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anti-Human NOD1 Antikörper:
anti-Mouse (Murine) NOD1 Antikörper:
anti-Rat (Rattus) NOD1 Antikörper:
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Human Polyclonal NOD1 Primary Antibody für IHC, IHC (p) - ABIN4340241
Swaan, Bensman, Bahadduri, Hall, Sarkar, Bao, Khantwal, Ekins, Knoell: Bacterial peptide recognition and immune activation facilitated by human peptide transporter PEPT2. in American journal of respiratory cell and molecular biology 2008
Show all 2 Pubmed References
Human Polyclonal NOD1 Primary Antibody für IHC (fro), IHC (p) - ABIN537419
Necchi, Sommi, Vanoli, Manca, Ricci, Solcia: Proteasome particle-rich structures are widely present in human epithelial neoplasms: correlative light, confocal and electron microscopy study. in PLoS ONE 2011
Human Polyclonal NOD1 Primary Antibody für IF (p), IHC (p) - ABIN872332
Arentsen, Qian, Gkotzis, Femenia, Wang, Udekwu, Forssberg, Diaz Heijtz: The bacterial peptidoglycan-sensing molecule Pglyrp2 modulates brain development and behavior. in Molecular psychiatry 2016
Human Polyclonal NOD1 Primary Antibody für ELISA, WB - ABIN4235349
Lu, Zou, Feng, Yuan, Gu, Li, Li, Jin, Li: Association of NOD1 (CARD4) insertion/deletion polymorphism with susceptibility to IBD: a meta-analysis. in World journal of gastroenterology 2010
Human Polyclonal NOD1 Primary Antibody für WB - ABIN1169390
Costello, Joyce, Abrahams: NOD protein expression and function in first trimester trophoblast cells. in American journal of reproductive immunology (New York, N.Y. : 1989) 2006
Human Polyclonal NOD1 Primary Antibody für IHC (p), WB - ABIN4340243
Scott, Chen, Sun, Billiar: Hepatocytes express functional NOD1 and NOD2 receptors: a role for NOD1 in hepatocyte CC and CXC chemokine production. in Journal of hepatology 2010
Human Polyclonal NOD1 Primary Antibody für ELISA, FACS - ABIN4340244
Hosokawa, Hirao, Yumoto, Washio, Nakanishi, Takegawa, Kitamura, Matsuo: Functional Roles of NOD1 in Odontoblasts on Dental Pulp Innate Immunity. in BioMed research international 2016
study provides structural and dynamic insights into the NOD1-RIP2 (zeige ARHGEF28 Antikörper) oligomer formation, which will be crucial in understanding the molecular basis of NOD1-mediated CARD-CARD interaction in higher and lower eukaryotes
Nucleotide-binding oligomerization domain (NOD1) was the most significantly associated gene when analyzing exonic rare variants (RVs) in chromosome 7p to carotid bifurcation intima-media thickness (bIMT).
Fusion of human SGT1 (zeige SUGT1 Antikörper) (hSGT1 (zeige ECD Antikörper)) to NOD1 LRR significantly enhanced the solubility, and the fusion protein was stabilized by coexpression of mouse Hsp90alpha (zeige HSP90AA2 Antikörper).
the results suggest that the chronic activation of NOD1 and NOD2 (zeige NOD2 Antikörper) receptors might play a role in the development of gastric cancer.
this study reveals that LRRK2 (zeige LRRK2 Antikörper) is a new positive regulator of Rip2 (zeige ARHGEF28 Antikörper) and promotes inflammatory cytokine induction through the Nod1/2-Rip2 (zeige ARHGEF28 Antikörper) pathway.
Finally, NOD1 agonist increased the formation of cranial and subintestinal vessel plexus in zebrafish, and this effect was abrogated by concurrent PPARgamma (zeige PPARG Antikörper) activation. Overall, these findings identify a PPARgamma (zeige PPARG Antikörper)-miR (zeige MLXIP Antikörper)-125a-NOD1 signaling axis in endothelial cells that is critical in the regulation of inflammation-mediated angiogenesis.
