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

Proenkephalin-B (Beta-neoendorphin-dynorphin) (Preprodynorphin) [Cleaved into: Alpha-neoendorphin; Beta-neoendorphin; Big dynorphin (Big Dyn); Dynorphin A(1-17) (Dyn-A17) (Dynorphin A); Dynorphin A(1-13); Dynorphin A(1-8); Leu-enkephalin; Rimorphin (Dynorphin B) (Dyn-B) (Dynorphin B(1-13)); Leumorphin (Dynorphin B-29)]

 PDYN_HUMAN              Reviewed;         254 AA.
P01213; A8K0Q3;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
20-JUN-2018, entry version 160.
RecName: Full=Proenkephalin-B;
AltName: Full=Beta-neoendorphin-dynorphin;
AltName: Full=Preprodynorphin;
Contains:
RecName: Full=Alpha-neoendorphin;
Contains:
RecName: Full=Beta-neoendorphin;
Contains:
RecName: Full=Big dynorphin;
Short=Big Dyn;
Contains:
RecName: Full=Dynorphin A(1-17);
Short=Dyn-A17;
Short=Dynorphin A;
Contains:
RecName: Full=Dynorphin A(1-13);
Contains:
RecName: Full=Dynorphin A(1-8);
Contains:
RecName: Full=Leu-enkephalin;
Contains:
RecName: Full=Rimorphin;
AltName: Full=Dynorphin B;
Short=Dyn-B;
AltName: Full=Dynorphin B(1-13);
Contains:
RecName: Full=Leumorphin;
AltName: Full=Dynorphin B-29;
Flags: Precursor;
Name=PDYN;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6316163; DOI=10.1038/306611a0;
Horikawa S., Takai T., Toyosato M., Takahashi H., Noda M.,
Kakidani H., Kubo T., Hirose T., Inayama S., Hayashida H., Miyata T.,
Numa S.;
"Isolation and structural organization of the human preproenkephalin B
gene.";
Nature 306:611-614(1983).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Amygdala;
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).
[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 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[6]
STRUCTURE BY NMR OF DYNORPHIN A(1-17).
PubMed=9047294; DOI=10.1021/bi961457h;
Tessmer M.R., Kallick D.A.;
"NMR and structural model of dynorphin A (1-17) bound to
dodecylphosphocholine micelles.";
Biochemistry 36:1971-1981(1997).
[7]
FUNCTION.
PubMed=17316701; DOI=10.1016/j.lfs.2007.01.018;
Chen Y., Chen C., Liu-Chen L.-Y.;
"Dynorphin peptides differentially regulate the human kappa opioid
receptor.";
Life Sci. 80:1439-1448(2007).
[8]
FUNCTION.
PubMed=16515546; DOI=10.1111/j.1471-4159.2006.03732.x;
Merg F., Filliol D., Usynin I., Bazov I., Bark N., Hurd Y.L.,
Yakovleva T., Kieffer B.L., Bakalkin G.;
"Big dynorphin as a putative endogenous ligand for the kappa-opioid
receptor.";
J. Neurochem. 97:292-301(2006).
[9]
VARIANTS SCA23 SER-138; SER-211; TRP-212 AND CYS-215, AND
CHARACTERIZATION OF VARIANTS SCA23 SER-138; SER-211; TRP-212 AND
CYS-215.
PubMed=21035104; DOI=10.1016/j.ajhg.2010.10.001;
Bakalkin G., Watanabe H., Jezierska J., Depoorter C.,
Verschuuren-Bemelmans C., Bazov I., Artemenko K.A., Yakovleva T.,
Dooijes D., Van de Warrenburg B.P., Zubarev R.A., Kremer B.,
Knapp P.E., Hauser K.F., Wijmenga C., Nyberg F., Sinke R.J.,
Verbeek D.S.;
"Prodynorphin mutations cause the neurodegenerative disorder
spinocerebellar ataxia type 23.";
Am. J. Hum. Genet. 87:593-603(2010).
[10]
ERRATUM.
Bakalkin G., Watanabe H., Jezierska J., Depoorter C.,
Verschuuren-Bemelmans C., Bazov I., Artemenko K.A., Yakovleva T.,
Dooijes D., Van de Warrenburg B.P., Zubarev R.A., Kremer B.,
Knapp P.E., Hauser K.F., Wijmenga C., Nyberg F., Sinke R.J.,
Verbeek D.S.;
Am. J. Hum. Genet. 87:736-736(2010).
