|Anti-rabbit IgG, HRP-linked Antibody 7074||100 µl||
|Calreticulin (D3E6) XP® Rabbit mAb 12238||20 µl||
||H M R||55||Rabbit IgG|
|Ubiquitin (E4I2J) Rabbit mAb 43124||20 µl||
|HLA-G (E8N9C) XP® Rabbit mAb 79769||20 µl||
|Calnexin (C5C9) Rabbit mAb 2679||20 µl||
||H Mk||90||Rabbit IgG|
|PSMB8/LMP7 (D1K7X) Rabbit mAb 13635||20 µl||
||H M R||23, 28||Rabbit IgG|
|β2-microglobulin (D8P1H) Rabbit mAb 12851||20 µl||
||H Mk||12||Rabbit IgG|
|IFNGR1 (E444) Antibody 10405||20 µl||
|TAP2 (E8G5I) Rabbit mAb 25657||20 µl||
|TAP1 (E4T4F) Rabbit mAb 49671||20 µl||
Monoclonal antibodies are produced by immunizing animals either with a recombinant protein specific to the carboxy terminus of human TAP1 protein or a synthetic peptide corresponding to residues near the amino terminus of human calreticulin protein, the carboxy terminus of human PSMB8/LMP7 protein, Gly35 of human ubiquitin protein, Leu102 of human HLA-G protein, Val57 of human β2-microglobulin protein, Val485 of human TAP2 protein, or Pro52 of human calnexin protein. Polyclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Glu444 of human IFNGR1 protein. Polyclonal antibody is purified by protein A and peptide affinity chromatography.
The predominant function of class I MHC/β2-microglobulin dimers, which are expressed on the surface of most nucleated cell types, is to modulate the adaptive immune response by presenting proteolytic peptide fragments from cytosolic proteins to cytotoxic CD8+ T cells. In order for self and nonself peptides to be presented by MHC class I molecules, the peptide fragments must first be derived from polyubiquitinated proteins that undergo degradation via the ubiquitin-proteasome system. In the context of inflammatory processes, the enzymatic core of the proteasome can be shaped by IFNγ signaling to contain subunits, such as PSMB8/LMP7, which enhance the presentation of antigenic peptides by antigen presenting cells (1). The resulting cytosolic peptide fragments generated through ubiquitin-dependent proteasomal degradation are then transported into the ER lumen via the peptide transporters, TAP1 and TAP2, where the activity of multiple chaperone proteins, such as calnexin and calreticulin, facilitate loading onto class I MHC/β2-microglobulin dimers for transport to the Golgi and eventually, the cell surface (2-6). Defects in the expression of multiple components of the class I antigen presenting machinery have been observed in both solid and liquid tumors, which serves as a mechanism of tumor-immune evasion (7).
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