Anti-PARVA Polyclonal Antibody for WB and ELISA - Q9NVD7

Core Product Specifications and Parameters

Biological Background: PARVA Function and Localization

• Alpha-parvin (PARVA) is also known as actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), and matrix-remodeling-associated protein 2 (MXRA2). It is a member of the parvin family and exists in multiple isoforms due to alternative splicing.
• PARVA plays a critical role in sarcomere organization, smooth muscle cell contraction, and normal cardiovascular development, including septation of the heart outflow tract and vascular smooth muscle cell adhesion to endothelial cells during blood vessel formation (by similarity).
• Within the IPP (ILK-PINCH-PARVIN) complex, PARVA binds directly to F-actin and promotes F-actin bundling, a process essential for force generation during actin cytoskeleton reorganization and dynamic cell adhesion events such as cell spreading and migration. Related references: PMID:30367047
• PARVA is involved in laminin-induced actin reorganization, lamellipodia formation, and ciliogenesis. It contributes to the establishment of cell polarity, cell adhesion, cell spreading, and directed cell migration.
• Subcellularly, PARVA localizes to focal adhesions at the cell membrane, the cytoplasmic cytoskeleton, and the sarcomeric Z-line in myofibrils, reflecting its dual role in cellular adhesion and muscle structure.
• Post-translational modifications include acetylation and phosphorylation, which may regulate its activity and binding interactions.
• PARVA is widely expressed across tissues, with notably high levels in heart, skeletal muscle, kidney, and liver, consistent with its functions in muscle biology and cell adhesion.
• Key biological processes associated with PARVA, as indicated by UniProt keywords, encompass actin binding, cell adhesion, angiogenesis, cell shape, chemotaxis, and cilium biogenesis/degradation.

Experimental Guidance and Technical Tips

• The immunogen used is a synthetic peptide from the N-terminal region (amino acids 1-100) of human PARVA. This design may confer specificity for the target and could be suitable for detecting both full-length (42 kDa) and potential splice variants or cleavage products (e.g., 20 kDa band observed in some contexts).
• For Western blot applications, consider performing initial titration experiments to determine the optimal antibody dilution. Use appropriate positive controls such as lysates from heart, skeletal muscle, or cell lines known to express PARVA. The predicted molecular weight is approximately 42 kDa; however, confirm band size using a molecular weight marker and account for possible isoforms.
• In ELISA, this polyclonal antibody may be used as either a capture or detection reagent. Validate performance by testing a range of antigen concentrations and ensure compatibility with your assay buffer and detection system.
• Given the annotated cross-reactivity with human, mouse, and rat, this antibody is a candidate for studies involving these species. However, independent verification of reactivity in your specific sample type is recommended.

CamelBio: Your One-Stop Sourcing Bridge

CamelBio partners with diagnostic manufacturers, laboratories, and research institutes to offer a complete portfolio of IVD raw materials. For targets like PARVA, involved in cell adhesion and cardiovascular biology, CamelBio provides access to validated antibody pairs, optimized polyclonal and monoclonal antibodies, and bulk ancillary reagents. Our sourcing services extend to rare and specialized raw materials, supporting your projects from concept to clinic.