[11]
VARIANTS SCA23 SER-211; TRP-212 AND CYS-215, AND CHARACTERIZATION OF
VARIANTS SCA23 SER-211; TRP-212 AND CYS-215.
PubMed=21712028; DOI=10.1016/j.bbrc.2011.06.105;
Madani F., Taqi M.M., Warmlander S.K., Verbeek D.S., Bakalkin G.,
Graslund A.;
"Perturbations of model membranes induced by pathogenic dynorphin A
mutants causing neurodegeneration in human brain.";
Biochem. Biophys. Res. Commun. 411:111-114(2011).
[12]
VARIANT SCA23 TYR-22, AND VARIANT GLN-25.
PubMed=23108490; DOI=10.1007/s00415-012-6721-1;
Fawcett K., Mehrabian M., Liu Y.T., Hamed S., Elahi E., Revesz T.,
Koutsis G., Herscheson J., Schottlaender L., Wardle M., Morrison P.J.,
Morris H.R., Giunti P., Wood N., Houlden H.;
"The frequency of spinocerebellar ataxia type 23 in a UK population.";
J. Neurol. 260:856-859(2013).
[13]
VARIANTS SCA23 CYS-206; HIS-206 AND ASP-227.
PubMed=23471613; DOI=10.1007/s00415-013-6882-6;
Jezierska J., Stevanin G., Watanabe H., Fokkens M.R., Zagnoli F.,
Kok J., Goas J.Y., Bertrand P., Robin C., Brice A., Bakalkin G.,
Durr A., Verbeek D.S.;
"Identification and characterization of novel PDYN mutations in
dominant cerebellar ataxia cases.";
J. Neurol. 260:1807-1812(2013).
-!- FUNCTION: Leu-enkephalins compete with and mimic the effects of
opiate drugs. They play a role in a number of physiologic
functions, including pain perception and responses to stress (By
similarity). {ECO:0000250}.
-!- FUNCTION: Dynorphin peptides differentially regulate the kappa
opioid receptor. Dynorphin A(1-13) has a typical opiod activity,
it is 700 times more potent than Leu-enkephalin (By similarity).
{ECO:0000250}.
-!- FUNCTION: Leumorphin has a typical opiod activity and may have
anti-apoptotic effect. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- PTM: The N-terminal domain contains 6 conserved cysteines thought
to be involved in disulfide bonding and/or processing.
-!- DISEASE: Spinocerebellar ataxia 23 (SCA23) [MIM:610245]:
Spinocerebellar ataxia is a clinically and genetically
heterogeneous group of cerebellar disorders. Patients show
progressive incoordination of gait and often poor coordination of
hands, speech and eye movements, due to degeneration of the
cerebellum with variable involvement of the brainstem and spinal
cord. SCA23 is an adult-onset autosomal dominant form
characterized by slowly progressive gait and limb ataxia, with
variable additional features, including peripheral neuropathy and
dysarthria. {ECO:0000269|PubMed:21035104,
ECO:0000269|PubMed:21712028, ECO:0000269|PubMed:23108490,
ECO:0000269|PubMed:23471613}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the opioid neuropeptide precursor family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X02536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; K02267; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AH002816; AAA58456.2; -; Genomic_DNA.
EMBL; X00176; CAA24999.1; -; Genomic_DNA.
EMBL; AK289618; BAF82307.1; -; mRNA.
EMBL; AL034562; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471133; EAX10604.1; -; Genomic_DNA.
EMBL; BC026334; AAH26334.1; -; mRNA.
CCDS; CCDS13023.1; -.
PIR; A01478; DFHU.
RefSeq; NP_001177821.1; NM_001190892.1.
RefSeq; NP_001177827.1; NM_001190898.2.
RefSeq; NP_001177828.1; NM_001190899.2.
RefSeq; NP_001177829.1; NM_001190900.1.
RefSeq; NP_077722.1; NM_024411.4.
RefSeq; XP_011527546.1; XM_011529244.1.
RefSeq; XP_011527547.1; XM_011529245.1.
RefSeq; XP_011527548.1; XM_011529246.2.
RefSeq; XP_011527549.1; XM_011529247.1.
RefSeq; XP_011527550.1; XM_011529248.1.
RefSeq; XP_011527551.1; XM_011529249.2.
RefSeq; XP_011527552.1; XM_011529250.2.
RefSeq; XP_016883367.1; XM_017027878.1.
UniGene; Hs.22584; -.
PDB; 2N2F; NMR; -; A=207-219.
