PD-1 is spiked at three known concentrations throughout the range of the assay and run to measure response of the spiked sample matrix. Serum recovery is 95% compared to 136% for the top competitor. EDTA Plasma recovery ...read more
The Quantikine™ Human Programmed Death-1 (PD-1) Immunoassay is a 4.5 hour solid-phase ELISA designed to measure human PD-1 in cell culture supernates, cell lysates, serum, plasma, and urine. It contains HEK293-expressed recombinant human PD-1 and has been shown to accurately quantitate the recombinant factor. Results obtained using natural human PD-1
showed li...near curves that were parallel to the standard curves obtained using the Quantikine kit standards. These results indicate that this kit can be used to determine relative mass values for natural human PD-1.
Store the unopened product at 2 - 8 °C. Do not use past expiration date.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Human PD-1 Quantikine ELISA Kit
CD279 antigen
CD279
hPD-1
PD1
PD-1
PD1hPD-l
PDCD1
programmed cell death 1
programmed cell death protein 1
Protein PD-1
SLEB2
Background
Programmed Death-1 (PD-1), also known as Programmed cell death protein and CD279, is an
extensively studied immune checkpoint inhibitory receptor. Given PD-1's role in peripheral
tolerance, it is not surprising that increased PD-1 expression is a mechanism for immune
escape, which is permissive for cancer growth and metastasis (1,2). PD‐1 is encoded by the
PDCD1 gene (3). The PD-1 glycoprotein is a monomeric 50-55kDa type 1 transmembrane
protein that belongs to the immunoglobulin (Ig) superfamily (4). PD-1 expression and
induction have been well studied (3,5,6). It is expressed in CD4+ and CD8+ T cells as well as B
cells, macrophages, some dendritic cell subsets and NK cells. PD-1 is induced by T cell receptor
(TCR) signaling as well as interleukin 2 (IL-2), IL-7 and type 1 interferons. A variety of reagents
are used to experimentally induce PD-1 expression, including, phorbol 12-myristate 13 acetate,
ionomycin, concanavalin A, CD3/CD28 antibodies, or most notably lymphocytic
choriomeningitis virus in vivo (6).
PD-1 expression is also regulated post-translationally (2). The PD-1 extracellular domain is
glycosylated at asparagine (N) residues N49 and N72 while in the endoplasmic reticulum. PD-1
subsequently transits to the golgi apparatus where it is fucosylated at the same sites by the
core fucosylase FUT8. This post translational modification represents a novel therapeutic target
as T cells have a more robust anticancer response due to reduced surface expression of
de-fucosylated PD-1. PD-1 is polyubiquinated at lysine (K) residue K48 by the E3 ligase F-Box 38
(FBX028) (2,7) which results in PD-1 degradation via the proteosome.
PD-1 serves as the receptor for programmed death ligand 1 (PD-L1/CD274/B7-H1) and PD-L2
(CD273/B7-DC) (8,9). The interaction of the extracellular domains of PD-1 and PD-L1 causes a
confirmational change that results in the phosphorylation of the cytoplasmic immunoreceptor
tyrosine-based inhibitory motif (ITIM) and the immunoreceptor tyrosine-based switch motif
(ITSM) by Src family kinases (4). Src homology 2 containing tyrosine phosphatase 2 (SHP-2) and
SHP-1 are recruited in order to attenuate T cell activating signals via dephosphorylation of
downstream signaling cascades.
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