- Tel: 858.663.9055
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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
SRPX antibody detects Sushi repeat-containing protein X-linked, a secreted and membrane-associated glycoprotein encoded by the SRPX gene located on chromosome Xq22.1. SRPX is a member of the sushi repeat (also called complement control protein or CCP) family, characterized by tandemly repeated domains that mediate protein-protein interactions involved in immune signaling, cell adhesion, and extracellular matrix organization. The SRPX protein localizes to the extracellular space and plasma membrane, where it participates in cellular communication, angiogenesis, and synaptic remodeling.
SRPX antibody identifies a multifunctional protein expressed in various tissues, including the brain, lung, and vascular endothelium. Within the extracellular environment, SRPX acts as an adhesion molecule that facilitates interactions between cells and matrix components. It is upregulated during wound healing and tissue remodeling, suggesting a role in extracellular matrix turnover and endothelial migration. SRPX contains three sushi domains, an N-terminal signal peptide, and glycosylation sites that support secretion and stability in the extracellular milieu.
In the nervous system, SRPX contributes to synapse formation and refinement. A related paralog, SRPX2, has been implicated in synaptic development and language-associated brain disorders, suggesting possible functional overlap within this protein family. SRPX also interacts with urokinase-type plasminogen activator receptor (uPAR) and complement components, supporting its role in both immune regulation and neurodevelopment. The presence of sushi domains links SRPX to complement control proteins that regulate immune activation and inflammation. Functional studies suggest that SRPX can influence cell migration, angiogenic responses, and matrix protease activity, making it relevant in vascular biology and tumor progression.
Clinically, altered SRPX expression has been observed in cancer, where it may contribute to tumor angiogenesis and metastasis. Overexpression has been reported in certain carcinomas, whereas decreased expression may impair extracellular signaling and cell adhesion. SRPX mutations have been studied in relation to X-linked intellectual disability and speech delay, although functional evidence remains limited. The SRPX gene resides in a genomic region frequently associated with inherited neurological disorders and may have regulatory overlap with neighboring genes involved in synaptic signaling.
From a structural standpoint, SRPX shares sequence homology with complement control proteins and contains conserved cysteine residues essential for disulfide bond formation. Its extracellular localization allows it to function as a scaffold in tissue remodeling and immune recognition. The protein family classification places SRPX among sushi domain-containing adhesion molecules, emphasizing its dual role in immune defense and neuronal plasticity.
Immunohistochemical analysis using SRPX antibody demonstrates extracellular and membrane-associated localization in endothelial cells, neurons, and epithelial tissues. The SRPX antibody from NSJ Bioreagents provides a useful reagent for studying sushi repeat proteins, angiogenesis, and cell-matrix interactions relevant to both neural and vascular biology.
Optimal dilution of the SRPX antibody should be determined by the researcher.
E.coli-derived human SRPX recombinant protein (Position: E40-T464) was used as the immunogen for the SRPX antibody.
After reconstitution, the SRPX antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
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