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Bradykinin-potentiating and C-type natriuretic peptides (Brain BPP-CNP) (bBPP-CNP) (Evasin-CNP) [Cleaved into: Bradykinin-potentiating peptide 13a QQWA (BPP-13a QQWA); Bradykinin-potentiating peptide 13a QWA (BPP-13a QWA); Bradykinin-potentiating peptide 13a (BPP-13a); Bradykinin-potentiating peptide 10c QQWA (BPP-10c QQWA); Bradykinin-potentiating peptide 10c (BPP-10c) (BPP-2) (Evasin-10c); Bradykinin-potentiating peptide 12b (BPP-12b) (Evasin-12b); Bradykinin-potentiating peptide AP; Bradykinin-potentiating peptide APL (BPP-APL); Bradykinin-potentiating peptide 11e (BPP-11e) (Evasin-11e); Bradykinin-potentiating peptide 5a (BPP-5a) (Bradykinin-potentiating peptide Va) (BPPVa) (Evasin-5a) (Proline-rich peptide 5a) (Bj-PRO-5a) (PRO-5a); Poly-His-poly-Gly peptide 1 (pHpG-1); C-type natriuretic peptide (Bj-CNP)]

 BNP2_BOTJA              Reviewed;         265 AA.
Q9PW56; P85167;
03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 2.
22-NOV-2017, entry version 58.
RecName: Full=Bradykinin-potentiating and C-type natriuretic peptides;
AltName: Full=Brain BPP-CNP;
Short=bBPP-CNP;
AltName: Full=Evasin-CNP;
Contains:
RecName: Full=Bradykinin-potentiating peptide 13a+QQWA {ECO:0000303|PubMed:20146532};
Short=BPP-13a+QQWA {ECO:0000303|PubMed:20146532};
Contains:
RecName: Full=Bradykinin-potentiating peptide 13a+QWA {ECO:0000303|PubMed:20146532};
Short=BPP-13a+QWA {ECO:0000303|PubMed:20146532};
Contains:
RecName: Full=Bradykinin-potentiating peptide 13a {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:20146532, ECO:0000303|PubMed:22869554};
Short=BPP-13a {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:20146532, ECO:0000303|PubMed:22869554};
Contains:
RecName: Full=Bradykinin-potentiating peptide 10c+QQWA {ECO:0000303|PubMed:20146532};
Short=BPP-10c+QQWA {ECO:0000303|PubMed:20146532};
Contains:
RecName: Full=Bradykinin-potentiating peptide 10c {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:22869554};
Short=BPP-10c {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:22869554};
Short=BPP-2 {ECO:0000303|PubMed:11994001};
AltName: Full=Evasin-10c {ECO:0000303|PubMed:15922781};
Contains:
RecName: Full=Bradykinin-potentiating peptide 12b {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:22869554};
Short=BPP-12b {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:22869554};
AltName: Full=Evasin-12b {ECO:0000303|PubMed:15922781};
Contains:
RecName: Full=Bradykinin-potentiating peptide AP {ECO:0000303|PubMed:20146532, ECO:0000303|PubMed:22869554};
Contains:
RecName: Full=Bradykinin-potentiating peptide APL {ECO:0000303|PubMed:20146532};
Short=BPP-APL;
Contains:
RecName: Full=Bradykinin-potentiating peptide 11e {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:22869554};
Short=BPP-11e {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:22869554};
AltName: Full=Evasin-11e {ECO:0000303|PubMed:15922781};
Contains:
RecName: Full=Bradykinin-potentiating peptide 5a {ECO:0000303|PubMed:15245866};
Short=BPP-5a {ECO:0000303|PubMed:15245866};
AltName: Full=Bradykinin-potentiating peptide Va {ECO:0000250|UniProtKB:Q6LEM5};
Short=BPPVa {ECO:0000250|UniProtKB:Q6LEM5};
AltName: Full=Evasin-5a {ECO:0000303|PubMed:15922781};
AltName: Full=Proline-rich peptide 5a {ECO:0000303|PubMed:21185808};
Short=Bj-PRO-5a {ECO:0000303|PubMed:21185808};
Short=PRO-5a {ECO:0000303|PubMed:21185808};
Contains:
RecName: Full=Poly-His-poly-Gly peptide 1 {ECO:0000303|PubMed:22869554};
Short=pHpG-1 {ECO:0000303|PubMed:22869554};
Contains:
RecName: Full=C-type natriuretic peptide;
AltName: Full=Bj-CNP;
Flags: Precursor;
Bothrops jararaca (Jararaca) (Bothrops jajaraca).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
NCBI_TaxID=8724;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=12716428;
Hayashi M.A.F., Murbach A.F., Ianzer D., Portaro F.C.V., Prezoto B.C.,
Fernandes B.L., Silveira P.F., Silva C.A., Pires R.S., Britto L.R.G.,
Dive V., Camargo A.C.M.;
"The C-type natriuretic peptide precursor of snake brain contains
highly specific inhibitors of the angiotensin-converting enzyme.";
