|Datasheet||Specific References||Reviews||Related Products||Protocols|
|Vector Type||Mammalian Expression Vector|
|Expression Method||Constiutive, Stable / Transient|
|Selection In Mammalian Cells||Hygromycin|
A polyhistidine-tag is an amino acid motif in proteins that consists of at least five histidine (His) residues, often at the N- or C-terminus of the protein.
Polyhistidine-tags are often used for affinity purification of polyhistidine-tagged recombinant proteins expressed in Escherichia coli and other prokaryotic expression systems.
|Human TREM1 ORF mammalian expression plasmid, C-GFPSpark tag||HG10511-ACG|
|Human TREM1 ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG10511-ACR|
|Human TREM1 ORF mammalian expression plasmid, C-Flag tag||HG10511-CF|
|Human TREM1 ORF mammalian expression plasmid, C-His tag||HG10511-CH|
|Human TREM1 ORF mammalian expression plasmid, C-Myc tag||HG10511-CM|
|Human TREM1 ORF mammalian expression plasmid, C-HA tag||HG10511-CY|
|Human TREM1 Gene cDNA clone plasmid||HG10511-M|
|Human TREM1 ORF mammalian expression plasmid, N-Flag tag||HG10511-NF|
|Human TREM1 ORF mammalian expression plasmid, N-His tag||HG10511-NH|
|Human TREM1 ORF mammalian expression plasmid, N-Myc tag||HG10511-NM|
|Human TREM1 ORF mammalian expression plasmid, N-HA tag||HG10511-NY|
|Human TREM1 natural ORF mammalian expression plasmid||HG10511-UT|
|Learn more about expression Vectors|
TREM1 (triggering receptor expressed on myeloid cells) is a type I transmembrane protein with a single Ig-like domain, and is selectively expressed on blood neutrophils and a subset of monocytes. As a member of the growing family of receptors related to NK cell receptors, TREM1 activates downstream signaling events with the help of an adapter protein called DAP12. Expression of TREM1 is up-regulated by bacterial LPS, a ligand for TLR4, as well as lipoteichoic acid. Although its natural ligand has not been identified, engagement of TREM1 with agonist mAbs triggers secretion of the proinflammatory cytokines TNF-α and IL-1β, as well as chemokines such as IL-8 and monocyte chemoattractant protein (MCP)-1. Intracellularly, TREM1 induces Ca2+ mobilization and tyrosine phosphorylation of extracellular signal-related kinase 1 (ERK1), ERK2 and phospholipase C-γ. In an animal model of LPS-induced septic shock, blockade of TREM1 signaling inhibited hyperresponsiveness and death. Thus, it has been demonstrated that TREM1 performs a critical function in immune responses involved in host defense against microbial challenges, and is suggested to be a potential therapeutic target for septic shock.