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Natural killer (NK) cells express multiple calcium-dependent (C-type) lectin-like receptors, such as CD94 (KLRD1\; MIM 602894) and NKG2D (KLRC4\; MIM 602893), that interact with major histocompatibility complex class I molecules and either inhibit or activate cytotoxicity and cytokine secretion. Additionally we are shipping C-Type Lectin Domain Family 1, Member B Antibodies (85) and C-Type Lectin Domain Family 1, Member B Kits (9) and many more products for this protein.
Showing 8 out of 10 products:
Mouse (Murine) CLEC1B Protein expressed in HEK-293 - ABIN2666791
Bénézech, Nayar, Finney, Withers, Lowe, Desanti, Marriott, Watson, Caamaño, Buckley, Barone: CLEC-2 is required for development and maintenance of lymph nodes. in Blood 2014
Show all 6 references for ABIN2666791
Mouse (Murine) CLEC1B Protein expressed in Human Cells - ABIN2007639
Hughes, Navarro-Núñez, Finney, Mourão-Sá, Pollitt, Watson: CLEC-2 is not required for platelet aggregation at arteriolar shear. in Journal of thrombosis and haemostasis : JTH 2010
Show all 3 references for ABIN2007639
Human CLEC1B Protein expressed in Human Cells - ABIN2003677
Christou, Pearce, Watson, Mistry, Pollitt, Fenton-May, Johnson, Jackson, Watson, OCallaghan: Renal cells activate the platelet receptor CLEC-2 through podoplanin. in The Biochemical journal 2008
Show all 3 references for ABIN2003677
CLEC-2 regulates Akt and MAPK downstream of PI3K and PKC, leading to phosphorylation and inhibition of GSK3alpha/beta, and enhanced platelet aggregation and secretion.
Data (including data from studies using recombinant proteins) suggest that a diverse range of ligands activate platelets through activation/phosphorylation (show CD36 Proteins) of C (show GP6 Proteins)D36/GPVI (glycoprotein VI) and/or CLEC-2 (C-type lectin-like receptor-2).
PI3K (show PIK3CA Proteins) and Tec (show NR4A3 Proteins) family kinases play a crucial role in the regulation of platelet activation and Syk (show SYK Proteins) phosphorylation downstream of the CLEC-2 receptor
fucoidan is a novel CLEC-2 receptor agonist that activates platelets through a SFK-dependent signaling pathway
Dimerization of two phosphorylated CLEC-2 molecules leads to recruitment of the tyrosine kinase Syk via its tandem SH2 domains and initiation of a downstream signaling cascade
A differential proteomic analysis of basal and rhodocytin-activated platelets with the aim of providing novel clues on CLEC-2 signaling regulation.
The glycosylation sites (N120 and N134) are necessary for the surface expression of CLEC-2.
Shedding of CLEC-2 from the cell surface may reflect increased expression of this membrane protein and serve as a marker of disease activity.
Here, the bidirectional relationship between CLEC-2 and podoplanin (show PDPN Proteins) is described and considered in the context of tumour growth and metastasis.
platelets regulate blood/lymphatic vessel separation by inhibiting the proliferation, migration, and tube formation of LECs, mainly because of the release of BMP-9 (show GDF2 Proteins) upon activation by CLEC-2/podoplanin (show PDPN Proteins) in
A reciprocal interaction between CLEC-2 on megakaryocytes and PDPN (show PDPN Proteins) on Bone marrow (BM) Fibroblastic reticular cell-like cells contributes to the periarteriolar megakaryopoietic microenvironment in mouse BM.
A role for CLEC2 as a regulator of macrophage polarity and Kupffer cell polarity, lipid and glucose homeostasis
Data indicate that C-type lectin-like receptor-2 (CLEC-2) is highly expressed on bone marrow megakaryocytes (Mks (show MKKS Proteins)).
Data (including data from studies in transgenic mice) suggest that a diverse range of ligands activate platelets through activation/phosphorylation of Cd36 (show CD36 Proteins)/GPVI (show GP6 Proteins) (glycoprotein VI) and/or Clec-2 (C-type lectin-like receptor-2).
Podoplanin (show PDPN Proteins) and CLEC-2 critically drive the formation and integrity of developing cerebral blood vessels.
PI3K and Tec (show NR4A3 Proteins) family kinases play a crucial role in the regulation of platelet activation and Syk (show SYK Proteins) phosphorylation downstream of the CLEC-2 receptor
CLEC-2 signaling promotes adhesion to Podoplanin (show PDPN Proteins) and regulation of Podoplanin (show PDPN Proteins) signaling, thereby contributing to lymphatic vasculature development.
Under resting conditions, when FRCs are unlikely to encounter mature DCs expressing the PDPN (show PDPN Proteins) receptor CLEC-2, PDPN (show PDPN Proteins) endowed FRCs with contractile function and exerted tension within the reticulum.
Functional studies of platelets from Ceacam2 (show CEACAM2 Proteins)(-/-)-deficient mice (Cc2 (show TSG101 Proteins)(-/-)) revealed that CEACAM2 (show CEACAM2 Proteins) serves to negatively regulate collagen glycoprotein VI (platelet) (GPVI (show GP6 Proteins))-FcRgamma (show FCER1G Proteins)-chain and the C-type lectinlike receptor 2 (CLEC-2) signaling
The results demonstrated that CLEC-2-dependent platelet activation is insensitive to cGMP-elevation and only partially sensitive to cAMP-elevation.
Natural killer (NK) cells express multiple calcium-dependent (C-type) lectin-like receptors, such as CD94 (KLRD1\; MIM 602894) and NKG2D (KLRC4\; MIM 602893), that interact with major histocompatibility complex class I molecules and either inhibit or activate cytotoxicity and cytokine secretion. CLEC2 is a C-type lectin-like receptor expressed in myeloid cells and NK cells (Colonna et al., 2000
C-type lectin domain family 1, member B
, C-type lectin domain family 1 member B
, c-type lectin domain family 1 member B-like
, C-type lectin-like receptor 2
, C-type lectin-like receptor-2