NSJ Bioreagents
SKU:FY13201
SUSD2 Antibody / Sushi domain-containing protein 2, 100 ug
SUSD2 Antibody / Sushi domain-containing protein 2, 100 ug
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SUSD2 antibody detects Sushi domain-containing protein 2, a type I transmembrane glycoprotein involved in cell adhesion, immune modulation, and tumor progression. The UniProt recommended name is Sushi domain-containing protein 2 (SUSD2). This protein contains multiple extracellular domains that mediate interactions with matrix components and immune receptors, influencing cell signaling and tissue organization.
Functionally, SUSD2 antibody identifies a 822-amino-acid membrane protein that includes somatomedin B, AMOP, von Willebrand factor type D, and Sushi (CCP) domains. These motifs facilitate cell-cell and cell-matrix adhesion while modulating immune recognition and tumor microenvironment interactions. SUSD2 supports epithelial integrity and participates in TGF-beta and Wnt signaling pathways that control cell differentiation and invasion.
The SUSD2 gene is located on chromosome 22q11.23 and is expressed in endothelial cells, epithelial tissues, and several cancer types. Its expression is elevated in breast, ovarian, and colorectal cancers, where it contributes to tumor growth, angiogenesis, and immune evasion. In normal physiology, SUSD2 is thought to support epithelial repair and maintain mucosal homeostasis.
Pathologically, overexpression of SUSD2 promotes tumor cell adhesion, migration, and immune suppression through interactions with Galectin-1 and other immunoregulatory factors. Conversely, in certain contexts, SUSD2 may enhance antitumor immune responses by facilitating macrophage activation. Research using SUSD2 antibody supports studies in cancer immunology, cell adhesion, and signal transduction.
SUSD2 antibody is validated for western blotting, immunohistochemistry, and flow cytometry to detect adhesion-related glycoproteins. NSJ Bioreagents provides SUSD2 antibody reagents optimized for oncology, immunology, and cell signaling research.
Structurally, Sushi domain-containing protein 2 features multiple modular domains connected by disulfide bonds, forming a flexible extracellular scaffold that mediates protein-protein interactions. The cytoplasmic tail contains potential phosphorylation sites that regulate receptor signaling and intracellular trafficking. This antibody enables investigation of SUSD2's functional role in adhesion, cancer progression, and immune modulation.
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