A11

A11 is a short, engineered peptide motif containing hydrophobic and charged residues arranged to explore binding-site complementarity. Its compact structure enables flexible conformational sampling in solution. Researchers use it for protein-surface screening and early-stage ligand discovery. Applications include probe optimization, SAR evaluations, and motif-function analysis.

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

CAT No: R2783

CAS No:2412926-30-6

Synonyms/Alias:CPP-EYVQTVKSSKG;YGRKKRRQRRREYVQTVKSSKG;L-tyrosylglycyl-L-arginyl-L-lysyl-L-lysyl-L-arginyl-L-arginyl-L-glutaminyl-L-arginyl-L-arginyl-L-arginyl-L-α-glutamyl-L-tyrosyl-L-valyl-L-glutaminyl-L-threonyl-L-valyl-L-lysyl-L-seryl-L-seryl-L-lysyl-glycine

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M.F/Formula
C117H204N46O32
M.W/Mr.
2767.16
Sequence
One Letter Code:YGRKKRRQRRREYVQTVKSSKG
Three Letter Code:Tyr-Gly-Arg-Lys-Lys-Arg-Arg-Gln-Arg-Arg-Arg-Glu-Tyr-Val-Gln-Thr-Val-Lys-Ser-Ser-Lys-Gly

A11 is a specialized carbohydrate compound recognized for its unique structural features and versatile functional properties, making it a valuable tool in a variety of scientific research domains. As a member of the oligosaccharide family, A11 is characterized by its defined monosaccharide sequence and specific glycosidic linkages. These attributes not only confer stability and solubility in aqueous environments but also enable precise interactions with a range of biological molecules. Researchers appreciate A11 for its reproducibility and compatibility with diverse analytical techniques, which facilitates its integration into complex experimental workflows. Its role as a model substrate and molecular probe has garnered significant attention in glycobiology and related disciplines, where understanding carbohydrate-mediated processes is essential.

Glycan-Protein Interaction Studies: A11 serves as an indispensable probe in the investigation of glycan-protein interactions. By mimicking natural carbohydrate structures found on cell surfaces, it allows researchers to elucidate the binding specificity and affinity of lectins, antibodies, and other glycan-recognizing proteins. These studies are crucial for mapping cellular communication pathways, exploring pathogen-host recognition mechanisms, and advancing the field of glycomics. The use of A11 in microarray platforms and surface plasmon resonance assays enables high-throughput and quantitative analysis, leading to a deeper understanding of molecular recognition events governed by carbohydrates.

Enzyme Substrate Characterization: In enzymology, A11 is frequently employed as a substrate to assess the activity and specificity of glycosidases and glycosyltransferases. Its well-defined structure makes it suitable for kinetic studies, where the catalytic efficiency and substrate preferences of carbohydrate-active enzymes are evaluated. By monitoring the enzymatic modification or cleavage of A11, researchers can identify novel enzyme functions, optimize biocatalytic processes, and contribute to the development of enzyme-based synthesis of complex glycans. This application is particularly relevant in biotechnology and synthetic biology, where enzyme engineering is pivotal for the design of new biomolecules.

Cell Signaling Pathway Elucidation: Oligosaccharides like A11 play a pivotal role in modulating cell signaling pathways. By integrating it into cell culture systems or in vitro assays, scientists can dissect the influence of specific glycan motifs on receptor activation, signal transduction, and downstream cellular responses. Such studies provide insights into the regulatory roles of carbohydrates in immune modulation, development, and disease progression. The ability of A11 to selectively interact with cell surface receptors enables targeted investigations into the mechanisms by which glycosylation patterns affect cellular communication and fate decisions.

Analytical Method Development: The structural uniformity and chemical stability of A11 make it an ideal standard for the calibration and validation of analytical techniques in carbohydrate research. It is routinely used in mass spectrometry, high-performance liquid chromatography (HPLC), and capillary electrophoresis to establish baseline retention times, fragmentation patterns, and detection limits. By providing a reliable reference, A11 enhances the accuracy and reproducibility of glycan analysis, facilitating the identification and quantification of complex carbohydrate mixtures in biological samples.

Biosensor and Diagnostic Tool Design: The incorporation of A11 into biosensor platforms has opened new avenues for the detection of glycan-binding proteins, pathogens, and disease biomarkers. By immobilizing it on sensor surfaces, researchers can create highly specific recognition elements that translate molecular binding events into measurable signals. This approach underpins the development of innovative diagnostic assays with applications in infectious disease surveillance, food safety, and environmental monitoring. The versatility of A11 in biosensor design underscores its value as both a research reagent and a building block for translational technologies, driving progress in analytical and diagnostic sciences.

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