PDBsum; 2N2F; -.
ProteinModelPortal; P01213; -.
SMR; P01213; -.
BioGrid; 111199; 11.
STRING; 9606.ENSP00000217305; -.
BindingDB; P01213; -.
ChEMBL; CHEMBL2227; -.
TCDB; 1.C.89.1.1; the dynorphin channel-forming neuropeptide (dynorphin) family.
iPTMnet; P01213; -.
PhosphoSitePlus; P01213; -.
BioMuta; PDYN; -.
EPD; P01213; -.
PaxDb; P01213; -.
PeptideAtlas; P01213; -.
PRIDE; P01213; -.
ProteomicsDB; 51345; -.
DNASU; 5173; -.
Ensembl; ENST00000217305; ENSP00000217305; ENSG00000101327.
Ensembl; ENST00000539905; ENSP00000440185; ENSG00000101327.
Ensembl; ENST00000540134; ENSP00000442259; ENSG00000101327.
GeneID; 5173; -.
KEGG; hsa:5173; -.
UCSC; uc002wfv.4; human.
CTD; 5173; -.
DisGeNET; 5173; -.
EuPathDB; HostDB:ENSG00000101327.8; -.
GeneCards; PDYN; -.
HGNC; HGNC:8820; PDYN.
HPA; HPA049841; -.
HPA; HPA053342; -.
MalaCards; PDYN; -.
MIM; 131340; gene.
MIM; 610245; phenotype.
neXtProt; NX_P01213; -.
OpenTargets; ENSG00000101327; -.
Orphanet; 101108; Spinocerebellar ataxia type 23.
PharmGKB; PA33163; -.
eggNOG; ENOG410IIMD; Eukaryota.
eggNOG; ENOG4111RTT; LUCA.
GeneTree; ENSGT00530000063761; -.
HOGENOM; HOG000013003; -.
HOVERGEN; HBG000063; -.
InParanoid; P01213; -.
KO; K15840; -.
OMA; WERCQGL; -.
OrthoDB; EOG091G0HV8; -.
PhylomeDB; P01213; -.
TreeFam; TF332620; -.
Reactome; R-HSA-111885; Opioid Signalling.
Reactome; R-HSA-202040; G-protein activation.
Reactome; R-HSA-375276; Peptide ligand-binding receptors.
Reactome; R-HSA-418594; G alpha (i) signalling events.
SIGNOR; P01213; -.
GenomeRNAi; 5173; -.
PMAP-CutDB; P01213; -.
PRO; PR:P01213; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000101327; -.
CleanEx; HS_PDYN; -.
Genevisible; P01213; HS.
GO; GO:0043679; C:axon terminus; IBA:GO_Central.
GO; GO:0030425; C:dendrite; IBA:GO_Central.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005184; F:neuropeptide hormone activity; IBA:GO_Central.
GO; GO:0001515; F:opioid peptide activity; IEA:UniProtKB-KW.
GO; GO:0031628; F:opioid receptor binding; IBA:GO_Central.
GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
GO; GO:0007600; P:sensory perception; IBA:GO_Central.
InterPro; IPR006024; Opioid_neupept.
InterPro; IPR000750; Proenkphlin_B.
PANTHER; PTHR11438; PTHR11438; 1.
PANTHER; PTHR11438:SF4; PTHR11438:SF4; 1.
Pfam; PF01160; Opiods_neuropep; 1.
PRINTS; PR01028; OPIOIDPRCRSR.
PRINTS; PR01030; PENKBPRCRSR.
PROSITE; PS01252; OPIOIDS_PRECURSOR; 1.
1: Evidence at protein level;
3D-structure; Cleavage on pair of basic residues; Complete proteome;
Disease mutation; Disulfide bond; Endorphin; Neurodegeneration;
Neuropeptide; Neurotransmitter; Opioid peptide; Reference proteome;
Secreted; Signal; Spinocerebellar ataxia.
SIGNAL 1 20
PROPEP 21 172
/FTId=PRO_0000008176.
PEPTIDE 175 184 Alpha-neoendorphin.
/FTId=PRO_0000306347.
PEPTIDE 175 183 Beta-neoendorphin.
/FTId=PRO_0000008177.
PEPTIDE 175 179 Leu-enkephalin. {ECO:0000250}.
/FTId=PRO_0000306348.
PROPEP 186 204
/FTId=PRO_0000008178.
PEPTIDE 207 238 Big dynorphin.
