Recombinant Human PD-L2 Protein (C-mFc)

Beta LifeScience SKU/CAT #: BL-2281NP
BL-2281NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
BL-2281NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Human PD-L2 Protein (C-mFc)

Beta LifeScience SKU/CAT #: BL-2281NP
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Product Overview

Description Recombinant Human Programmed Cell Death 1 Ligand 2 is produced by our Mammalian expression system and the target gene encoding Leu20-Pro219 is expressed with a mouse IgG1 Fc tag at the C-terminus.
Accession Q9BQ51
Synonym Programmed Cell Death 1 Ligand 2; PD-1 Ligand 2; PD-L2; PDCD1 Ligand 2; Programmed Death Ligand 2; Butyrophilin B7-DC; B7-DC; CD273; PDCD1LG2; B7DC; CD273; PDCD1L2; PDL2
Gene Background Programmed Cell Death 1 Ligand 2 (PDCD1LG2) is a member of the BTN/MOG family. PDCD1LG2 contains one Ig-like C2-type domain and one Ig-like V-type domain. PDCD1LG2 is highly expressed in the heart, placenta, pancreas, lung and liver; it is weakly expressed in the spleen, lymph nodes, and thymus. PDCD1LG2 is involved in the costimulatory signal, essential for T-cell proliferation and IFNG production in a PDCD1-independent manner. PDCD1LG2 interaction with PDCD1 inhibits T-cell proliferation by blocking cell cycle progression and cytokine production.
Molecular Mass 49.2 KDa
Apmol Mass 60-90 KDa, reducing conditions
Formulation Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity Not tested
Reconstitution Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage For Research Use Only

Target Details

Target Function Involved in the costimulatory signal, essential for T-cell proliferation and IFNG production in a PDCD1-independent manner. Interaction with PDCD1 inhibits T-cell proliferation by blocking cell cycle progression and cytokine production.
Subcellular Location [Isoform 3]: Secreted.; [Isoform 2]: Endomembrane system; Single-pass type I membrane protein.; [Isoform 1]: Cell membrane; Single-pass type I membrane protein.
Protein Families Immunoglobulin superfamily, BTN/MOG family
Database References
Tissue Specificity Highly expressed in heart, placenta, pancreas, lung and liver and weakly expressed in spleen, lymph nodes and thymus.