J. Neurochem. 85:969-977(2003).
[2]
PROTEIN SEQUENCE OF 31-43; 51-63; 71-80; 88-99; 107-117; 107-119 AND
216-234 (BPP-10C; BPP-11E; BPP-12B; BPP-13A; BPP-AP AND PHPG-1),
SYNTHESIS OF 71-80 (BPP-10C), FUNCTION, PYROGLUTAMATE FORMATION AT
GLN-31; GLN-51; GLN-71; GLN-88 AND GLN-107, AND MASS SPECTROMETRY.
TISSUE=Venom;
PubMed=22869554; DOI=10.1074/mcp.M112.019331;
Tashima A.K., Zelanis A., Kitano E.S., Ianzer D., Melo R.L., Rioli V.,
Sant'anna S.S., Schenberg A.C., Camargo A.C., Serrano S.M.T.;
"Peptidomics of three Bothrops snake venoms: insights into the
molecular diversification of proteomes and peptidomes.";
Mol. Cell. Proteomics 11:1245-1262(2012).
[3]
PROTEIN SEQUENCE OF 27-43; 28-43; 31-43; 47-63; 48-63; 51-63; 67-80;
107-119 AND 107-120 (BPP-13A+QQWA; BPP-13A+QWA; BPP-13A; BPP-10C+QQWA;
BPP-AP AND BPP-APL), PYROGLUTAMATE FORMATION AT GLN-27; GLN-28;
GLN-31; GLN-47; GLN-48; GLN-51; GLN-67 AND GLN-107, DEVELOPMENTAL
STAGE, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Venom;
PubMed=20146532; DOI=10.1021/pr901027r;
Zelanis A., Tashima A.K., Rocha M.M., Furtado M.F., Camargo A.C.,
Ho P.L., Serrano S.M.;
"Analysis of the ontogenetic variation in the venom proteome/peptidome
of Bothrops jararaca reveals different strategies to deal with prey.";
J. Proteome Res. 9:2278-2291(2010).
[4]
PROTEIN SEQUENCE OF 31-43; 51-63; 71-80; 88-99; 107-117; 121-125 AND
127-131 (BPP-13A; BPP-10C; BPP-12B; BPP11E AND BPP-5A), FUNCTION,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND
PYROGLUTAMATE FORMATION AT GLN-31; GLN-51; GLN-71; GLN-88; GLN-107;
GLN-121 AND GLN-127.
TISSUE=Venom;
PubMed=15245866; DOI=10.1016/j.peptides.2004.04.006;
Ianzer D., Konno K., Marques-Porto R., Portaro F.C.V., Stoecklin R.,
de Camargo A.C.M., Pimenta D.C.;
"Identification of five new bradykinin potentiating peptides (BPPs)
from Bothrops jararaca crude venom by using electrospray ionization
tandem mass spectrometry after a two-step liquid chromatography.";
Peptides 25:1085-1092(2004).
[5]
SYNTHESIS OF 71-80, AND FUNCTION.
PubMed=11994001; DOI=10.1021/bi012121x;
Cotton J., Hayashi M.A., Cuniasse P., Vazeux G., Ianzer D.,
De Camargo A.C., Dive V.;
"Selective inhibition of the C-domain of angiotensin I converting
enzyme by bradykinin potentiating peptides.";
Biochemistry 41:6065-6071(2002).
[6]
FUNCTION BPP-10C.
