B7-H3/CD276 Extracellular Domain (human, recombinant)

Territorial Availability: Available through Bertin Technologies only in France

• Correlated keywords
  • B7RP2 B-7RP2 B7-RP2 B-7RP-2 RP 4IgB7H3 4IgB7H-3 7H3 B7H3 CD-276 B7CD28 B7CD-28 B-7 H-3 AP1 NF?B IgG-1 Gly-27 HEK-293
• Product Overview:
  B7-H3, also known as CD276, is a type I transmembrane glycoprotein and member of the B7-CD28 immune checkpoint protein family with roles in the T cell-mediated immune response.{52819,57242} It is encoded by CD276 in humans and is composed of an N-terminal signal peptide, an extracellular domain containing two identical pairs of immunoglobulin (Ig) constant (IgC) and variable (IgV) domains, a transmembrane region, and an intracellular tail. CD276 is ubiquitously expressed, however, protein expression is post-transcriptionally regulated.{57242} B7-H3 protein is constitutively expressed on non-immune fibroblasts, endothelial cells, and osteoblasts, and can be induced in immune cells such as dendritic cells, macrophages, natural killer (NK) cells, and T cells. It inhibits NK cell-mediated lysis, as well as induces co-inhibition of T cells, increases activation of tumor-specific cytotoxic T cells, and decreases proliferation of CD4+ and CD8+ T cells through modulation of nuclear factor of activated T cells (NFAT), NF-?B, and AP-1. Serum levels of B7-H3 are increased in patients with sepsis, as are intestinal levels in patients with graft versus host disease. High tumor levels of B7-H3 protein are associated with increased tumor size, poorly differentiated tumors, lymph invasion, and shorter overall survival in patients with lung and breast cancers.{52820} Cayman’s B7-H3/CD276 Extracellular Domain (human, recombinant) protein is a disulfide-linked homodimer. The reduced monomer, comprised of B7-H3 (amino acids 1-461) fused to human IgG1 Fc at its C-terminus, consists of 673 amino acids, has a calculated molecular weight of 73.4 kDa, and a predicted N-terminus of Gly27 after signal peptide cleavage. As a result of glycosylation, the monomer migrates at approximately 116 kDa by SDS-PAGE under reducing conditions.