NOD1/2 gene variants are not linked with T2DM and IR.
findings show that NOD1, a PRR (zeige PVRL1 Antikörper) that normally senses bacterial peptidoglycans, is activated by HCV viral polymerase, probably through an interaction with dsRNA, suggesting that NOD1 acts as an RNA ligand recognition receptor.
Brain pericytes can sense Gram-negative bacterial products by both NOD1 and TLR4 (zeige TLR4 Antikörper) receptors, acting through distinct pathways.
NOD1 And NOD2 (zeige NOD2 Antikörper) polymorphisms were associated with increased susceptibility to Guillain-Barre syndrome in a Northern Indian population.
These findings reveal macrophage NOD1 as a cell-specific target to combat diet-induced inflammation past the step of macrophage infiltration, leading to insulin (zeige INS Antikörper) resistance.
The studies establish chronic pancreatitis as an IL-33 (zeige IL33 Antikörper)-dependent inflammation resulting from synergistic interactions between the NOD1 and CCKR signaling pathways.
Results show that the simultaneous absence of Nod1 and Nod2 (zeige NOD2 Antikörper) is associated with accelerated T cell death upon alloantigen encounter, suggesting these proteins might provide new targets to ameliorate T cell responses in a variety of inflammatory states, including those associated with bone marrow or solid organ transplantation.
this study shows that the effect of the gut (zeige GUSB Antikörper) microbiota on bone is dependent on NOD1 and NOD2 (zeige NOD2 Antikörper) signaling
we propose that NOD1 signaling in mesenchymal stromal cells serves as an important pathway underlying the requirement for microbiota in the maintenance of steady-state hematopoiesis
results suggest a previously unappreciated role for the innate immune receptor Nod1 in suppressing colitis-associated tumorigenesis through a T cell-mediated mechanism
NOD1 activation in cardiac fibroblasts induces myocardial fibrosis in a murine model of type 2 diabetes.
this study reveals that LRRK2 (zeige LRRK2 Antikörper) is a new positive regulator of Rip2 (zeige ARHGDIG Antikörper) and promotes inflammatory cytokine induction through the Nod1/2-Rip2 (zeige ARHGDIG Antikörper) pathway.
this paper shows that deletion of NOD1 aggravated bone resorption induced by Gram-negative bacteria, accompanied by an increase in the numbers of osteoclasts
Sertoli cells have a functional NALP3 (zeige NLRP3 Antikörper) inflammasome that modulates NOD1 and pro-IL-1beta (zeige IL1B Antikörper) expression, while NOD2 (zeige NOD2 Antikörper) inversely promoted IL-1beta (zeige IL1B Antikörper) expression.
This gene encodes a member of the NOD (nucleotide-binding oligomerization domain) family. This member is a cytosolic protein. It contains an N-terminal caspase recruitment domain (CARD), a centrally located nucleotide-binding domain (NBD), and 10 tandem leucine-rich repeats (LRRs) in its C terminus. The CARD is involved in apoptotic signaling, LRRs participate in protein-protein interactions, and mutations in the NBD may affect the process of oligomerization and subsequent function of the LRR domain. This protein is an intracellular pattern-recognition receptor (PRR) that initiates inflammation in response to a subset of bacteria through the detection of bacterial diaminopimelic acid. Multiple alternatively spliced transcript variants differring in the 5' UTR have been described, but the full-length nature of these variants has not been determined.
NLR family, CARD domain containing 1
, caspase recruitment domain family, member 4
, caspase recruitment domain-containing protein 4
, nucleotide-binding oligomerization domain, leucine rich repeat and CARD domain containing 1
, nucleotide-binding oligomerization domain-containing protein 1
, caspase recruitment domain 4