PubMed=17475904; DOI=10.1124/jpet.107.120873;
Ianzer D., Santos R.A., Etelvino G.M., Xavier C.H.,
de Almeida Santos J., Mendes E.P., Machado L.T., Prezoto B.C.,
Dive V., de Camargo A.C.;
"Do the cardiovascular effects of angiotensin-converting enzyme (ACE)
I involve ACE-independent mechanisms? new insights from proline-rich
peptides of Bothrops jararaca.";
J. Pharmacol. Exp. Ther. 322:795-805(2007).
[7]
FUNCTION, BIOASSAY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-74;
PRO-76; ILE-78; PRO-79 AND PRO-80.
PubMed=19491403; DOI=10.1074/jbc.M109.021089;
Guerreiro J.R., Lameu C., Oliveira E.F., Klitzke C.F., Melo R.L.,
Linares E., Augusto O., Fox J.W., Lebrun I., Serrano S.M.,
Camargo A.C.;
"Argininosuccinate synthetase is a functional target for a snake venom
anti-hypertensive peptide: role in arginine and nitric oxide
production.";
J. Biol. Chem. 284:20022-20033(2009).
[8]
SYNTHESIS OF 121-125 AND 127-131 (BBP-5A), AND FUNCTION.
PubMed=21185808; DOI=10.1016/j.bcp.2010.12.016;
Morais K.L., Hayashi M.A., Bruni F.M., Lopes-Ferreira M.,
Camargo A.C., Ulrich H., Lameu C.;
"Bj-PRO-5a, a natural angiotensin-converting enzyme inhibitor,
promotes vasodilatation mediated by both bradykinin B(2)and M1
muscarinic acetylcholine receptors.";
Biochem. Pharmacol. 81:736-742(2011).
[9]
REVIEW, AND FUNCTION.
PubMed=15922781; DOI=10.1016/j.toxicon.2005.02.017;
Hayashi M.A., Camargo A.C.;
"The bradykinin-potentiating peptides from venom gland and brain of
Bothrops jararaca contain highly site specific inhibitors of the
somatic angiotensin-converting enzyme.";
Toxicon 45:1163-1170(2005).
-!- FUNCTION: Bradykinin-potentiating peptide 5a: modestly inhibits
ACE (with highest affinity for the N-site) and reveals strong
bradykinin-potentiating activity. Induces nitric oxide (NO)
production depended on muscarinic acetylcholine receptor M1
subtype (CHRM1) and bradykinin B2 receptor (BDKRB2) activation.
Both these receptors contribute to the vasodilation induced by
this peptide that may have an indirect action on BDKRB2 and a
direct agonistic action on CHRM1.
-!- FUNCTION: Bradykinin-potentiating peptide 10c: peptide with
several activities. It inhibits the activity of the angiotensin-
converting enzyme (ACE) by a preferential interaction with its C-
domain (PubMed:11994001). It evokes transient hypotension (-14
mmHg) similar to that evoked by 0,5 ug of bradykinin, when
injected alone into rats. It has a high bradykinin-potentiating
effect (120%), when 60 nmol of BPP-10c are coinjected with 0.5 ug
of bradykinin into rats (PubMed:22869554). Does not affect
angiotensin-1 pressor effects. Shows potent and long-lasting
antihypertensive activity as well as a reduction of the heart rate
(PubMed:17475904). It also binds and dose-dependently promotes the
activation of cytosolic argininosuccinate synthase (ASS1), an
enzyme that catalyzes the conversion of citrulline, L-aspartate
and ATP to argininosuccinate, AMP and pyrophosphate. It also
enhances ASS1-dependent arginine production in HEK 293 cells, as
well as in spontaneous hypertensive rat (SHR) and Wistar rat
plasma. In addition, it induces the production of nitric-oxide
(NO) by HUVEC cells via the endothelial nitric-oxide synthase
(NOS3), which use arginine as a substrate and produce NO. It has
been shown to be internalized by ASS1-expressing endothelial
(HUVEC) and kidney (HEK 293) cells, and is detected homogenously
distributed within the cell cytoplasm for up to 2 hours
(PubMed:19491403). {ECO:0000269|PubMed:11994001,
ECO:0000269|PubMed:17475904, ECO:0000269|PubMed:19491403,
ECO:0000269|PubMed:22869554}.
