CAS 1417221-06-7 Cys(Npys)-(Arg)9

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CAS 1417221-06-7 Cys(Npys)-(Arg)9
Details
•CAS No.: 1417221-06-7
•Synonyms: Cys(3-nitro-2-pyridinesulfenyl)-nona-L-arginine amide, Npys-activated nonaarginine
•Core Structure: N-terminal cysteine side chain thiol activated with Npys; nine L-arginine residues in tandem; C-terminal amidation
•Purity: HPLC ≥95% (free base); typically provided as TFA salt
Related Documents
•Certificate of Analysis (COA)
•Mass Spectrometry Report (MS)
•HPLC Purity Report
•Peptide Solubility and Storage Guide
Category
Drug Delivery Peptides
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Description

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Description Cys(Npys)-(Arg)₉ is a tool peptide in which a cysteine residue activated with 3-nitro-2-pyridinesulfenyl (Npys) is added to the N-terminus of the nona-L-arginine ((Arg)₉) cell-penetrating peptide, with C-terminal amidation, sequence C(Npys)RRRRRRRRR-NH₂, CAS No. 1417221-06-7. Nonaarginine is one of the most efficiently penetrating members of the arginine oligomer family, carrying a net positive charge of +9 and efficiently entering cells through multiple mechanisms including macropinocytosis and direct translocation. The Npys-activated cysteine can undergo selective disulfide conjugation with free thiol-containing cargo (such as cysteine peptides, thiolated nucleic acids, thiolated small molecules) under mild conditions, forming disulfide linkages that can be cleaved by the intracellular reducing environment. This product is a commonly used reagent for constructing peptide-drug conjugates, nucleic acid delivery systems, and protein transduction tools. Note: This product is the L-arginine configuration, distinct from the D-arginine configuration Cys(Npys)-(D-Arg)₉.
Molecular formula C₆₂H₁₁₈N₄₀O₁₂S₂
Molecular weight (Da) 1679.99
Structure type N-terminal Cys(Npys)-activated linear decapeptide (9 L-Arg), C-terminal amidated
Solubility Freely soluble in water, PBS
Storage Powder at -20°C, dry and protected from light; avoid contact with reducing agents

 

Product Basic Information Table

 

Product Standard English Name Product Abbreviation / Alias Function Tags (comma-separated) Core Structure Molecular Formula Exact Mass (Da) Average MW (Da) Salt Form Length (aa)
Cys(Npys)-(Arg)9 Npys-modified nonaarginine; thiol-reactive polyarginine peptide Cell-penetrating peptide, site-specific chemical conjugation, nucleic acid/drug delivery, disulfide crosslinking Nona-L-arginine N-terminally linked to Npys-modified cysteine; strong positively charged sequence efficiently penetrates cell membranes, Npys enables site-specific disulfide conjugation to drugs, proteins and nanocarriers C₆₃H₁₃₀N₃₉O₁₀S₂ 1677 ~1678.6 Acetate 10

 

Physicochemical Solubility & Storage Parameters

 

Product Code Appearance Long-term Storage Short-term Storage Solution Stability Solid Powder Stability
PEP-R09-Npys Yellowish to off-white powder Store at -20°C, sealed, dry and protected from light, under inert gas. Aliquot for storage. Stable for 1 month at 2–8°C in sealed dry condition; protect from oxygen and light during shipping. Stable for 7 days at 4°C. Strong cationic peptide is highly soluble in water, dilute acetic acid and acidic buffers. Npys group is sensitive to thiols and strong reducing agents; prone to disulfide exchange and inactivation. Avoid combination with reducing agents and thiol compounds. Stable for 2 years at -20°C, dry, protected from light and under inert gas.

Functional Description

 

Product Code Frontend Short Summary (for search list display) Detailed Biological Function Description Applicable Research Areas (comma-separated) Targets / Pathways
PEP-R09-Npys Npys-modified nonaarginine with dual strong penetration and site-specific thiol conjugation Npys-modified nonaarginine is a bifunctional cell-penetrating peptide. The strong positively charged nonaarginine sequence efficiently penetrates cell membranes to deliver nucleic acids, proteins and small molecule drugs. The N-terminal Npys group provides a site-specific reactive site for disulfide exchange with thiols under mild conditions. Gene transfection & gene therapy, protein drug conjugation, nanocarrier functionalization, site-specific chemical modification, CPP technology Phospholipid bilayer; Npys-thiol conjugation site; electrostatic adsorption transmembrane transport

 

 

 

 

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