SCP0023
ANP 126-150 rat /Auriculin B, ANP 4-28 rat
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About This Item
Formula empirica (notazione di Hill):
C113H179N39O35S2
Peso molecolare:
2708.00
Codice UNSPSC:
51111800
NACRES:
NA.32
Saggio
≥95% (HPLC)
Forma fisica
lyophilized
Composizione
Peptide Content, ≥70%
Condizioni di stoccaggio
protect from light
Temperatura di conservazione
−20°C
Amino Acid Sequence
Arg-Ser-Ser-Cys-Phe-Gly-Gly-Arg-Ile-Asp-Arg-Ile-Gly-Ala-Gln-Ser-Gly-Leu-Gly-Cys-Asn-Ser-Phe-Arg-Tyr
Applicazioni
Atrial natriuretic peptide(s) (ANP) (Atriopeptin) are peptide hormones that regulate vasodilation. The ANP fragment Atriopeptin III (ANP 126-150) is used to study the regulation of Na+/H+ exchange mediated in erythrocytes by cGMP/guanylate-cyclase activity.
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Certificati d'analisi (COA)
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J Nortier et al.
Peptides, 14(2), 405-408 (1993-03-01)
Incubation of rANP(5-28)--also called atriopeptin III (AP III)--with purified endopeptidase 24.11 led preferentially to the production of Phe-Arg-Tyr, while other products of minor importance were detected. One of these was identified as rANP(5-25) (atriopeptin I) (AP I). This hydrolysis pattern
B M Schmitt et al.
Clinical and experimental pharmacology & physiology, 24(2), 131-138 (1997-02-01)
1. In mammalian plasma, many different inhibitors of Na+/K(+)-ATPase are present, but it is not clear whether their net effect on NA+/K(+)-ATPase activity changes during the regulation of electrolyte and fluid balance. We studied Na+/K(+)-ATPase inhibition by plasma extracts in
V Petrov et al.
European journal of biochemistry, 221(1), 195-199 (1994-04-01)
Human atrial natriuretic peptide (ANP) fragments ANP-(127-150) or ANP-III and ANP-(127-149) or ANP-II activate Na+/H+ exchange in human erythrocytes at concentrations as low as 1 pM. Both ANP-(127-147) or ANP-I and ANP-(129-150) or des-Ser5, Ser6-ANP-III have no effect on erythrocyte
V Petrov et al.
The American journal of physiology, 271(5 Pt 1), C1556-C1564 (1996-11-01)
Guanylate cyclase activity in human erythrocytes is investigated by evaluating the intracellular guanosine 3',5'-cyclic monophosphate (cGMP) content in the presence of various agents that exert specific effects on soluble or particulate guanylate cyclase. The increase in the intraerythrocyte cGMP content
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