-!- FUNCTION: Poly-His-poly-Gly peptide 1: may serve as a
metalloproteinase inhibitor during glandular storage. Their
inhibition may be instantly disengaged, by dilution or
physiochemical change, when venom is injected into tissue of the
victim. {ECO:0000250|UniProtKB:A8YPR6}.
-!- FUNCTION: Natriuretic peptide exhibits natriuretic and
vasodepressor activity. Acts by stimulating cGMP. {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Secreted. Cytoplasm, cytosol. Note=BPP-10c
is internalized in the cytosol of prey cells.
-!- TISSUE SPECIFICITY: Adult brain regions; ventromedial
hypothalamus, paraventricular nucleus, paraventricular organ, and
the subcommissural organ. Also expressed by the venom gland.
{ECO:0000269|PubMed:12716428, ECO:0000269|PubMed:15245866}.
-!- DEVELOPMENTAL STAGE: BPP-10a, BPP-10c+QQWA, BPP-AP, BPP-13A, BPP-
13a+QWA and BPP-13a+QQWA seem to be found in both adult and
newborn B.jararaca venoms, whereas BPP-APL seem to be only present
in newborn venom. {ECO:0000269|PubMed:20146532}.
-!- MASS SPECTROMETRY: Mass=1195.6; Method=Electrospray; Range=71-80;
Note=BPP-10c.; Evidence={ECO:0000269|PubMed:22869554};
-!- MASS SPECTROMETRY: Mass=1189.4; Method=Electrospray; Range=107-
117; Evidence={ECO:0000269|PubMed:15245866};
-!- MASS SPECTROMETRY: Mass=1188.7; Method=Electrospray; Range=107-
117; Note=BPP-11e.; Evidence={ECO:0000269|PubMed:22869554};
-!- MASS SPECTROMETRY: Mass=1356.5; Method=Electrospray; Range=107-
119; Note=BPP-AP.; Evidence={ECO:0000269|PubMed:22869554};
-!- MASS SPECTROMETRY: Mass=1280.7; Method=Electrospray; Range=88-99;
Note=BPP-12b.; Evidence={ECO:0000269|PubMed:22869554};
-!- MASS SPECTROMETRY: Mass=1563.7; Method=Electrospray; Range=216-
234; Note=pHpG-1.; Evidence={ECO:0000269|PubMed:22869554};
-!- MISCELLANEOUS: The name evasin stands for "Endogenous
VASopeptidase INhibitors" and is given to endogenous brain
proteins in order to distinguish them from venom proteins.
{ECO:0000305|PubMed:15922781}.
-!- MISCELLANEOUS: A BPP-13a without the two first amino acids has
been detected. {ECO:0000305|PubMed:20146532}.
-!- SIMILARITY: In the N-terminal section; belongs to the bradykinin-
potentiating peptide family. {ECO:0000305}.
-!- SIMILARITY: In the central section; belongs to the pHpG family.
{ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the natriuretic
peptide family. {ECO:0000255}.
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EMBL; AF171670; AAD51326.2; -; mRNA.
SMR; Q9PW56; -.
TCDB; 1.C.46.1.2; the c-type natriuretic peptide (cnp) family.
HOVERGEN; HBG073115; -.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005179; F:hormone activity; IEA:InterPro.
GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0060422; F:peptidyl-dipeptidase inhibitor activity; IDA:UniProtKB.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0045776; P:negative regulation of blood pressure; IDA:UniProtKB.
GO; GO:0006469; P:negative regulation of protein kinase activity; NAS:UniProtKB.
GO; GO:0050880; P:regulation of blood vessel size; IDA:UniProtKB.
GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
InterPro; IPR000663; Natr_peptide.
InterPro; IPR030480; Natr_peptide_CS.
Pfam; PF00212; ANP; 1.
SMART; SM00183; NAT_PEP; 1.
PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
1: Evidence at protein level;
Cleavage on pair of basic residues; Cytoplasm;
Direct protein sequencing; Disulfide bond;
G-protein coupled receptor impairing toxin; Hypotensive agent;
Metalloenzyme inhibitor; Metalloprotease inhibitor;
Protease inhibitor; Pyrrolidone carboxylic acid; Secreted; Signal;
Toxin; Vasoactive; Vasodilator.
