|98240T||1 Kit (5 x 20 microliters)||
|TREM2 (E7P8J) Rabbit mAb (Carboxy-terminal Antigen, Mouse Specific) 76765||20 µl||
||M||11, 28||Rabbit IgG|
|TREM2 (E6T1P) Rabbit mAb (Amino-terminal Antigen, Mouse Specific) 61788||20 µl||
|Syk (D3Z1E) XP® Rabbit mAb 13198||20 µl||
||H M R||72||Rabbit IgG|
|Phospho-Zap-70 (Tyr319)/Syk (Tyr352) (65E4) Rabbit mAb 2717||20 µl||
||H M||70, 72||Rabbit IgG|
|DAP12 (D7G1X) Rabbit mAb 12492||20 µl||
||H M||10, 12||Rabbit IgG|
|Anti-rabbit IgG, HRP-linked Antibody 7074||100 µl||
Monoclonal antibodies are produced by immunizing animals with synthetic peptides corresponding to residues surrounding Gly215 of mouse TREM2 protein, near the amino terminus of mouse TREM2 protein, Asn463 of human Syk protein, Tyr319 of human Zap-70, and near the carboxy terminus of human DAP12 protein.
Alzheimer's Disease (AD) is one of the most common neurodegenerative diseases worldwide. Clinically, it is characterized by the presence of extracellular amyloid plaques and intracellular neurofibrillary tangles, resulting in neuronal dysfunction and cell death. Triggering receptor expressed on myeloid cells 2 (TREM2), a protein localized at the membrane of innate immune cells, including microglia in the brain, has been genetically linked to AD, with specific variants increasing disease risk by as much as threefold (1,2). The TREM2 receptor is a single-pass type I membrane glycoprotein that consists of an extracellular immunoglobulin-like domain, a transmembrane domain, and a cytoplasmic tail. Upon activation, TREM2 interacts with the tyrosine kinase-binding protein DNAX-activating protein 12 (DAP12, TYROBP) to form a receptor-signaling complex. The DAP12 protein structure consists of a short extracellular domain, a transmembrane domain, and a cytoplasmic immunoreceptor tyrosine-based activation motif (ITAM) (2-9). ITAMs function as a binding site for tyrosine kinases, including spleen tyrosine kinase (Syk). Syk is comprised of two tandem amino-terminal Src homology (SH) 2 domains separated by an SH2-kinase linker, and a C-terminal tyrosine kinase domain, separated from the SH2 domains by an inter-domain linker. When Syk binds to an ITAM, it changes conformation, allowing for residues within the inter-domain linker region, including Tyr352, to become phosphorylated. Residues within the activation loop subsequently become phosphorylated, leading to full Syk activation. Tyr525 and Tyr526 are located in the activation loop of the Syk kinase domain and phosphorylation at these residues (equivalent to Tyr519/520 of mouse Syk) is essential for Syk function (10-12). This activation can lead to the mediation of a variety of cellular responses, including proliferation, differentiation, inflammation, and phagocytosis. Evidence suggests that TREM2 and DAP12 may act in a Syk-dependent manner to drive microglial cellular responses in AD (2,4-8,13).
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