISSGF FSPKEPDCFK DIVNMLMHHD RFKVFADYEA
YMQCQAQVDQ LYRNPKEWTK KVIRNIACSG KFSSDRTITE YAREIWGVEP SDLQIPPPNI
PRD


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GTX20883 Glycogen phosphorylase brain form 100 µg
ARP48587_P050 Glycogen phosphorylase brain form 50 µg
ARP48586_P050 Glycogen phosphorylase brain form 50 µg
GTX20877 Glycogen phosphorylase brain form 100 µg


 

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