/FTId=PRO_0000306349.
PEPTIDE 207 223 Dynorphin A(1-17).
/FTId=PRO_0000008179.
PEPTIDE 207 219 Dynorphin A(1-13). {ECO:0000250}.
/FTId=PRO_0000306350.
PEPTIDE 207 214 Dynorphin A(1-8). {ECO:0000250}.
/FTId=PRO_0000306351.
PEPTIDE 207 211 Leu-enkephalin. {ECO:0000250}.
/FTId=PRO_0000306352.
PEPTIDE 226 254 Leumorphin.
/FTId=PRO_0000008180.
PEPTIDE 226 238 Rimorphin.
/FTId=PRO_0000008181.
PEPTIDE 226 230 Leu-enkephalin.
/FTId=PRO_0000008182.
VARIANT 22 22 C -> Y (in SCA23; dbSNP:rs773876922).
{ECO:0000269|PubMed:23108490}.
/FTId=VAR_072266.
VARIANT 25 25 R -> Q (very rare neutral polymorphism;
dbSNP:rs369559888).
{ECO:0000269|PubMed:23108490}.
/FTId=VAR_072267.
VARIANT 138 138 R -> S (in SCA23; PDYN, dynorphin A and
dynorphin B are located in Purkinje cells
as observed in control cerebellum, but
cerebellar tissue with the mutation has
decreased levels of SLC1A6 and CALB1,
both of which are markers of Purkinje
cells; SLC1A6 accumulates and aggregates
in patient cerebellar tissue;
dbSNP:rs267606941).
{ECO:0000269|PubMed:21035104}.
/FTId=VAR_064913.
VARIANT 206 206 R -> C (in SCA23; dbSNP:rs575606358).
{ECO:0000269|PubMed:23471613}.
/FTId=VAR_072268.
VARIANT 206 206 R -> H (in SCA23; dbSNP:rs1004881058).
{ECO:0000269|PubMed:23471613}.
/FTId=VAR_072269.
VARIANT 211 211 L -> S (in SCA23; the mutant PDYN protein
is produced, but processing to opioid
peptides is dramatically affected, with
increased levels of dynorphin A compared
to dynorphin B; these results suggest
slow conversion of dynorphin A to short
enkephalins; mutant S-211 dynorphin A is
not neurotoxic to cultured striatal
neurons; no effect on membrane property;
dbSNP:rs267606940).
{ECO:0000269|PubMed:21035104,
ECO:0000269|PubMed:21712028}.
/FTId=VAR_064914.
VARIANT 212 212 R -> W (in SCA23; the mutant PDYN protein
is produced, but processing to opioid
peptides is dramatically affected, with
increased levels of dynorphin A compared
to dynorphin B; mutant dynorphin A is
neurotoxic to cultured striatal neurons,
suggesting a dominant-negative effect;
disrupts membrane property;
dbSNP:rs201486601).
{ECO:0000269|PubMed:21035104,
ECO:0000269|PubMed:21712028}.
/FTId=VAR_064915.
VARIANT 215 215 R -> C (in SCA23; the mutant PDYN protein
is produced, but processing to opioid
peptides is dramatically affected,
resulting in an approximately 2-fold
decreased level of dynorphin B compared
to dynorphin A; mutant dynorphin A is
neurotoxic to cultured striatal neurons,
suggesting a dominant-negative effect;
disrupts membrane property;
dbSNP:rs267606939).
{ECO:0000269|PubMed:21035104,
ECO:0000269|PubMed:21712028}.
/FTId=VAR_064916.
VARIANT 227 227 G -> D (in SCA23).
{ECO:0000269|PubMed:23471613}.
/FTId=VAR_072270.
HELIX 211 213 {ECO:0000244|PDB:2N2F}.
