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LECT2 encodes a secreted, 16 kDa protein that acts as a chemotactic factor to neutrophils and stimulates the growth of chondrocytes and osteoblasts. Additionally we are shipping LECT2 Kits (14) and LECT2 Proteins (9) and many more products for this protein.
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Human Monoclonal LECT2 Primary Antibody for WB - ABIN1108031
Rudinskaya, Poltoranina, Baranov, Petrovichev, Voytenkov, Tretyakov: D11, a novel monoclonal antibody specific for human mature macrophages and peripheral blood monocytes. in Immunology letters 1992
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Human Monoclonal LECT2 Primary Antibody for IP - ABIN1108032
Yamagoe, Mizuno, Suzuki: Molecular cloning of human and bovine LECT2 having a neutrophil chemotactic activity and its specific expression in the liver. in Biochimica et biophysica acta 1998
Show all 5 references for ABIN1108032
findings indicated that serum LECT2 level is negatively associated with the presence of diabetic retinopathy and suggest that low circulating LECT2 level is a risk factor for diabetic retinopathy
LECT2 amyloidosis is prevalent among Hispanic decedents in New Mexico.
Localized LECT2 amyloidosis of the adrenal gland with coexisting MGUS: a diagnostic challenge.
LECT2 immunostain is useful in confirming subtype of amyloid within the liver in ALECT2..
There were no mutations detected in the LECT2 gene, although all renal leukocyte chemotactic factor 2 amyloidosis patients tested were homozygous for the G nucleotide in a non-synonymous SNP at position 172.
LECT2 is regulated by beta-catenin (show CTNNB1 Antibodies) in HCC (show FAM126A Antibodies) in both mice and men, but serum LECT2 reflects beta-catenin (show CTNNB1 Antibodies) activity only in mice. Serum LECT2 could be a potential biomarker of HCC (show FAM126A Antibodies) in patients.
First Nations people from British Columbia who presented with chronic kidney disease, were found to be due to LECT2 amyloidosis.
The study indicates that serum LECT2 levels are increased by obesity and fatty liver, and suggests that LECT2 is a novel obesity-related protein.
The data from this study show that weak LECT2 staining should be regarded as indeterminate or a negative result and does not per se allow diagnosis of specific amyloid type. The diagnosis of LECT2 renal amyloidosis may require LMD/MS confirmation.
These results demonstrate the involvement of LECT2 in glucose metabolism and suggest that LECT2 may be a therapeutic target for obesity-associated insulin (show INS Antibodies) resistance.
We found that treatment with LECT2 enhanced H. pylori killing and nitric oxide production in macrophages. In addition, DNA-binding activity and nuclear translocation of p65 (show NFkBP65 Antibodies) were up-regulated by LECT2 treatment
LECT2 improves protective immunity in bacterial sepsis, possibly as a result of enhanced macrophages functions via the CD209a receptor.
Zinc stabilizes the LECT2 structure.
Data suggest the involvement of LECT2 in the regulation of fatal SEA (show Slc25a1 Antibodies)-induced toxicity in d-GalN (show GAL Antibodies)-sensitized mice.
Our results suggest that LECT2 regulates neuritic extension through microtubular morphallaxis through the control of katanin-P60 (show STIP1 Antibodies) levels.
Our results show that LECT2 regulates the extension of axons and dendrites and the expressions of NGF (show NGFB Antibodies), BDNF (show BDNF Antibodies) and NT-3 (show NTF3 Antibodies) during neuronal development.
LECT2, which encodes a protein with chemotactic properties for human neutrophils, is a direct target gene of Wnt (show WNT2 Antibodies)/beta-catenin (show CTNNB1 Antibodies) signaling in the liver.
LECT2 directly suppresses the development of collagen antibody induced arthritis
This gene encodes a secreted, 16 kDa protein that acts as a chemotactic factor to neutrophils and stimulates the growth of chondrocytes and osteoblasts. This protein has high sequence similarity to the chondromodulin repeat regions of the chicken myb-induced myeloid 1 protein. A polymorphism in this gene may be associated with rheumatoid arthritis.
, leukocyte cell-derived chemotaxin-2
, chondromodulin II
, cell-derived chemotaxin 2
, myeloid protein (mim-1)
, myeloid protein 1