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Prepro-Atrial Natriuretic Factor (56-92) (human)

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Prepro-Atrial Natriuretic Factor (56-92) (human) is used to raise antibodies.

Category

Others

Catalog number

BAT-015257

CAS number

112199-06-1

Molecular Formula

C173H270N44O57

Molecular Weight

3878.26

Prepro-Atrial Natriuretic Factor (56-92) (human)

Specification
Reference Reading

IUPAC Name

(4S)-4-amino-5-[[(2S)-1-[[(2S)-1-[(2S)-2-[(2S)-2-[[(2S)-5-amino-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[(2S)-2-[[(2S)-4-amino-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[2-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[(2S)-2-[[(2S)-1-[(2S)-2-[[(2S)-1-[[(2S)-1-[(2S)-2-[(2S)-2-[[(2S)-1-[[(2S,3R)-1-[[2-[[(2S)-1-[[(2S)-1-[[(2S)-1-[(2S)-2-[[(2S)-1-[[(2S)-5-amino-1-[[(1S)-4-carbamimidamido-1-carboxybutyl]amino]-1,5-dioxopentan-2-yl]amino]-1-oxopropan-2-yl]carbamoyl]pyrrolidin-1-yl]-3-hydroxy-1-oxopropan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-2-oxoethyl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]carbamoyl]pyrrolidine-1-carbonyl]pyrrolidin-1-yl]-3-methyl-1-oxobutan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]carbamoyl]pyrrolidin-1-yl]-4-methyl-1-oxopentan-2-yl]carbamoyl]pyrrolidin-1-yl]-3-hydroxy-1-oxopropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-2-oxoethyl]amino]-1-oxopropan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-1,4-dioxobutan-2-yl]carbamoyl]pyrrolidin-1-yl]-4-carboxy-1-oxobutan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-1,5-dioxopentan-2-yl]carbamoyl]pyrrolidine-1-carbonyl]pyrrolidin-1-yl]-3-methyl-1-oxobutan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-5-oxopentanoic acid

Synonyms

NT-pro-ANP (human) (31-67); H-Glu-Val-Val-Pro-Pro-Gln-Val-Leu-Ser-Glu-Pro-Asn-Glu-Glu-Ala-Gly-Ala-Ala-Leu-Ser-Pro-Leu-Pro-Glu-Val-Pro-Pro-Trp-Thr-Gly-Glu-Val-Ser-Pro-Ala-Gln-Arg-OH; L-alpha-glutamyl-L-valyl-L-valyl-L-prolyl-L-prolyl-L-glutaminyl-L-valyl-L-leucyl-L-seryl-L-alpha-glutamyl-L-prolyl-L-asparagyl-L-alpha-glutamyl-L-alpha-glutamyl-L-alanyl-glycyl-L-alanyl-L-alanyl-L-leucyl-L-seryl-L-prolyl-L-leucyl-L-prolyl-L-alpha-glutamyl-L-valyl-L-prolyl-L-prolyl-L-tryptophyl-L-threonyl-glycyl-L-alpha-glutamyl-L-valyl-L-seryl-L-prolyl-L-alanyl-L-glutaminyl-L-arginine