SEQUENCE 254 AA; 28385 MW; 783E7D6AC068CE68 CRC64;
MAWQGLVLAA CLLMFPSTTA DCLSRCSLCA VKTQDGPKPI NPLICSLQCQ AALLPSEEWE
RCQSFLSFFT PSTLGLNDKE DLGSKSVGEG PYSELAKLSG SFLKELEKSK FLPSISTKEN
TLSKSLEEKL RGLSDGFREG AESELMRDAQ LNDGAMETGT LYLAEEDPKE QVKRYGGFLR
KYPKRSSEVA GEGDGDSMGH EDLYKRYGGF LRRIRPKLKW DNQKRYGGFL RRQFKVVTRS
QEDPNAYSGE LFDA


Related products :

Catalog number Product name Quantity
D-0911 Dynorphin B (1-9) Rimorphin (1-9), Prepro-Dynorphin (217-225) (guinea pig), Prepro-Dynorphin (221-239) (rat), Prepro-Dynorphin (226-234) (human), Prepro-Dynorphin (228-236) (bovine, porcine) 98 percen 5mg
EIAAB30454 Beta-neoendorphin-dynorphin,PDYN,Pig,Preprodynorphin,Proenkephalin-B,Sus scrofa
EIAAB30455 Beta-neoendorphin-dynorphin,Mouse,Mus musculus,Pdyn,Preprodynorphin,Proenkephalin-B
EIAAB30456 Beta-neoendorphin-dynorphin,Bos taurus,Bovine,PDYN,Preprodynorphin,Proenkephalin-B
EIAAB30457 Beta-neoendorphin-dynorphin,Pdyn,Preprodynorphin,Proenkephalin-B,Rat,Rattus norvegicus
EIAAB30458 Beta-neoendorphin-dynorphin,Homo sapiens,Human,PDYN,Preprodynorphin,Proenkephalin-B
orb60033 Dynorphin A (1-13) Dynorphin A (1-13) Acetate is an acetate salt form of Dynorphin A (1-13) which is an extraordinarily potent opioid peptide and acts on the bradykinin receptor and a major metabolite 5 mg
E-0701-2 Leu-Enkephalin α-Neoendorphin (1-5), Dynorphin A (1-5) 98 percent C28H37N5O7 CAS: 58822-25-6 5mg
021-46 Dynorphin (228_256) _Pro (Dynorphin B 29)(Porcine) _ 200ug 200 µg
E-0701-8 Leu-Enkephalin amide α-Neoendorphin (1-5) amide, Dynorphin A (1-5) amide 98 percent C28H38N6O6 CAS: 5mg
AHP377 RABBIT ANTI DYNORPHIN B (aa1_13), Product Type Polyclonal Antibody, Specificity DYNORPHIN B, Target Species Pig, Host Rabbit, Format Serum, Isotypes Polyclonal IgG, Applications C, R, Clone 0.1 ml
SCH-AHP377 RABBIT ANTI DYNORPHIN B (aa1_13), Product Type Polyclonal Antibody, Specificity DYNORPHIN B, Target Species Pig, Host Rabbit, Format Serum, Isotypes Polyclonal IgG, Applications C, R, Clone 0.1 ml
83335-41-5 dynorphin b dynorphin b 1g
AHP373 RABBIT ANTI HUMAN DYNORPHIN A (aa1_17), Product Type Polyclonal Antibody, Specificity DYNORPHIN A , Target Species Human, Host Rabbit, Format Serum, Isotypes Polyclonal IgG, Applications C, P*, 0.1 ml
SCH-AHP373 RABBIT ANTI HUMAN DYNORPHIN A (aa1_17), Product Type Polyclonal Antibody, Specificity DYNORPHIN A , Target Species Human, Host Rabbit, Format Serum, Isotypes Polyclonal IgG, Applications C, P*, 0.1 ml
orb70614 Pig Dynorphin A (1-12) peptide This is Pig Dynorphin A (1-12) peptide. For research use only. 1 mg
orb70624 Pig Dynorphin A (8-17) peptide This is Pig Dynorphin A (8-17) peptide. For research use only. 1 mg
orb71550 Pig Dynorphin A peptide This is Pig Dynorphin A peptide. For research use only. 1 mg
orb70611 Pig Dynorphin A (1-10) peptide This is Pig Dynorphin A (1-10) peptide. For research use only. 1 mg
orb70626 Dynorphin B (1-9) peptide This is Dynorphin B (1-9) peptide. For research use only. 1 mg
orb71548 Pig Dynorphin (2-17) peptide This is Pig Dynorphin (2-17) peptide. For research use only. 1 mg
orb70620 Pig Dynorphin A (3-8) peptide This is Pig Dynorphin A (3-8) peptide. For research use only. 1 mg
orb70625 Pig Dynorphin A (9-17) peptide This is Pig Dynorphin A (9-17) peptide. For research use only. 1 mg
orb70612 Pig Dynorphin A (1-10) peptide This is Pig Dynorphin A (1-10) peptide. For research use only. 1 mg
orb70623 Pig Dynorphin A (7-17) peptide This is Pig Dynorphin A (7-17) peptide. For research use only. 1 mg


 

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