SPARCL1 (Secreted Protein Acidic and Cysteine-Rich-like 1), also known as Hevin or MAST9. is a member of the SPARC family of matricellular proteins. It is a secreted glycoprotein involved in regulating cell-matrix interactions, tissue remodeling, and cellular adhesion. Structurally, SPARCL1 contains conserved domains typical of SPARC family members, including an N-terminal acidic region and a C-terminal extracellular calcium-binding domain. It plays critical roles in diverse biological processes, such as synaptic organization in the nervous system, angiogenesis, and tumor suppression. Studies highlight its dual role in cancer: it can inhibit tumor progression by modulating cell adhesion and signaling pathways (e.g., TGF-β, Wnt), but may also promote metastasis in certain contexts by facilitating extracellular matrix (ECM) remodeling.
SPARCL1 antibodies are immunological tools designed to detect and quantify SPARCL1 protein expression in research applications. These antibodies are widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to study SPARCL1's spatial-temporal expression patterns, particularly in neurological disorders, vascular diseases, and cancer biology. Commercial SPARCL1 antibodies are typically raised against specific epitopes (human or murine) and validated for species reactivity. Recent research explores SPARCL1's potential as a diagnostic or prognostic biomarker, driving demand for high-specificity antibodies. However, challenges remain in distinguishing SPARCL1 from homologous family members (e.g., SPARC/osteonectin) due to sequence similarities, necessitating rigorous validation for experimental accuracy.