Appearance

White Powder

Purity

95%

Sequence

EVVPPQVLSEPNEEAGAALSPLPEVPPWTGEVSPAQR

Storage

Store at -20°C

Solubility

Soluble in Water

InChI

InChI=1S/C173H270N44O57/c1-80(2)69-105(196-141(242)90(19)185-139(240)89(18)184-124(225)75-182-138(239)88(17)186-143(244)100(48-56-128(231)232)190-144(245)101(49-57-129(233)234)191-151(252)108(73-123(177)224)198-157(258)115-38-26-61-210(115)164(265)103(51-59-131(237)238)194-153(254)110(77-218)201-149(250)106(70-81(3)4)199-161(262)132(83(7)8)206-147(248)99(46-53-122(176)223)192-156(257)117-40-29-65-214(117)168(269)120-43-32-68-217(120)171(272)136(87(15)16)208-163(264)134(85(11)12)204-142(243)95(174)44-54-126(227)228)150(251)202-111(78-219)166(267)213-64-28-39-116(213)159(260)200-109(71-82(5)6)165(266)211-62-27-37-114(211)155(256)193-102(50-58-130(235)236)148(249)207-135(86(13)14)170(271)216-67-31-42-119(216)169(270)215-66-30-41-118(215)158(259)197-107(72-93-74-181-96-34-23-22-33-94(93)96)152(253)209-137(92(21)221)160(261)183-76-125(226)188-97(47-55-127(229)230)146(247)205-133(84(9)10)162(263)203-112(79-220)167(268)212-63-25-36-113(212)154(255)187-91(20)140(241)189-98(45-52-121(175)222)145(246)195-104(172(273)274)35-24-60-180-173(178)179/h22-23,33-34,74,80-92,95,97-120,132-137,181,218-221H,24-32,35-73,75-79,174H2,1-21H3,(H2,175,222)(H2,176,223)(H2,177,224)(H,182,239)(H,183,261)(H,184,225)(H,185,240)(H,186,244)(H,187,255)(H,188,226)(H,189,241)(H,190,245)(H,191,252)(H,192,257)(H,193,256)(H,194,254)(H,195,246)(H,196,242)(H,197,259)(H,198,258)(H,199,262)(H,200,260)(H,201,250)(H,202,251)(H,203,263)(H,204,243)(H,205,247)(H,206,248)(H,207,249)(H,208,264)(H,209,253)(H,227,228)(H,229,230)(H,231,232)(H,233,234)(H,235,236)(H,237,238)(H,273,274)(H4,178,179,180)/t88-,89-,90-,91-,92+,95-,97-,98-,99-,100-,101-,102-,103-,104-,105-,106-,107-,108-,109-,110-,111-,112-,113-,114-,115-,116-,117-,118-,119-,120-,132-,133-,134-,135-,136-,137-/m0/s1

InChI Key

IMNAEOZBAKUDSB-YYYBCFRQSA-N

Canonical SMILES

CC(C)CC(C(=O)NC(CO)C(=O)N1CCCC1C(=O)NC(CC(C)C)C(=O)N2CCCC2C(=O)NC(CCC(=O)O)C(=O)NC(C(C)C)C(=O)N3CCCC3C(=O)N4CCCC4C(=O)NC(CC5=CNC6=CC=CC=C65)C(=O)NC(C(C)O)C(=O)NCC(=O)NC(CCC(=O)O)C(=O)NC(C(C)C)C(=O)NC(CO)C(=O)N7CCCC7C(=O)NC(C)C(=O)NC(CCC(=O)N)C(=O)NC(CCCNC(=N)N)C(=O)O)NC(=O)C(C)NC(=O)C(C)NC(=O)CNC(=O)C(C)NC(=O)C(CCC(=O)O)NC(=O)C(CCC(=O)O)NC(=O)C(CC(=O)N)NC(=O)C8CCCN8C(=O)C(CCC(=O)O)NC(=O)C(CO)NC(=O)C(CC(C)C)NC(=O)C(C(C)C)NC(=O)C(CCC(=O)N)NC(=O)C9CCCN9C(=O)C1CCCN1C(=O)C(C(C)C)NC(=O)C(C(C)C)NC(=O)C(CCC(=O)O)N

1. Kaliuretic peptide: the most potent inhibitor of Na(+)-K+ ATPase of the atrial natriuretic peptides

S Chiou, D L Vesely Endocrinology. 1995 May;136(5):2033-9. doi: 10.1210/endo.136.5.7720651.

