Non-specific lipid transfer proteins （nsLTPs） play a crucial role in the transport and secretion of lipids in plants. In this study， two type II nsLTPs were cloned， namely nsLTP2-1 and nsLTP2-2， and analyzes it with functional analysis from Lavandula angustifolia. The analysis of sequence characteristics revealed that the nsLTP2-1 and nsLTP2-2 genes putatively encode 119 and 117 amino acids， respectively， which exhibit conserved lipid transfer proteins （LTP） domains and 8 highly conserved cysteine residues. The phylogenetic analysis revealed that these genes are located in separate branches and share the closest genetic relationship with Perilla frutescens， a member of the Labiatae family. The analysis of gene expression showed that both genes exhibit high expression levels in flower buds， with minimal expression observed in leaves， stems， and petals. However， notable disparities in expression were observed in the calyx， with nsLTP2-1 and nsLTP2-2 demonstrating higher expression levels in mature and young calyxes， respectively. The expression of these genes in flower buds and leaves was found to be stimulated by heavy light， while their expression in flower buds was also induced by abscisic acid. Additionally， the expression of nsLTP2-1 and nsLTP2-2 in leaves was found be triggered by methyl jasmonate and ethylene， respectively. The subcellular localization of the yellow fluorescent protein （EYFP） fusion protein demonstrated that both nsLTPs were localized on the cell membrane and cell wall， indicating they may be related to the transport of secondary metabolites. Following the overexpression of nsLTP2-1 and nsLTP2-2， tobacco leaves were subjected to Nile red staining， after 485-543 nm excitation light excitation， the fluorescence of leaf glandular hair was more than that of wild type. This observation suggests a potential significance of the nsLTPs investigated in this study with regards to lipid synthesis and transport. These findings provide a fundamental basis for elucidating the role of lavender lipid transfer protein in lipid and terpenoid transportation.