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What is CD8?

The LAG3 protein belongs to the Ig superfamily and contains 4 extracellular Ig-like domains (D1-D4). This molecule plays an key role in the immune response through negative regulation of T-cell proliferation, function, and homeostasis. It is required for maximum natural and induced regulatory T-cell function. LAG3 is closely related to the T-cell co-receptor CD4, and like CD4, binds to MHC class II molecules - but with a significantly higher affinity. It is expressed exclusively in activated T- and natural killer (NK) lymphocytes.

TNF alpha is a multifunctional proinflammatory cytokine that belongs to the tumor necrosis factor (TNF)-receptor superfamily. It is involved in the regulation of a wide spectrum of biological processes: cell proliferation, differentiation, apoptosis, inflammation, lipid metabolism, and coagulation. TNF alpha has been implicated in a variety of autoimmune diseases (rheumatoid arthritis, Crohn's disease, multiple sclerosis, and psoriasis), insulin resistance, septic shock, and tumor metastases related to cancer.

The type I transmembrane glycoprotein EpCAM is a monomeric membrane glycoprotein that is expressed on most epithelial cell membranes as well as on a variety of epithelial carcinomas. It contains an extracellular domain with two epidermal growth factor-like extracellular domain repeats adjacent to a cysteine-poor region, along with a transmembrane domain, and a short cytoplasmic tail. EpCAM is a powerful tool for the detection of circulating and disseminated cancer cells (CTCs/DTCs) in blood and bone marrow, and it is the most commonly used epithelial marker to capture CTCs/DTCs.

The B-cell antigen receptor (BCR) is a complex multimeric aggregate that includes the following key noncovalently-bound components: antigen-specific surface immunoglobulin (Ig), CD79a (Ig-alpha), and CD79b (Ig-beta). BCR signaling is a pivotal pathway in tumorigenesis. The CD79 signaling subunits are essential for proper B-cell development, maintenance, and activation. Both are transmembrane proteins with extended cytoplasmic domains containing immunoreceptor tyrosine activation motives (ITAMs).

The products of MHC genes are antigen-presenting molecules (APMs) designed for antigen fragment (peptide) presentation to the T-cell receptor. In particular, MHC Class I molecules play a key role in the immune system by presenting endogenously synthesized peptides derived from the endoplasmic reticulum (ER) lumen to CD8+ T-lymphocytes, which are usually cytotoxic T-cells. MHC Class I antigens are heterodimers consisting of one 44kD highly polymorphic alpha chain non-covalently complexed with an invariant 11.5kD beta2-microglobulin subunit.

CD38 is a 42 kD type II transmembrane glycoprotein that uses nicotinamide adenine dinucleotide (NAD) as a substrate to form cyclic adenosine diphosphate ribose (cADPR). This novel multifunctional ectoenzyme has both cyclase and hydrolase enzymatic activity, and is expressed on the surface of most white blood cells (CD4+, CD8+, B-lymphocytes and natural killer (NK) cells).  It is also expressed at high levels in normal tissues and organs like the pancreas, liver, and kidney as well as in malignant lymphoma and neuroblastoma.

Keratins, also called cytokeratins, are a family of filamentous structural proteins that form the intermediate filaments within epithelial cells. Keratins are differentially expressed depending on both the epithelial cell origin and degree of differentiation. An antibody to any given keratin is useful either as a stand-alone or part of an antibody panel to help identify or clarify tissue origin. Cytokeratin 18 (CK18) is a 45 kD normal constituent of the hepatocyte cytoskeleton and is expressed in combination with cytokeratin 8.

The Ki67 antigen is a prototypic cell cycle-related protein expressed by proliferating cells in all phases of the active cell cycle (G1, S, G2 and M). It is a non-histone nuclear protein originally identified in a Hodgkin's lymphoma-derived cell line. Ki67 interacts with KIF15 and MKI67IP, and is approximately 395 kD. It exhibits a complex nuclear localization pattern that is cell cycle-dependent - expression peaks during late G1, S, G2, and M phases, but is undetectable in G0.

Podoplanin is a mucin-type 1 transmembrane glycoprotein found in a wide range of tissues. It appears to be differentially expressed in endothelial cells of lymphatic but not blood vessel origin. In normal skin and kidney, podoplanin co-localizes with VEGFR3/FLT4, another marker for lymphatic endothelial cells. It appears to be involved in lymphangioigenesis and cell migration and is regulated by the lymphatic-specific homeobox gene Prox1. Podoplanin has also been found to be expressed on a wide variety of tumors.