Recombinant Mouse PD-L1/B7-H1 protein (His tag)
Species
Mouse
Purity
>90 %, SDS-PAGE
Tag
His Tag
Activity
not tested
Cat no : Eg0986
Validation Data Gallery
Product Information
Purity | >90 %, SDS-PAGE |
Endotoxin | <1.0 EU/μg protein, LAL method |
Activity |
Not tested |
Expression | HEK293-derived Mouse PD-L1/B7-H1 protein Phe19-His239 (Accession# Q9EP73) with a His tag at the C-terminus. |
GeneID | 60533 |
Accession | Q9EP73 |
PredictedSize | 26.0 kDa |
SDS-PAGE | |
Formulation | Lyophilized from sterile PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization. |
Reconstitution | Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water. |
Storage Conditions |
It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
|
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature. |
Background
PD-L1 (programmed cell death ligand 1, also known as CD274 or B7-H1) is a 290 aa type I transmembrane protein. PD-L1 is expressed constitutively on T cells, B cells, DCs, macrophages, mesenchymal stem cells and cultured bone marrow-derived mast cells. In addition, PD-L1 is also expressed on many nonhematopoietic cell types, including vascular endothelial cells, epithelial cells, muscle cells, hepatocytes, pancreatic islet cells, astrocytes in the brain, placental syncytiotrophoblasts, and cells in cornea, iris-ciliary body and retina of eye. PD-L1 is frequently upregulated in a wide variety of solid tumors, including melanoma, ovarian, lung, glioblastoma, breast, and pancreatic cancers. PD-L1 and PD-L2 are two ligands of PD-1. Engagement of PD-1 by PD-L1 or PD-L2 transduces a signal that inhibits T-cell proliferation, cytokine production, and cytolytic function. It is critical for the regulation of T cell function during tolerance, autoimmunity and infection. Besides the membrane-bound form, PD-L1 can also exist as a soluble form (sPD-L1) generated either by proteolytic cleavage of membrane-bound form or by translation of alternative spliced mRNA.
References:
1. Sharpe, Arlene H et al. Nature immunology vol. 8,3 (2007): 239-45. 2. Keir, Mary E et al. Annual review of immunology vol. 26 (2008): 677-704. 3. Riley, James L. Immunological reviews vol. 229,1 (2009): 114-25. 4. Takeuchi, Masahiro et al. Immunology letters vol. 196 (2018): 155-160.