NLS-StAx-h

NLS-StAx-h combines a nuclear localization sequence with a stapled α-helical domain to promote nuclear targeting and structural stability. Hydrocarbon stapling locks helical conformation, improving resistance to proteolysis. Researchers use it to deliver helix-based motifs into the nucleus and probe transcriptional machinery. Applications include stapled-peptide technology, nuclear delivery, and PPI modulation.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: R2732

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cGMP Peptide
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M.F/Formula
C161H275N55O29
M.W/Mr.
3445.3

NLS-StAx-h is a specialized carbohydrate compound designed to facilitate advanced research in glycobiology and molecular biology. Characterized by a unique structural motif that combines nuclear localization signals (NLS) with carbohydrate-based scaffolding, NLS-StAx-h enables targeted delivery and precise molecular interactions within cellular environments. Its innovative design allows researchers to study intricate cellular processes, particularly those involving nucleocytoplasmic transport and glycan-mediated signaling, without introducing extraneous variables that might confound experimental outcomes. The versatility and stability of NLS-StAx-h make it an exceptional tool for a wide range of laboratory investigations, supporting both exploratory and hypothesis-driven research.

Cellular Trafficking Studies: NLS-StAx-h is extensively used in the study of nucleocytoplasmic transport mechanisms. By leveraging its nuclear localization signal, the compound can be tracked as it translocates through nuclear pores, providing valuable insights into the regulation and efficiency of nuclear import pathways. Researchers can use labeled versions of the compound to visualize its movement in live-cell imaging experiments, elucidating the dynamics of cargo recognition and transport in response to various cellular conditions. These studies are instrumental in deciphering the molecular determinants that govern nuclear-cytoplasmic compartmentalization and the impact of post-translational modifications on nuclear trafficking.

Glycan-Protein Interaction Analysis: In the context of glycan-protein interactions, NLS-StAx-h serves as a robust probe to investigate the binding specificity and affinity of lectins and other glycan-recognizing proteins. Utilizing its carbohydrate moiety, the compound can mimic natural glycan ligands, enabling the dissection of protein recognition events that underlie cellular communication, immune response modulation, and pathogen-host interactions. Through methods such as surface plasmon resonance or glycan microarrays, scientists can employ NLS-StAx-h to map out interaction networks, identify novel glycan-binding proteins, and characterize the functional consequences of these molecular engagements.

Intracellular Targeting in Molecular Delivery: The unique combination of a nuclear localization signal with a carbohydrate scaffold allows NLS-StAx-h to function as a molecular carrier for intracellular delivery applications. Researchers can conjugate small molecules, peptides, or nucleic acids to the compound, harnessing its targeting capabilities to ensure precise localization within the nuclear compartment. This targeted delivery approach is particularly valuable in studies aiming to modulate gene expression, investigate nuclear signaling pathways, or introduce reporter constructs for functional genomics experiments. The ability to direct molecular cargoes specifically to the nucleus enhances experimental specificity and reduces off-target effects.

Structural Biology and Crystallography: Structural biologists utilize NLS-StAx-h as a model system to study the three-dimensional architecture of glycan-containing complexes. By incorporating the compound into crystallization trials, researchers can capture high-resolution snapshots of glycan-protein assemblies, shedding light on the molecular determinants of recognition and binding. These structural insights are crucial for rational drug design, as they inform the development of glycomimetic inhibitors or modulators that target specific protein-glycan interactions. Additionally, the compound's stability and defined structure make it suitable for NMR spectroscopy and other biophysical analyses aimed at elucidating conformational dynamics.

Synthetic Biology and Biomaterials Research: In the realm of synthetic biology, NLS-StAx-h is employed as a modular building block for the design of multifunctional biomaterials and engineered cellular systems. Its dual functionality—combining nuclear targeting and glycan-based recognition—enables the construction of synthetic circuits that respond to nuclear signals or glycan-mediated cues. Researchers can integrate NLS-StAx-h into hydrogels, nanoparticles, or other delivery platforms to create responsive materials for controlled release, cellular sensing, or programmable cell behavior. This application highlights the compound's potential in advancing the interface between chemistry, biology, and materials science, paving the way for innovative solutions in research and biotechnology.

InChI
InChI=1S/C161H275N55O29/c1-13-97(10)128-149(240)206-117(83-93(2)3)140(231)205-120(87-124(218)219)144(235)215-160(11,151(242)209-119(86-100-90-181-92-193-100)142(233)212-126(95(6)7)147(238)204-112(58-29-41-73-187-156(173)174)135(226)201-114(59-30-42-74-188-157(175)176)139(230)211-127(96(8)9)148(239)207-118(84-98-88-191-103-49-20-18-47-101(98)103)141(232)195-105(129(166)220)51-26-38-70-184-153(167)168)64-32-16-14-15-17-33-65-161(12,152(243)213-128)214-143(234)116(60-31-43-75-189-158(177)178)203-145(236)122-63-46-79-216(122)150(241)121(85-99-89-192-104-50-21-19-48-102(99)104)208-137(228)111(57-28-40-72-186-155(171)172)197-131(222)107(56-27-39-71-185-154(169)170)194-123(217)91-245-82-81-244-80-78-183-146(237)125(94(4)5)210-138(229)113(55-25-37-69-165)200-136(227)115(62-45-77-190-159(179)180)202-134(225)110(54-24-36-68-164)199-133(224)109(53-23-35-67-163)198-132(223)108(52-22-34-66-162)196-130(221)106-61-44-76-182-106/h14-15,18-21,47-50,88-90,92-97,105-122,125-128,182,191-192H,13,16-17,22-46,51-87,91,162-165H2,1-12H3,(H2,166,220)(H,181,193)(H,183,237)(H,194,217)(H,195,232)(H,196,221)(H,197,222)(H,198,223)(H,199,224)(H,200,227)(H,201,226)(H,202,225)(H,203,236)(H,204,238)(H,205,231)(H,206,240)(H,207,239)(H,208,228)(H,209,242)(H,210,229)(H,211,230)(H,212,233)(H,213,243)(H,214,234)(H,215,235)(H,218,219)(H4,167,168,184)(H4,169,170,185)(H4,171,172,186)(H4,173,174,187)(H4,175,176,188)(H4,177,178,189)(H4,179,180,190)/b15-14-/t97-,105+,106-,107-,108-,109-,110-,111-,112+,113-,114+,115-,116-,117+,118+,119+,120+,121-,122-,125-,126+,127+,128-,160+,161-/m0/s1
InChI Key
NQDXIROEXUQMGO-HKEYISNASA-N

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