Hyaluronan-Binding Peptide, biotin labeled

Product Name: Hyaluronan-Binding Peptide, biotin labeled

Sequence One Letter Code: GAHWQFNALTVRGGGS-K(Biotin)

Sequence Three Letter Code: H-Gly-Ala-His-Trp-Gln-Phe-Asn-Ala-Leu-Thr-Val-Arg-Gly-Gly-Gly-Ser-Lys(Biotin)-OH

Molecular Weight: 2012.4

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: Cancer Immunotherapy

Conjugation: Conjugated

Conjugation Type: Biotins

Code Nacres: NA.26

Application: This biotinylated hyaluronan-binding peptide is designed to interact specifically with hyaluronan (HA), a major glycosaminoglycan component of the extracellular matrix that plays key roles in cell migration, inflammation, angiogenesis, and tumor progression. The peptide contains a C-terminal GGGSK linker with biotinylation, enabling efficient immobilization and detection through streptavidin-based systems. By binding to HA, this peptide can block HA interactions with CD44 receptors and has been reported to inhibit T-cell proliferation, highlighting its utility in studies of immune modulation. It is widely used as a research tool for investigating HA-mediated signaling pathways, cell–matrix interactions, and the molecular mechanisms underlying inflammatory responses and cancer metastasis.

Current Research: Hyaluronan (HA), also known as hyaluronic acid, is a major glycosaminoglycan component of the extracellular matrix (ECM) that plays a crucial role in regulating cell behavior, tissue architecture, and intercellular communication. HA participates in a wide range of biological processes, including cell migration, inflammation, angiogenesis, wound healing, and tumor progression. Because HA-mediated signaling pathways are involved in both normal physiology and disease development, research tools that allow scientists to analyze HA interactions are essential. The biotinylated hyaluronan-binding peptide is a synthetic peptide specifically designed to interact with HA. The peptide includes a C-terminal GGGSK linker with biotinylation, allowing efficient immobilization and detection using streptavidin-based systems. Through its ability to bind HA and interfere with HA–receptor interactions, this peptide provides a convenient platform for studying extracellular matrix signaling, immune regulation, and cancer-related processes. Hyaluronan in the Extracellular Matrix Hyaluronan is a high–molecular weight polysaccharide composed of repeating disaccharide units of glucuronic acid and N-acetylglucosamine. Unlike many other glycosaminoglycans, HA is not sulfated and is synthesized directly at the plasma membrane by hyaluronan synthase enzymes. Once produced, HA becomes a major structural component of the extracellular matrix. Within tissues, HA forms hydrated networks that contribute to tissue elasticity, mechanical support, and cell motility. Its large size and high water-binding capacity allow it to create an environment that facilitates cell migration and tissue remodeling. HA is particularly abundant in connective tissues, skin, cartilage, and the tumor microenvironment. Beyond its structural functions, HA also acts as a signaling molecule that interacts with cell surface receptors such as CD44, RHAMM (receptor for hyaluronan-mediated motility), and LYVE-1. These interactions regulate processes such as cell proliferation, immune cell activation, and vascular development. HA–CD44 Signaling and Biological Regulation One of the most important receptors for hyaluronan is CD44, a transmembrane glycoprotein widely expressed on immune cells, epithelial cells, and many tumor cells. The HA–CD44 interaction plays a central role in cell adhesion, migration, and signal transduction. When HA binds to CD44, it can activate signaling pathways that regulate cytoskeletal organization, inflammatory responses, and cell survival. In the immune system, HA–CD44 interactions influence T-cell activation, leukocyte trafficking, and inflammatory signaling. In cancer biology, these interactions contribute to tumor cell invasion, metastasis, and the formation of supportive tumor microenvironments. Because of its involvement in multiple disease-related pathways, the HA–CD44 axis has become an important target in biomedical research. Design of the Biotinylated HA-Binding Peptide The biotinylated hyaluronan-binding peptide is engineered to specifically recognize and bind HA molecules while incorporating structural features that facilitate experimental applications. Key design elements include: A hyaluronan-binding sequence that interacts selectively with HA chains in the extracellular matrix A C-terminal GGGSK linker, which provides flexibility and spatial separation from the peptide’s functional region Biotin conjugation at the lysine residue, enabling affinity capture through streptavidin-based systems The GGGSK linker helps ensure that the biotin tag does not interfere with the HA-binding region of the peptide. This configuration preserves binding functionality while allowing the peptide to be immobilized or detected in biochemical assays. Advantages of Biotinylated Peptides in Research Biotinylation provides a powerful strategy for peptide-based experimental systems because of the extremely strong interaction between biotin and streptavidin. This binding pair enables reliable immobilization and detection in a variety of assay formats. For HA-binding peptides, biotinylation allows: Immobilization on streptavidin-coated beads or surfaces Efficient pull-down assays to study HA-binding proteins Detection in biochemical or imaging assays Integration into biosensor or microplate-based systems These capabilities make the peptide a flexible tool for analyzing extracellular matrix interactions and HA-related signaling pathways. Applications in HA and Extracellular Matrix Research The biotinylated hyaluronan-binding peptide is widely used in studies investigating HA biology and cell–matrix communication. Its ability to bind HA and interfere with receptor interactions allows researchers to explore how HA influences cellular behavior. Common applications include: HA interaction studies The peptide can be used to examine how HA interacts with cell surface receptors and extracellular matrix components. CD44 signaling research By blocking HA binding to CD44, the peptide helps researchers analyze the downstream signaling pathways regulated by this receptor. Immune modulation studies The peptide has been reported to inhibit T-cell proliferation, making it useful for investigating immune regulation and inflammatory responses. Cancer and metastasis research HA–CD44 signaling is strongly associated with tumor progression and metastasis. The peptide can help explore how HA contributes to tumor cell migration and microenvironment interactions. Extracellular matrix biology Researchers use the peptide to investigate the structural and signaling roles of HA within complex tissue environments. Supporting Research on HA-Driven Biological Processes The extracellular matrix is not only a structural framework but also a dynamic signaling platform that regulates cellular behavior. Hyaluronan plays a particularly important role in coordinating these signals, especially in inflammation, tissue remodeling, and cancer progression. The biotinylated hyaluronan-binding peptide provides a convenient and versatile research tool for studying these processes. By combining HA-binding capability with a biotin affinity tag, the peptide enables efficient experimental approaches such as pull-down assays, receptor interaction studies, and extracellular matrix analysis. Through these applications, this peptide supports ongoing research aimed at understanding how HA-mediated signaling pathways influence immune responses, cell migration, and tumor biology.