PD-L2 is a member of the B7 family. Upregulation of PD-L2 is primarily triggered via Th2 cell lineage toward the inflammatory macrophages. P7103G contains the human PD-L2 ECD fused with an aglycosylated mouse IgG2a Fc domain.
Interacting protein(s): PD-1 (P7099F, P7099G)
Related products: Checkpoint Proteins
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|Synonym:||B7DC, bA574F11.2, Btdc, PDCD1LG2, PDCD1L2, PD-1 L2|
|Tag:||Aglycosylated mouse IgG2a-Fc|
|MW (Calculated):||49,803 daltons|
|MW (SDS-PAGE):||52 Kd|
|Abs 0.1% (= 1 mg/ml):||1.234|
PD-L2 was identified by searching the human EST database with the murine PD-L2 homolog. Human and mouse PD-L2 share 70% amino acid identity, this is similar to those of PD-L1, 69%. Together, there are a total of 5 proteins in B7 family, each with known respective counter receptor(s). All share similar structural organization: a signal peptide, an IgV domain, an IgC domain, a transmembrane region, and a short cytoplasmic tail.
While the human and mouse PD-L1 proteins an identical cytoplasmic tail, human and mouse PD-L2 proteins have very different cytoplasmic tail. Yet, both genes are located on human 9q24.2 with the same orientation and are only 42 kb apart. An alternatively spliced form of PD-L2 missing the IgV region was identified and shown not bind to PD-1. PD-L2, but not PD-L1, mRNA was found in human pancreas, lung and liver. In contrast, PD-L1, but not PD-L2 is found in human fetal liver.
Similar to singals through CTLA-4, PD-1/PD-L2 interaction was shown to suppress TCR-mediated cell proliferation and cytokine production via the cross-talk of cytoplasmic ITIM domain of PD-1. Since PD-L1 and PD-L2 are up-regulated in a variety of tumor cell lines, PD-1 is considered a great target research for anti-tumor therapeutics.
Amino Acid Sequence
1. PD-L2 is a second ligand for PD-1 and inhibits T cell activation. Latchman Y., Wood C.R., Chernova T., Chaudhary D., Borde M., Chernova I., Iwai Y., Long A.J., Brown J.A., Nunes R., Greenfield E.A., Bourque K., Boussiotis V.A., Carter L.L., Carreno B.M., Malenkovich N., Nishimura H., Okazaki T., Honjo T., Sharpe A.H., Freeman G.J. Nat. Immunol. 2:261-8 (2001)
2. The role of novel T cell costimulatory pathways in autoimmunity and transplantation. Yamada A., Salama A.D., Sayegh M.H. J. Am. Soc. Nephrol. 13:559-75 (2002)
3. The role of B7 family molecules in hematologic malignancy. Greaves P., Gribben J.G. Blood 121:734-44 (2013)