Sign in or Register   Sign in or Register
  |  

Mouse Anti-NOD1 Recombinant Antibody (CBWJN-1458) (CBMAB-N2861-WJ)

This product is a Mouse antibody that recognizes NOD1. The antibody CBWJN-1458 can be used for immunoassay techniques such as: WB, IHC.
See all NOD1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBWJN-1458
Antibody Isotype
IgG2b
Application
WB, IHC

Basic Information

Specificity
Human
Antibody Isotype
IgG2b
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Lyophilized
Buffer
PBS
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Nucleotide Binding Oligomerization Domain Containing 1
Introduction
This gene encodes a member of the nucleotide-binding oligomerization domain (NOD)-like receptor (NLR) family of proteins. The encoded protein plays a role in innate immunity by acting as a pattern-recognition receptor (PRR) that binds bacterial peptidoglycans and initiates inflammation. This protein has also been implicated in the immune response to viral and parasitic infection. Major structural features of this protein include 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. Mutations in this gene are associated with asthma, inflammatory bowel disease, Behcet disease and sarcoidosis in human patients. [provided by RefSeq, Aug 2017]
Entrez Gene ID
UniProt ID
Alternative Names
Nucleotide Binding Oligomerization Domain Containing 1; Nucleotide-Binding Oligomerization Domain, Leucine Rich Repeat And CARD Domain Containing 1; Caspase Recruitment Domain-Containing Protein 4; Caspase Recruitment Domain Family, Member 4; NLR Family, CARD Domain Containing 1; CARD4; Nucleotide-Binding Oligomerization Domain-Containing Protein 1; CLR7.1; NLRC1;
Function
Pattern recognition receptor (PRR) that detects bacterial peptidoglycan fragments and other danger signals and thus participates in both innate and adaptive immune responses (PubMed:19043560, PubMed:22672233, PubMed:27099311).
Ligand binding triggers oligomerization that facilitates the binding and subsequent activation of the receptor interacting protein-2/RIPK2. RIPK2 subsequently recruits the kinase TAK1 to activate NF-kappa-B and MAPK signaling pathways (PubMed:10880512).
Regulates also antiviral response elicited by dsRNA and the expression of RLR pathway members by targeting IFIH1 and TRAF3 to modulate the formation of IFIH1-MAVS and TRAF3-MAVS complexes leading to increased transcription of type I IFNs (PubMed:32169843).
Besides recognizing pathogens, participates in surveillance of cellular homeostasis through sensing and binding to the cytosolic metabolite sphingosine-1-phosphate and then initating inflammation process (PubMed:33942347).
In addition, plays a role in insulin trafficking in beta cells in a cell-autonomous manner. Mechanistically, upon recognizing cognate ligands, NOD1 and RIPK2 localize to insulin vesicles where they recruit RAB1A to direct insulin trafficking through the cytoplasm (By similarity).
Biological Process
Activation of cysteine-type endopeptidase activity involved in apoptotic processManual Assertion Based On ExperimentIDA:MGI
Apoptotic processManual Assertion Based On ExperimentTAS:ProtInc
Cellular response to muramyl dipeptideManual Assertion Based On ExperimentIMP:UniProtKB
Defense responseManual Assertion Based On ExperimentTAS:HGNC-UCL
Defense response to bacteriumManual Assertion Based On ExperimentIDA:HGNC-UCL
Defense response to Gram-positive bacteriumIEA:Ensembl
Detection of bacteriumManual Assertion Based On ExperimentIDA:HGNC-UCL
Detection of biotic stimulusManual Assertion Based On ExperimentTAS:HGNC-UCL
Inflammatory responseManual Assertion Based On ExperimentTAS:HGNC-UCL
Innate immune responseIEA:UniProtKB-KW
Intracellular signal transductionManual Assertion Based On ExperimentIDA:HGNC-UCL
Pattern recognition receptor signaling pathwayManual Assertion Based On ExperimentIDA:UniProtKB
Positive regulation of cell deathIEA:Ensembl
Positive regulation of cysteine-type endopeptidase activity involved in apoptotic processManual Assertion Based On ExperimentIDA:MGI
Positive regulation of dendritic cell antigen processing and presentationISS:BHF-UCL
Positive regulation of ERK1 and ERK2 cascadeIEA:Ensembl
Positive regulation of I-kappaB kinase/NF-kappaB signalingManual Assertion Based On ExperimentIDA:MGI
Positive regulation of interleukin-1 beta productionIEA:Ensembl
Positive regulation of interleukin-6 productionIEA:Ensembl
Positive regulation of interleukin-8 productionManual Assertion Based On ExperimentIDA:HGNC-UCL
Positive regulation of JNK cascadeIEA:Ensembl
Positive regulation of NF-kappaB transcription factor activityManual Assertion Based On ExperimentIDA:UniProtKB
Positive regulation of NIK/NF-kappaB signalingManual Assertion Based On ExperimentIMP:UniProtKB
Positive regulation of nitric-oxide synthase activityIEA:Ensembl
Positive regulation of tumor necrosis factor productionIEA:Ensembl
Positive regulation of xenophagyIEA:Ensembl
Regulation of apoptotic processIEA:InterPro
Signal transductionManual Assertion Based On ExperimentTAS:HGNC-UCL
Cellular Location
Cytoplasm
Cell membrane
Apical cell membrane
Basolateral cell membrane
Detected in the cytoplasm and at the cell membrane. Following bacterial infection, localizes to bacterial entry sites in the cell membrane. Recruited to the basolateral and apical membranes in polarized epithelial cells.
PTM
Palmitoylated. Palmitoylation is required for proper recruitment to the bacterial entry site and hence for proper signaling upon cognate peptidoglycan detection
Ubiquitinated. 'Lys-48'-linked polyubiquitination by RNF34 promotes proteasomal degradation and thereby negatively regulates NOD1 for instance in NF-kappa-B activation.