The present investigation was designed to determine whether atrial natriuretic peptides consisting of amino acids 1-30 (i.e. long-acting natriuretic peptide), 31-67 (vessel dilator), 79-98 (kaliuretic peptide), and 99-126 [atrial natriuretic factor (ANF)] of the 126 amino acid ANF prohormone inhibit sodium-potassium-ATPase as part of their mechanism(s) of action for producing a natriuresis and/or kaliuresis. Kaliuretic peptide, long-acting natriuretic peptide, vessel dilator and ANF at their 10(-11) M concentrations inhibited Na(+)-K(+)-ATPase 39.5%, 27.8%, 19.2%, and 4% respectively, in bovine renal medulla, whereas their inhibition in renal cortical membranes was 37.5%, 27.5%, 20%, and 0%, respectively. Ouabain (0.5 mM) inhibited kidney medullary Na(+)-K(+)-ATPase 45% and in the cortex, 38%. There was no additive effect of any of these peptides with ouabain suggesting that they are interacting with the same site on the Na(+)-K(+)-ATPase as ouabain. To help elucidate the mechanism of these peptides' interaction with Na(+)-K(+)-ATPase, naproxen (0.5 mM), an inhibitor of prostaglandin synthesis, and direct measurement of prostaglandin E2 by RIA were used. Naproxen completely blocked the inhibition of Na(+)-K(+)-ATPase by kaliuretic peptide, long-acting natriuretic peptide, and vessel dilator suggesting that their inhibition of Na(+)-K(+)-ATPase in both the kidney medulla and cortex are mediated by prostaglandins. Direct measurement of prostaglandin E2 revealed that kaliuretic peptide > long-acting natriuretic peptide > vessel dilator increased prostaglandin E2 synthesis, whereas ANF did not have any effect. Of interest, angiotensin II and ouabain inhibition of Na(+)-K(+)-ATPase were also completely blocked by naproxen.

2. Peptides from the N-terminus of the atrial natriuretic factor prohormone enhance guanylate cyclase activity and increase cyclic GMP levels in a wide variety of tissues

D L Vesely Mol Cell Biochem. 1992 Jan 15;109(1):43-50. doi: 10.1007/BF00230872.

The 98 amino acid (a.a.) N-terminus of the 126 a.a. atrial natriuretic factor (ANF) prohormone contains three peptides consisting of a.a. 1-30 (proANF 1-30), a.a. 31-67 (proANF 31-67) and a.a. 79-98 (proANF 79-98) with blood pressure lowering, sodium and/or potassium excreting properties similar to atrial natriuretic factor (a.a. 99-126, C-terminus of prohormone). ProANF 1-30 and proANF 31-67 have separate and distinct receptors from ANF in both vasculature and in the kidney to help mediate the above effects. At the cellular level proANFs 1-30, 31-67, and 79-98 as well as ANF's effects are mediated by enhancement of the guanylate cyclase (EC 4.6.1.2)-cyclic GMP system in vasculature and in the kidney. These peptides from the N-terminus of the ANF prohormone circulate normally in man and in all animal species tested. The object of the present investigation was to determine if these peptides have the ability to enhance either guanylate cyclase and/or adenylate cyclase in a variety of other tissues in addition to kidney and vasculature. ProANF 1-30, proANF 31-67, proANF 79-98, and ANF all increased rat lung, liver, heart and testes, but not spleen, particulate guanylate cyclase 2- to 3-fold at their 100 nM concentrations. Dose response curves revealed that maximal stimulation of particulate guanylate cyclase activity by these newly discovered peptides was at their 1 microM concentrations, with no further increase in activity above their 1 microM concentrations.(ABSTRACT TRUNCATED AT 250 WORDS)

3. Evidence for particulate guanylate cyclase in rat kidney after stimulation by atrial natriuretic factor. An ultracytochemical study

M G Rambotti, C Saccardi, A Spreca Histochem J. 1990 Sep;22(9):469-74. doi: 10.1007/BF01007230.

Cytochemical localization of particulate guanylate cyclase (GC) in rat kidney, after stimulation with atrial natriuretic factor (ANF), was studied by electron microscopy. In the renal corpuscle GC reaction was localized on podocytes. Other segments of the nephron that showed ultracytochemical evidence of GC activity were the proximal convoluted tubule, the thick ascending limb of the loop of Henle and the collecting tubule. All GC positivity was associated with plasma membranes. Samples incubated in basal conditions (without ANF) did not reveal any GC reaction product. These results indicate that ANF is a strong activator of particulate GC. Our data also suggests that, through the enzyme, ANF acts directly on epithelial cells of tubules where Na+ reabsorption occurs. This is in agreement with the hypothesis that ANF has a direct tubular effect on natriuresis.