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Human LBP Protein expressed in Wheat germ - ABIN1309198
Gu, Werner, Bergmann, Whitcomb, Büchler, Fortunato: Necro-inflammatory response of pancreatic acinar cells in the pathogenesis of acute alcoholic pancreatitis. dans Cell death & disease 2013
Show all 2 Pubmed References
Human LBP Protein expressed in - ABIN624268
Gladigau, Haselmayer, Scharrer, Munder, Prinz, Lackner, Schild, Stein, Radsak: A role for Toll-like receptor mediated signals in neutrophils in the pathogenesis of the anti-phospholipid syndrome. dans PLoS ONE 2012
This study shows a remarkable reversal of amyloid fibrin formation by LBP (Montrer RPSA Protéines) addition to the plasma of Parkinson's Disease patients .
Serum LBP (Montrer RPSA Protéines) levels are associated with arterial stiffness, independent of obesity and traditional cardiovascular risk factors, especially in men with type 2 diabetes.
novel observation that sCD14 compared with lipopolysaccharide binding protein, offers a preferred target to ameliorate TLR especially TLR4 (Montrer TLR4 Protéines)-induced inflammation and insulin (Montrer INS Protéines) resistance in human obesity and metabolic syndrome
LBP (Montrer RPSA Protéines), an endotoxemia associated protein might be used as an inflammatory biomarker of both infectious and non-infectious origins in HCV-infected subjects
Data show that after matching for gender, age, and body mass index (BMI), serum lipopolysaccharide-binding protein (LBP) does not improve prediction of the development of type 2 diabetes mellitus (T2DM) independently.
The main findings of this study are that, in acute stroke patients, levels of LBP (Montrer RPSA Protéines), IL-10 (Montrer IL10 Protéines), IL-6 (Montrer IL6 Protéines) and CRP (Montrer CRP Protéines) show a different time course in patients with and without post-stroke infection.
Serum LBP (Montrer RPSA Protéines) level is significantly elevated in polycystic ovary syndrome women and is associated with insulin (Montrer INS Protéines) resistance.
LBP (Montrer RPSA Protéines) serves not only as an extracellular LPS (Montrer IRF6 Protéines) shuttle but in addition facilitates intracellular transport of LPS (Montrer IRF6 Protéines).
LBP (Montrer RPSA Protéines) level was not significantly different in neutropenic systemic inflammatory response syndrome patients and sepsis patients.
Report increased secretion of Fetuin A (Montrer AHSG Protéines), LBP (Montrer RPSA Protéines) and HMGB-1 (Montrer HMGB1 Protéines) from subcutaneous adipose tissue in metabolic syndrome.
The LBP gene is a macrophage-specific LXR target that promotes foam cell survival and atherogenesis.
LBP is a critical factor in the development of non-alcoholic fatty liver disease.
LBP is a proinflammatory soluble adipokine that acts as a brake for adipogenesis, strengthening the negative effects of palmitate and LPS (Montrer TLR4 Protéines) on adipocyte differentiation.
Differential expression of LBP and TGFB1 (Montrer TGFB1 Protéines), along with other genes, in different mesenchymal stromal cells preparations, produces the variable responses to external stimuli.
findings describe a novel role for LBP in normal hippocampal development and raise the possibility that some of the behavioral sequelae of early life stress are mediated by reduced expression of LBP during a critical period of neurodevelopment.
The amino acid sequence for two mimic epitopes of the inflammatory site of LBP were determined to be WKAQKRFMKKSG and LKTRKLFWKYKD.
LBP plays an important role in early alcohol-induced liver injury by enhancing LPS (Montrer TLR4 Protéines)-induced signal transduction, most likely in Kupffer cells.
LBP plays an important role in resistance to lethal Salmonella peritonitis (but not to oral or intravenous infection) by facilitating the role of neutrophils in mediating acute inflammation.
role LBP plays in local pulmonary immune defenses to bacterial challenge
In the case of intraperitoneal infection of LBP-deficient mice with Salmonella typhimurium, no local inflammatory response is evident, neutrophil influx is delayed, and the mice succumb to the infection.
Our study provides an overview of the gene expression profile between wild LBP and mutant LBP on the LPS (Montrer IRF6 Protéines)-induced inflammatory response of bovine mammary epithelial cells , which will lead to further understanding of the potential effects of LBP mutations on bovine mammary glands.
The presence of lipopolysaccharide binding protein (LBP) and alpha1-acid glycoprotein (AGP (Montrer ORM1 Protéines)) was demonstrated in all seven adipose tissue depots. Expression of AGP (Montrer ORM1 Protéines) and LBP suggests that they may have roles as local and systemic inflammatory adipokines.
One possible anti-inflammatory mechanism can be attributed to the negative role of BRLBP (Montrer IGFBP2 Protéines) in suppressing TLR4 (Montrer TLR4 Protéines)/NF-kappaB (Montrer NFKB1 Protéines) activation mediated by LPS (Montrer IRF6 Protéines). These findings suggested that BRLBP (Montrer IGFBP2 Protéines) may be a useful agent to treat LPS (Montrer IRF6 Protéines)-induced mastitis
Single nucleotide polymorphisms in the lipopolysaccharide-binding protein may hold the secret of susceptibility to clinical mastitis in Chinese Holstein.
The protein encoded by this gene is involved in the acute-phase immunologic response to gram-negative bacterial infections. Gram-negative bacteria contain a glycolipid, lipopolysaccharide (LPS), on their outer cell wall. Together with bactericidal permeability-increasing protein (BPI), the encoded protein binds LPS and interacts with the CD14 receptor, probably playing a role in regulating LPS-dependent monocyte responses. Studies in mice suggest that the encoded protein is necessary for the rapid acute-phase response to LPS but not for the clearance of LPS from circulation. This protein is part of a family of structurally and functionally related proteins, including BPI, plasma cholesteryl ester transfer protein (CETP), and phospholipid transfer protein (PLTP).
BPI fold containing family D, member 2
, LPS-binding protein
, lipopolysaccharide-binding protein
, lipopolysaccharide binding protein
, lipopolysaccharide-binding protein-like