Cancer Diagnostics Solutions
This MAb recognizes proteins of 19-22kDa (reducing) and 38kDa-44kDa (non-reducing), identified as various isoforms of Vascular Endothelial Growth Factor or Vascular Permeability Factor (VEGF/VPF). It is highly specific to VEGF, which is a homodimeric, disulfide-linked glycoprotein with a close homology to platelet-derived growth factor (PDGF).
There are multiple isoforms of VEGF containing 206-, 189-, 165-, and 121-amino acid residues. The smaller two isoforms, VEGF165 and VEGF121, are secreted proteins and act as diffusible agents, whereas the larger two remain cell associated. VEGF/VPF plays an important role in angiogenesis, which promotes tumor progression and metastasis.
Villin is a tissue-specific actin-binding protein localized to the cytoskeletal framework of the brush border, where it regulates actin filament dynamics through bundling, nucleation, capping, and severing activities. In normal physiology, Villin expression is restricted to differentiated epithelial cells possessing a brush border, including those lining the intestinal villi, proximal renal tubules, oviducts, and seminiferous ducts. Owing to its limited tissue distribution, anti-Villin-1 antibodies are employed in immunohistochemistry to aid in the identification of gastrointestinal adenocarcinomas.
When used in conjunction with cytokeratin 7 (CK7) and cytokeratin 20 (CK20), Villin is valuable in the differential diagnosis of metastatic colorectal adenocarcinoma versus primary lung adenocarcinoma, particularly those with rootlet structures. Moreover, Villin expression has been documented in approximately 85% of gastrointestinal carcinoid tumors and 40% of pulmonary carcinoid tumors, supporting its utility in distinguishing carcinoid neoplasms from other neuroendocrine tumors.
Vimentin is a member of the intermediate filament family of proteins. Intermediate filaments are an important structural feature of eukaryotic cells. Together with microtubules and actin microfilaments, they make up the cytoskeleton. Expression of vimentin, when used in conjunction with keratin, is helpful in distinguishing melanomas from Undifferentiated Carcinomas and Large-Cell Lymphomas. All Melanomas and Schwannomas react strongly with vimentin. This antibody recognizes a 57 kDa intermediate filament. It labels a variety of mesenchymal cells, including melanocytes, lymphcells, endothelial cells and fibroblasts. Non-reactivity of vimentin antibody is often considered more useful than its presence, since there are a few tumors that do not contain vimentin (e.g., Hepatoma and Seminoma).
Von Willebrand Factor (vWF), also referred to as Factor VIII?related antigen, is a multimeric glycoprotein localized in endothelial cells, plasma, and platelets. It functions as a carrier molecule for Factor VIII, facilitating its stability and bioavailability, and plays a pivotal role in mediating platelet adhesion and aggregation, as well as in the transport of various plasma proteins. vWF undergoes multiple post-translational modifications that modulate its binding affinity and availability for Factor VIII, including propeptide cleavage and the formation of N-terminal disulfide linkages. Immunohistochemical detection of vWF is employed to confirm endothelial lineage in lesions of uncertain histogenesis, such as Kaposi?s sarcoma and cardiac myxoma. It is extensively utilized in the immunophenotypic differentiation of vascular neoplasms from tumors of non-vascular origin, in conjunction with other vascular markers, although expression is not uniformly present in all endothelial-derived tumors