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| Description | This biotin-labeled peptide specifically recognizes and binds hyaluronan; via a streptavidin platform it enables HA-coating visualization, HA-protein capture and HA-targeted drug delivery. It is used to study extracellular-matrix HA interactions with CD44/RHAMM and as a targeting ligand for HA biomaterials and the tumor HA-rich microenvironment. |
| Structure type | Linear HA-binding peptide (biotin-labeled) |
| Solubility | Readily soluble in water/PBS |
| Storage | Powder, −20°C, dry, light-protected |
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) |
| Hyaluronan-binding peptide, biotin labeled (GAHWQFNALTVRGGGSK, Lys(Biotin)) | Biotin-HABP; hyaluronan-binding peptide-biotin; HA-binding peptide (Pep-1 derived) biotinylated; biotin-labeled hyaluronic-acid-binding peptide; HA-binding probe; CD44/RHAMM ligand peptide; MCE HY-P5351 | biotinylated peptide, hyaluronan (HA)-binding peptide, hyaluronic acid, CD44, RHAMM, extracellular matrix, leukocyte migration/inflammation, tumor metastasis, tissue engineering, streptavidin probe | 17-mer, sequence GAHWQFNALTVRGGGS-{Lys(Biotin)}; the core HA-binding region is the N-terminal 12-mer GAHWQFNALTVR (derived from the HA-binding inhibitory peptide Pep-1 reported by Mummert et al., JEM 2000, selected by phage display), followed by a flexible GGGSK linker; biotin is conjugated to the epsilon-amino side chain of the C-terminal Lys (side-chain biotinylation, not N-terminal); no disulfide, no Met; contains 1 Trp, 1 His, 1 Arg (a B-X7-B-type basic binding motif); net charge ~+1 to +2 at pH 7 (Arg12 +1, His partially protonated, N-terminal Gly-NH2 +1); polar/amphipathic short peptide with good water solubility. Biotin net addition C10H14N2O2S. | C89H134N28O24S | 2010.98 | 2012.28 | Free base; TFA salt also available (MCE HY-P5351A); C-terminal Lys side-chain biotin label; no CAS | 17 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-BioHABP-01 | White to off-white powder | Store at -20C, sealed, desiccated, ~2-3 years; aliquot to avoid repeated freeze-thaw. Contains Trp (oxidizable/light-sensitive)-store light-protected and dry. | 2-8C for ~1-2 weeks; working aliquots at -20C, prepare fresh; in solution -80C for ~6 months. | Cationic/polar short peptide with good water solubility; soluble in water or pH 7.4 PBS; ~12.5 mg/mL in DMSO (with sonication). Biotin is on the C-terminal Lys side chain and does not affect the N-terminal HA-binding core; it binds streptavidin with high affinity (Kd ~ 1e-14 M) for detection/pull-down of immobilized HA. Prepare fresh and avoid repeated freeze-thaw that may cause precipitation. | solid stable ~2-3 years at -20C, sealed and desiccated; Trp may slowly oxidize and discolor on prolonged air exposure-recommended to store under inert gas, light-protected. |
Functional Description
| Product Code | Frontend Short Summary | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-BioHABP-01 | Biotin-labeled hyaluronan (HA)-binding peptide GAHWQFNALTVRGGGSK(Lys-Biotin), derived from the phage-display HA-binding inhibitory peptide Pep-1; blocks HA interaction with CD44/RHAMM for extracellular-matrix/leukocyte-migration/tumor-metastasis research and as an HA-streptavidin detection probe. | Hyaluronic acid (hyaluronan, HA) is a non-sulfated glycosaminoglycan abundant in the extracellular matrix (ECM) and on cell surfaces, participating in fertilization, embryonic development, wound healing, angiogenesis, leukocyte trafficking to inflamed tissues, and tumor metastasis; HA signals mainly through its cell-surface receptors CD44 and RHAMM (receptor for hyaluronan-mediated motility, HMMR). HA-receptor binding relies on a characteristic basic-amino-acid-rich motif, B-X7-B (B = Arg/Lys, X = non-acidic residues); both RHAMM and CD44 contain such B-X7-B motifs to recognize the glucuronic acid-N-acetylglucosamine disaccharide repeats of HA. This 17-mer has a core HA-binding region GAHWQFNALTVR (12-mer) derived from the HA-binding inhibitory peptide Pep-1 identified by phage display (Mummert et al., J Exp Med, 2000, 192:769-79), which competitively blocks the binding of cells expressing HA receptors (e.g., CD44) to immobilized HA, inhibits leukocyte adhesion and recruitment, and suppresses T-cell proliferation; a flexible GGGSK linker places biotin on the C-terminal Lys side chain, preserving the free orientation of the N-terminal HA-binding core while providing a streptavidin (SA) tag. Biotin labeling enables: (1) use as an HA probe to detect HA distribution/deposition in tissue sections or on cell surfaces via fluorescence/HRP-streptavidin; (2) after streptavidin immobilization, measuring binding affinity and competition with HA and CD44/RHAMM ectodomains; (3) in vitro blockade of HA-CD44 signaling to study leukocyte migration, inflammation, and tumor cell adhesion/invasion; (4) targeting HA hydrogels/scaffolds in tissue-engineering and ECM research. The peptide is polar and water-soluble; Trp gives weak UV absorbance; side-chain biotinylation does not interfere with HA binding. | hyaluronic acid (HA)/extracellular matrix, CD44/RHAMM (HMMR) receptors, HA-binding inhibitory peptide (Pep-1), leukocyte migration/inflammation, tumor metastasis/cell invasion, tissue engineering/HA hydrogels, streptavidin HA detection probe | Hyaluronic acid (HA) and its receptors CD44, RHAMM (HMMR); B-X7-B HA-binding motif; high-affinity binding to streptavidin/avidin |
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