Mao, D., Inoue, H., & Goda, S. (2024). Role of the nucleotide-binding oligomerization domain-containing protein 1 pathway in the development of periodontitis. Journal of Oral Biosciences.

Apaza, C. J., Días, M., García Tejedor, A., Boscá, L., & Laparra Llopis, J. M. (2024). Contribution of Nucleotide-Binding Oligomerization Domain-like (NOD) Receptors to the Immune and Metabolic Health. Biomedicines, 12(2), 341.

Dixon, C. L., Wu, A., & Fairn, G. D. (2023). Multifaceted roles and regulation of nucleotide-binding oligomerization domain containing proteins. Frontiers in Immunology, 14, 1242659.

Chen, Z., Zhao, Z., Liu, Y., Imran, M., Rao, J., Cai, N., ... & Cao, S. (2022). Nucleotide-Binding Oligomerization Domain 1 (NOD1) positively regulates neuroinflammation during japanese encephalitis virus infection. Microbiology Spectrum, 10(3), e02583-21.

Wei, X., Liu, Y., Li, W., & Shao, X. (2022). Nucleotide-binding oligomerization domain-containing protein 1 regulates inflammatory response in endometriosis. Current Protein and Peptide Science, 23(2), 121-128.

Ahn, M. Y., Kang, J. K., Kwon, S. M., Yoon, H. E., & Yoon, J. H. (2020). Expression of nucleotide-binding oligomerization domain 1 and 2 in oral lichen planus. Journal of Dental Sciences, 15(1), 1-8.

Ma, X., Zhang, W., Xu, C., Zhang, S., Zhao, J., Pan, Q., & Wang, Z. (2020). Nucleotide-binding oligomerization domain protein 1 enhances oxygen-glucose deprivation and reperfusion injury in cortical neurons via activation of endoplasmic reticulum stress-mediated autophagy. Experimental and Molecular Pathology, 117, 104525.

Vlacil, A. K., Schuett, J., Ruppert, V., Soufi, M., Oberoi, R., Shahin, K., ... & Grote, K. (2020). Deficiency of Nucleotide-binding oligomerization domain-containing proteins (NOD) 1 and 2 reduces atherosclerosis. Basic Research in Cardiology, 115, 1-12.

Lassailly, G., Saleh, M. B., Leleu-Chavain, N., Ningarhari, M., Gantier, É., Carpentier, R., ... & Dubuquoy, L. (2019). Nucleotide-binding oligomerization domain 1 (NOD1) modulates liver ischemia reperfusion through the expression adhesion molecules. Journal of hepatology, 70(6), 1159-1169.

Chen, Y., Yu, S. L., Li, Y. P., & Zhang, M. M. (2019). Nucleotide-binding oligomerization domain (NOD) plays an important role in neonatal infection. International journal of biological macromolecules, 121, 686-690.

Ask a question We look forward to hearing from you.
0 reviews or Q&As
Loading...
Have you used Mouse Anti-NOD1 Recombinant Antibody (CBWJN-1458)?
Submit a review and get a Coupon or an Amazon gift card. 20% off Coupon $30 eGift Card
Submit a review
Loading...
For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

Online Inquiry

Documents

Contact us

  • Tel: (USA)
  • (UK)
  • Fax:
  • Email:

Submit A Review

Go to
Compare