Nogo-66 (1-40)

Nogo-66 (1-40) acts as a competitive antagonist at the Nogo-66 receptor (NgR) that blocks Nogo-66- and CNS myelin-induced inhibition of axonal growth, but does not reduce myelin-associated glycoprotein (MAG) inhibition of neurite outgrowth in vitro. It promotes neuron regeneration

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.
Nogo-66 (1-40)(CAS 475221-20-6)

CAT No: R0822

CAS No:475221-20-6

Synonyms/Alias:NEP1-40;RIYKGVIQAI QKSDEGHPFR AYLESEVAIS EELVQKYSNS;475221-20-6;AC-RIYKGVIQAIQKSDEGHPFRAYLESEVAISEELVQKYSNS-NH2;AKOS034831548;PD079236;

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M.F/Formula
C206H324N56O65
M.W/Mr.
4625
Sequence
One Letter Code:RXYKGVXQAXQKSDEGHPFRAYLESEVAXSEELVQKYSNS
Three Letter Code:Ac-DL-Arg-DL-xiIle-DL-Tyr-DL-Lys-Gly-DL-Val-DL-xiIle-DL-Gln-DL-Ala-DL-xiIle-DL-Gln-DL-Lys-DL-Ser-DL-Asp-DL-Glu-Gly-DL-His-DL-Pro-DL-Phe-DL-Arg-DL-Ala-DL-Tyr-DL-Leu-DL-Glu-DL-Ser-DL-Glu-DL-Val-DL-Ala-DL-xiIle-DL-Ser-DL-Glu-DL-Glu-DL-Leu-DL-Val-DL-Gln-DL-Lys-DL-Tyr-DL-Ser-DL-Asn-DL-Ser-NH2
Application
Peptide fragment corresponding to residues 1 - 40 of Nogo-66, the domain of the myelin protein Nogo that inhibits axonal outgrowth. Acts as a competitive antagonist at the Nogo-66 receptor (NgR)
Appearance
White lyophilised solid
Purity
>95%
Activity
Antagonist

Nogo-66 (1-40) is a synthetic peptide fragment derived from the Nogo-A protein, specifically encompassing amino acids 1 to 40 of the Nogo-66 domain. As a functionally significant region of the Nogo-A isoform, this peptide is recognized for its role in modulating neurite outgrowth and axonal regeneration within the central nervous system. Its biochemical relevance is rooted in its interaction with Nogo receptors, making it a valuable research tool for elucidating inhibitory signaling pathways that regulate neural plasticity. The availability of Nogo-66 (1-40) as a defined peptide sequence enables researchers to dissect the molecular mechanisms underlying neuronal growth inhibition and to model the effects of myelin-associated inhibitors in vitro and in vivo.

Neuroscience research: Nogo-66 (1-40) is widely utilized in neuroscience studies focused on axonal guidance and regeneration. By mimicking the inhibitory domain of the native Nogo-A protein, the peptide provides a controlled means to investigate how myelin-derived molecules restrict neural growth following injury. Researchers employ it in cell-based assays and primary neuronal cultures to study the molecular basis of axon growth inhibition, thereby advancing the understanding of central nervous system repair mechanisms.

Receptor-ligand interaction studies: The peptide serves as a critical tool for probing the binding interactions between Nogo-66 domains and their cognate receptors, such as NgR1 (Nogo receptor 1). By using Nogo-66 (1-40) in ligand-binding assays, surface plasmon resonance, or co-immunoprecipitation experiments, scientists can map the structural determinants of receptor engagement and downstream signaling. These insights are essential for identifying potential targets for modulating inhibitory cues in neural tissues.

Signal transduction analysis: Incorporation of Nogo-66 (1-40) in experimental systems facilitates the dissection of intracellular signaling cascades triggered by Nogo receptor activation. Researchers utilize the peptide to stimulate cellular models and monitor the activation of RhoA, ROCK, and other key signaling molecules implicated in cytoskeletal dynamics. Such studies are instrumental in clarifying how extracellular inhibitory signals are transduced into changes in neuronal morphology and motility.

Peptide antagonist screening: Nogo-66 (1-40) is employed in the development and evaluation of peptide-based or small-molecule antagonists designed to block Nogo-mediated inhibition. By serving as a reference ligand in competitive binding or functional assays, it enables the screening of candidate compounds that may interfere with the Nogo-receptor interaction. This application supports the identification of molecular probes for fundamental research and the exploration of neural plasticity modulation.