SIGNAL 1 23 {ECO:0000255}.
PROPEP 24 26 {ECO:0000269|PubMed:20146532}.
/FTId=PRO_0000252066.
PEPTIDE 27 43 Bradykinin-potentiating peptide 13a+QQWA.
{ECO:0000269|PubMed:20146532}.
/FTId=PRO_0000422964.
PEPTIDE 28 43 Bradykinin-potentiating peptide 13a+QWA.
{ECO:0000269|PubMed:20146532}.
/FTId=PRO_0000422965.
PEPTIDE 31 43 Bradykinin-potentiating peptide 13a.
{ECO:0000269|PubMed:15245866,
ECO:0000269|PubMed:20146532,
ECO:0000269|PubMed:22869554}.
/FTId=PRO_0000252067.
PROPEP 44 46 {ECO:0000305}.
/FTId=PRO_0000252068.
PEPTIDE 47 63 Bradykinin-potentiating peptide 13a+QQWA.
{ECO:0000269|PubMed:20146532}.
/FTId=PRO_0000422966.
PEPTIDE 48 63 Bradykinin-potentiating peptide 13a+QWA.
{ECO:0000269|PubMed:20146532}.
/FTId=PRO_0000422967.
PEPTIDE 51 63 Bradykinin-potentiating peptide 13a.
{ECO:0000269|PubMed:15245866,
ECO:0000269|PubMed:20146532,
ECO:0000269|PubMed:22869554}.
/FTId=PRO_0000252069.
PROPEP 64 66 {ECO:0000305}.
/FTId=PRO_0000252070.
PEPTIDE 67 80 Bradykinin-potentiating peptide 10c+QQWA.
{ECO:0000269|PubMed:20146532}.
/FTId=PRO_0000422968.
PEPTIDE 71 80 Bradykinin-potentiating peptide 10c.
{ECO:0000269|PubMed:15245866,
ECO:0000269|PubMed:22869554}.
/FTId=PRO_0000252071.
PROPEP 81 87 {ECO:0000305}.
/FTId=PRO_0000252072.
PEPTIDE 88 99 Bradykinin-potentiating peptide 12b.
{ECO:0000269|PubMed:15245866,
ECO:0000269|PubMed:22869554}.
/FTId=PRO_0000252073.
PROPEP 100 106 {ECO:0000305}.
/FTId=PRO_0000252074.
PEPTIDE 107 120 Bradykinin-potentiating peptide APL.
{ECO:0000269|PubMed:20146532,
ECO:0000269|PubMed:22869554}.
/FTId=PRO_0000422969.
PEPTIDE 107 119 Bradykinin-potentiating peptide AP.
{ECO:0000269|PubMed:20146532}.
/FTId=PRO_0000421889.
PEPTIDE 107 117 Bradykinin-potentiating peptide 11e.
{ECO:0000269|PubMed:15245866,
ECO:0000269|PubMed:22869554}.
/FTId=PRO_0000252075.
PROPEP 118 120 {ECO:0000305}.
/FTId=PRO_0000252076.
PEPTIDE 121 125 Bradykinin-potentiating peptide 5a.
{ECO:0000269|PubMed:15245866}.
/FTId=PRO_0000252077.
PROPEP 126 126 {ECO:0000305}.
/FTId=PRO_0000252078.
PEPTIDE 127 131 Bradykinin-potentiating peptide 5a.
{ECO:0000269|PubMed:15245866}.
/FTId=PRO_0000252079.
PROPEP 132 215 {ECO:0000305}.
/FTId=PRO_0000252080.
PEPTIDE 216 234 Poly-His-poly-Gly peptide 1.
{ECO:0000269|PubMed:22869554}.
/FTId=PRO_0000421890.
PROPEP 235 243 {ECO:0000305}.
/FTId=PRO_0000421891.
PEPTIDE 244 265 C-type natriuretic peptide.
/FTId=PRO_0000252081.
COMPBIAS 35 139 Pro-rich. {ECO:0000255}.
COMPBIAS 224 264 Gly-rich. {ECO:0000255}.
MOD_RES 27 27 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:20146532}.
MOD_RES 28 28 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:20146532}.