Gene Functions References

  1. Our results confirm and extend prior studies of PD-L1 and provide new data of PD-L2 expression in lymphomas PMID: 29122656
  2. High PD-L2 expression may be a target of immunotherapy in patients with PD-L1-negative Non-small Cell Lung Cancer. PMID: 30275216
  3. The high-affinity PD-1 mutant could compete with the binding of antibodies specific to PD-L1 or PD-L2 on cancer cells. PMID: 29890018
  4. the binding affinities of the PD-1-PD-L1/PD-L2 co-inhibitory receptor system, was characterized. PMID: 27447090
  5. Tumor PDCD1LG2 expression is inversely associated with Crohn-like lymphoid reaction to colorectal cancer, suggesting a possible role of PDCD1LG2-expressing tumor cells in inhibiting the development of tertiary lymphoid tissues during colorectal carcinogenesis. PMID: 29038297
  6. The biopsy tumor key protein measurements demonstrate substantial between-tumor variation in expression ratios of these proteins and suggest that programmed cell death 1 ligand 2 PD-L2 is present in some tumors at levels sufficient to contribute to programmed cell death-1 PD-1-dependent T-cell regulation and possibly to affect responses to PD-1- and programmed cell death 1 ligand 1 PD-L1-blocking drugs. PMID: 28546465
  7. the positive rate of PD-L2 did not show any differences between primary tumors and metastatic lymph nodes. In multivariate analysis, PD-L1 expression, PD-L2 expression, a low density of CD8(+) T cells in primary tumors, and PD-1 expression on CD8(+) T cells in primary tumors were associated with poor prognosis. PMID: 28754154
  8. in some tumor types, PD-L2 expression is more closely linked to Th1/IFNG expression and PD-1 and CD8 signaling than PD-L1 PMID: 27837027
  9. Clinical response to pembrolizumab in patients with head and neck squamous cell carcinoma (HNSCC)may be related partly to blockade of PD-1/PD-L2 interactions. Therapy targeting both PD-1 ligands may provide clinical benefit in these patients. PMID: 28619999
  10. PD-L2 is regulated by both interferon beta and gamma signaling. PMID: 28494868
  11. Overexpression of PD-L1 and PD-L2 Is Associated with Poor Prognosis in Patients with Hepatocellular Carcinoma PMID: 27456947
  12. Data suggest that hormonal 1,25-dihydroxyvitamin D is a direct transcriptional inducer of genes encoding PDL1 and PDL2 in myeloid cells/macrophages; this up-regulation of gene expression appears to be species- and cells-specific. PMID: 29061851
  13. PD-L2 copy number gains were not related to PD-L2 augmentation in non-small cell lung cancer. PMID: 27050074
  14. PD-L2 expression has been reported in 52% of esophageal adenocarcinomas but little is known about the expression of other immune checkpoints PMID: 28561677
  15. Low PD-L2 expression is associated with pediatric solid tumors. PMID: 28488345
  16. this study shows that higher PD-L2 expression on blood dendritic cells, from Plasmodium falciparum-infected individuals, correlates with lower parasitemia PMID: 27533014
  17. PD-L1/PD-L2 copy number alterations are a defining feature of classical Hodgkin lymphoma. PMID: 27069084
  18. PDL2 was overexpressed in Epstein Barr virus-associated gastric adenocarcinoma. PMID: 26980034
  19. higher expression of PD-L1 and PD-L2 on CD1a(+) cells than that on CD83(+) cells in cutaneous squamous cell carcinoma tumour tissues may contribute to negative regulation in anti-tumour immune responses PMID: 28052400
  20. stable ectopic expression of wild-type PDCD1LG2 and the PDCD1LG2-IGHV7-81 fusion showed, in coculture, significantly reduced T-cell activation. PMID: 27268263
  21. The expression levels of PD-1, PD-L1 and PD-L2 in CD3(+) T cells and CD19(+) B cells and serum IFN-gamma level in progressive hepatocellular carcinoma patients were significantly higher than controls. PMID: 27609582
  22. Downregulation of the immunosuppressive molecules, PD-1 and PD-L1, may imply that over-activation of immune cells in multiple sclerosis occurs through signaling dysfunction of these molecules and PD-L2 plays no important role in this context PMID: 27921410
  23. an IL-27/Stat3 axis induces expression of programmed cell death 1 ligands (PD-L1/2) on infiltrating macrophages in lymphoma PMID: 27564404
  24. High PD-L2 expression is associated with Renal Cell Carcinoma. PMID: 26464193
  25. knocking down in dendritic cells results in activation of inflammatory T cells PMID: 26599163
  26. We observed cogain or coamplification of CD274 and PDCD1LG2 in 32 of 48 cervical and 10 of 23 vulvar squamous cell carcinomas PMID: 26913631
  27. PD-L2 expression was neither associated with VEGF-TKI responsiveness nor patients' outcome PMID: 26424759
  28. PD-L1 and PD-L2 are useful new markers for identifying select histiocyte and dendritic cell disorders and reveal novel patient populations as rational candidates for immunotherapy PMID: 26752545
  29. Genomic amplification of 9p24.1 targeting JAK2, PD-L1, and PD-L2 is enriched in high-risk triple negative breast cancer. PMID: 26317899
  30. the inflammatory environment in Barrett's esophagus and esophageal adenocarcinoma may contribute to the expression of PD-L2. PMID: 26081225
  31. PDL2 could promote the ability of human placenta-derived mesenchymal stromal cells to augment the secretion of IL-10. PMID: 26432559
  32. We suggest that decreased expression of programmed death-ligand 1, 2 on psoriatic epidermis can contribute to its chronic unregulated inflammatory characteristics. PMID: 26133691
  33. Suggest role for PD-L2 in recurrence of hepatitis C infection post orthotopic liver transplantation. PMID: 25675203
  34. Report PD-L2 expression in breast neoplasms. PMID: 26541326
  35. Data indicate that pulmonary pleomorphic carcinoma (PC) very frequently express CD274 antigen (PD-L1) and CD273 antigen (PD-L2). PMID: 26329973
  36. PD-L1 and PD-L2 expression in pulmonary squamous cell carcinoma is associated with an increased number of CD8(+) tumor infiltrating lymphocytess and increased MET expression. PMID: 25662388
  37. Results show that human-derived chordoma cell lines demonstrate inducible expression of PD-L1 and PD-L2, and that primary chordoma tissue shows variable expression of PD-1 and PD-L1 in infiltrating immune cells PMID: 25349132
  38. conclude that PD-L2 protein is robustly expressed by the majority of primary mediastinal (thymic) large B-cell lymphomas PMID: 25025450
  39. PD-1/PD-Ls pathways on PMCs inhibited proliferation and adhesion activity of CD4+ T cells, suggesting that Mycobacterium tuberculosis might exploit PD-1/PD-Ls pathways to evade host cell immune response in human. PMID: 24406080
  40. High Expression of PD-L2 is associated with myelodysplastic syndromes. PMID: 24270737
  41. Data indicate that the bone morphogenetic proteins (BMPs) signaling pathway regulates PD-L1 and PD-L2 expression in monocyte-derived dendritic cells (MoDCs) during the maturation process. PMID: 24532425
  42. Recurrent genomic rearrangement events in CD274 and PDCD1LG2 underlie an immune privilege phenotype in a subset of B-cell lymphomas. PMID: 24497532
  43. PD-L1 and PD-L2 expressed on hPMSCs could inhibit the hPMSCs-mediated up-regulation on the expression of IL-17 secreted by peripheral blood T cells PMID: 23388330
  44. Macrophages from infected animals show increased expression of PDL2 and CD80 that was dependent from the sex of the host. PMID: 23533995
  45. expression of PD-1 and its ligands, PD-L1 and PD-L2, in liver biopsies from HBV-related acute-on-chronic liver failure (HBV-ACLF) and chronic hepatitis B (CHB) patients were analyzed; results showed all 3 molecules were observed in the HBV-ACLF samples and levels were significantly higher than in CHB PMID: 22895698
  46. Data show that PD-1, PD-L1, PD-L2, CCL17, and CCL22 mRNA was identified in papillomas. PMID: 22322668
  47. Data suggest that brain endothelial cells contribute to control T cell transmigration into the CNS and immune responses via PD-L2 but not PD-L1 expression. PMID: 22067141
  48. increased expression of PD-L2, as a costimulatory molecule, may have an important modulatory function on the local immune responses of OLP in vivo. PMID: 21457347
  49. Data suggest that PD-L1 may contribute to negative regulation of the immune response in chronic hepatitis B, and that PD-1 and PD-L1 and 2 may play a role in immune evasion of tumors. PMID: 21876620
  50. Our results suggest that PD-1 G-536A, PD-L1 A8923C and PD-L2 C47103T polymorphisms are associated with the presence of ankylosing spondylitis. PMID: 21791547

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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