Protein engineering and structural biology: The defined sequence of Nogo-66 (1-40) makes it a valuable substrate for structural and biophysical studies aimed at elucidating peptide conformation and receptor recognition. Researchers leverage the peptide in crystallography, NMR spectroscopy, or computational modeling to gain atomic-level insights into the inhibitory domain's structure and its interface with receptor proteins. Such information is critical for rational design of modified peptides or mimetics with altered biological activity.

Long-term Storage Conditions
Soluble in DMSO
Shipping Condition
Room temperature
InChI
InChI=1S/C206H324N56O65/c1-23-104(15)163(258-169(292)109(20)226-174(297)126(59-67-148(210)272)240-201(324)166(107(18)26-4)261-199(322)160(101(9)10)255-153(277)92-223-171(294)120(41-30-33-75-207)230-186(309)138(86-115-51-57-119(271)58-52-115)249-202(325)165(106(17)25-3)260-182(305)121(228-111(22)268)44-36-78-220-205(215)216)200(323)241-128(61-69-150(212)274)178(301)232-123(43-32-35-77-209)176(299)251-144(95-265)195(318)247-140(89-159(288)289)190(313)234-125(62-70-154(278)279)172(295)222-91-152(276)229-141(87-116-90-219-98-224-116)204(327)262-80-38-46-147(262)196(319)248-137(83-112-39-28-27-29-40-112)185(308)233-124(45-37-79-221-206(217)218)173(296)225-108(19)168(291)242-135(84-113-47-53-117(269)54-48-113)187(310)244-133(81-99(5)6)184(307)236-131(65-73-157(284)285)181(304)252-143(94-264)192(315)238-132(66-74-158(286)287)183(306)256-161(102(11)12)197(320)227-110(21)170(293)259-164(105(16)24-2)203(326)254-146(97-267)193(316)237-129(63-71-155(280)281)179(302)235-130(64-72-156(282)283)180(303)243-134(82-100(7)8)191(314)257-162(103(13)14)198(321)239-127(60-68-149(211)273)177(300)231-122(42-31-34-76-208)175(298)245-136(85-114-49-55-118(270)56-50-114)188(311)253-145(96-266)194(317)246-139(88-151(213)275)189(312)250-142(93-263)167(214)290/h27-29,39-40,47-58,90,98-110,120-147,160-166,263-267,269-271H,23-26,30-38,41-46,59-89,91-97,207-209H2,1-22H3,(H2,210,272)(H2,211,273)(H2,212,274)(H2,213,275)(H2,214,290)(H,219,224)(H,222,295)(H,223,294)(H,225,296)(H,226,297)(H,227,320)(H,228,268)(H,229,276)(H,230,309)(H,231,300)(H,232,301)(H,233,308)(H,234,313)(H,235,302)(H,236,307)(H,237,316)(H,238,315)(H,239,321)(H,240,324)(H,241,323)(H,242,291)(H,243,303)(H,244,310)(H,245,298)(H,246,317)(H,247,318)(H,248,319)(H,249,325)(H,250,312)(H,251,299)(H,252,304)(H,253,311)(H,254,326)(H,255,277)(H,256,306)(H,257,314)(H,258,292)(H,259,293)(H,260,305)(H,261,322)(H,278,279)(H,280,281)(H,282,283)(H,284,285)(H,286,287)(H,288,289)(H4,215,216,220)(H4,217,218,221)
InChI Key
OLEKMOOQFWTQGD-UHFFFAOYSA-N
Isomeric SMILES
CC[C@H](C)[C@@H](C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)NCC(=O)N[C@@H](CC1=CNC=N1)C(=O)N2CCC[C@H]2C(=O)N[C@@H](CC3=CC=CC=C3)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC4=CC=C(C=C4)O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC5=CC=C(C=C5)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H](CO)C(=O)N)NC(=O)[C@H](C)NC(=O)[C@H](CCC(=O)N)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@H](C(C)C)NC(=O)CNC(=O)[C@H](CCCCN)NC(=O)[C@H](CC6=CC=C(C=C6)O)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@H](CCCNC(=N)N)NC(=O)C

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