MOD_RES 31 31 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:15245866,
ECO:0000269|PubMed:20146532,
ECO:0000269|PubMed:22869554}.
MOD_RES 47 47 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:20146532}.
MOD_RES 48 48 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:20146532}.
MOD_RES 51 51 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:15245866,
ECO:0000269|PubMed:20146532,
ECO:0000269|PubMed:22869554}.
MOD_RES 67 67 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:20146532}.
MOD_RES 71 71 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:15245866,
ECO:0000269|PubMed:22869554}.
MOD_RES 88 88 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:15245866,
ECO:0000269|PubMed:22869554}.
MOD_RES 107 107 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:15245866,
ECO:0000269|PubMed:20146532,
ECO:0000269|PubMed:22869554}.
MOD_RES 121 121 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:15245866}.
MOD_RES 127 127 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:15245866}.
DISULFID 249 265 {ECO:0000250|UniProtKB:P23582}.
MUTAGEN 74 74 P->A: Low decrease in ability to enhance
AsS activity.
{ECO:0000269|PubMed:19491403}.
MUTAGEN 76 76 P->A: Low decrease in ability to enhance
AsS activity.
{ECO:0000269|PubMed:19491403}.
MUTAGEN 78 78 I->A: Low decrease in ability to enhance
AsS activity.
{ECO:0000269|PubMed:19491403}.
MUTAGEN 79 79 P->A: Important decrease in ability to
enhance AsS activity.
{ECO:0000269|PubMed:19491403}.
MUTAGEN 80 80 P->A: Important decrease in ability to
enhance AsS activity.
{ECO:0000269|PubMed:19491403}.
SEQUENCE 265 AA; 27763 MW; 8E99AEC976CCD439 CRC64;
MVLSRLAASG LLLLALLALS VDGKPVQQWA QGGWPRPGPE IPPLKVQQWA QGGWPRPGPE
IPPLTVQQWA QNWPHPQIPP LTVQQWAQWG RPPGPPIPPL TVQQWAQARP PHPPIPPAPL
QKWAPVQKWA PLLQPHESPA SGTTALREEL SLGPEAASGV PSAGAEVGRS GSKAPAAPHR
LSKSKGAAAT SAASRPMRDL RPDGKQARQN WGRMVHHDHH AAVGGGGGGG GGGARRLKGL
AKKGAAKGCF GLKVDRIGTM SGLGC


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orb70482 Bradykinin peptide This is Bradykinin peptide. For research use only. 1 mg
T-0513 TRH-Potentiating Peptide 98 percent C54H75N11O18S CAS: 122018-91-1 5mg
29-643 BDKRB2 is a receptor for bradykinin. The 9 aa bradykinin peptide elicits many responses including vasodilation, edema, smooth muscle spasm and pain fiber stimulation. This receptor associates with G p 0.1 mg
orb70514 Bradykinin Potentiator B peptide This is Bradykinin Potentiator B peptide. For research use only. 1 mg
orb70515 Bradykinin Potentiator C peptide This is Bradykinin Potentiator C peptide. For research use only. 1 mg
orb70158 [Des-Pro2]-Bradykinin peptide This is [Des-Pro2]-Bradykinin peptide. For research use only. 1 mg
orb70834 Lys-(Des-Arg9)-Bradykinin peptide This is Lys-(Des-Arg9)-Bradykinin peptide. For research use only. 1 mg
orb70837 Lys-(Tyr8)-Bradykinin peptide This is Lys-(Tyr8)-Bradykinin peptide. For research use only. 1 mg
orb70237 [Thr6]-Bradykinin peptide This is [Thr6]-Bradykinin peptide. For research use only. 1 mg
orb70833 Lys-(Ala3)-Bradykinin peptide This is Lys-(Ala3)-Bradykinin peptide. For research use only. 1 mg
orb70836 Lys-(Hyp3)-Bradykinin peptide This is Lys-(Hyp3)-Bradykinin peptide. For research use only. 1 mg
orb70263 [Tyr8]-Bradykinin peptide This is [Tyr8]-Bradykinin peptide. For research use only. 1 mg
orb70182 [Ile-Ser]-Bradykinin (T-Kinin) peptide This is [Ile-Ser]-Bradykinin (T-Kinin) peptide. For research use only. 1 mg


 

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