Product Pathways - Neuroscience
TREM2 (D8I4C) Rabbit mAb #91068
|91068S||100 µl ( 10 western blots )||￥3,100.00 现货查询||购买询价|
|91068||carrier free & custom formulation / quantity||email request|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation, IF-IC=Immunofluorescence (Immunocytochemistry),
Specificity / Sensitivity
TREM2 (D8I4C) Rabbit mAb recognizes endogenous levels of total TREM2 protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu221 of human TREM2 protein.
Confocal immunofluorescent analysis of THP-1 (positive, left) and HL-60 (negative, right) cells using TREM2 (D8I4C) Rabbit mAb (green). Actin filaments were labeled with DyLight™ 554 Phalloidin #13054 (red). Blue pseudocolor = DRAQ5® #4084 (fluorescent DNA dye).
Western blot analysis of extracts from THP-1, HL-60, and Jurkat cells using TREM2 (D8I4C) Rabbit mAb (upper) and β-Actin (D6A8) Rabbit mAb #8457 (lower).
Immunoprecipitation of TREM2 from THP-1 cell extracts. Lane 1 is 10% input, lane 2 is Rabbit (DA1E) mAb IgG XP® Isotype Control #3900, and lane 3 is TREM2 (D8I4C) Rabbit mAb. Western blot analysis was performed using TREM2 (D8I4C) Rabbit mAb.
The triggering receptor expressed on myeloid cells 2 (TREM2) protein is an innate immune receptor that is expressed on the cell surface of microglia, macrophages, osteoclasts, and immature dendritic cells (1). 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. TREM2 interacts with the tyrosine kinase-binding protein DAP12 to form a receptor-signaling complex (2). The TREM2 protein plays a role in innate immunity and a rare functional variant (R47H) of TREM2 is associated with the late-onset risk of Alzheimer’s disease (1,3). Research studies using mouse models of Alzheimer’s disease indicate that deficiency and haploinsufficiency of TREM2 can lead to increased β-amyloid (Aβ) accumulation as a result of dysfunctional microglia response (4). These results agree with the distribution of TREM2 in human brain regions (e.g., white matter, the hippocampus, and neocortex) that are involved in Alzheimer's disease pathology (2). In addition, amyloid plaque formation induces expression of TREM2 and amyloid phagocytosis (5). Loss-of-function mutations in the corresponding TREM2 or DAP12 genes can result in Nasu-Hakola disease, a rare form of progressive presenile dementia that results from polycystic osseous lesions (6).
- Colonna, M. (2003) Nat Rev Immunol 3, 445-53.
- Jonsson, T. et al. (2013) N Engl J Med 368, 107-16.
- Boutajangout, A. and Wisniewski, T. (2013) Int J Cell Biol 2013, 576383.
- Wang, Y. et al. (2015) Cell 160, 1061-71.
- Melchior, B. et al. (2010) ASN Neuro 2, e00037.
- Klünemann, H.H. et al. (2005) Neurology 64, 1502-7.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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