Nucleotide-Binding Oligomerization Domain-Containing Protein 1 (NOD1) Antibody
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Description
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.
Documents del producto
Product specifications
| Category | Primary Antibodies |
| Immunogen Target | Nucleotide-Binding Oligomerization Domain-Containing Protein 1 (NOD1) |
| Host | Rabbit |
| Reactivity | Human, Mouse |
| Recommended Dilution | WB: 1/1000, IHC-P: 1/500. Not tested in IHC-F. Optimal dilutions/concentrations should be determined by the end user. |
| Clonality | Polyclonal |
| Conjugation | Unconjugated |
| Isotype | IgG |
| Purification | Purified through a protein A column, followed by peptide affinity purification. |
| Size 1 | 80 µl |
| Size 2 | 400 µl |
| Form | Liquid |
| Tested Applications | ELISA, WB, IHC |
| Buffer | PBS containing 0.09% sodium azide. |
| Availability | Shipped within 5-10 working days. |
| Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | Q9Y239 |
| Alias | CARD4, CLR7.1, NLRC1, nucleotide binding oligomerization domain containing 1 |
| Background | Antibody anti-NOD1 |
| Status | RUO |
Descripción
NOD1 (Nucleotide-binding Oligomerization Domain Containing 1) is an intracellular protein involved in the immune response, particularly in the recognition of bacterial pathogens. It is a member of the NOD-like receptor (NLR) family and plays a crucial role in activating innate immunity. NOD1 detects specific bacterial peptidoglycan fragments, triggering a signaling cascade that leads to the activation of nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) and other inflammatory pathways. This process results in the production of pro-inflammatory cytokines that help recruit immune cells to the site of infection. NOD1's role in inflammation also links it to various diseases, including inflammatory bowel disease (IBD), atherosclerosis, and other conditions where immune system dysregulation is evident. NOD1 has also been implicated in cancer biology due to its influence on tumor-promoting inflammatory responses.
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Nucleotide-Binding Oligomerization Domain-Containing Protein 1 (NOD1) Antibody
NOD1 Antibody is a Rabbit Polyclonal antibody against NOD1. 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.
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Nucleotide-Binding Oligomerization Domain-Containing Protein 1 (NOD1) Antibody
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.
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