Novus Biologicals Rabbit TLR8 Antibody - BSA Free (NBP1-77203) is a polyclonal antibody validated for use in WB, ELISA and ICC/IF. Anti-TLR8 Antibody: Cited in 1 publication. All Novus Biologicals antibodies are covered by our 100% guarantee.
Immunogen
Antibody was raised against a peptide corresponding to 16 amino acids near the middle of human TLR8. The immunogen is located within amino acids 790 - 840 of TLR8. Amino Acid Squence: CASPGDQRGKSIVSLE
Isotype
IgG
Clonality
Polyclonal
Host
Rabbit
Gene
TLR8
Purity
Peptide affinity purified
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107 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
Buffer
PBS
Preservative
0.02% Sodium Azide
Concentration
1 mg/ml
Purity
Peptide affinity purified
Alternate Names for TLR8 Antibody - BSA Free
CD288 antigen
CD288
MGC119599
MGC119600
TLR8
toll-like receptor 8
Background
Toll-like receptor 8 (TLR8) is a member of the TLR family of receptors that play a role in innate immune system activation and the recognition of pathogen-associated molecular patterns (PAMPs) or damage-associated molecular patterns (DAMPs) (1,2). TLRs are type I membrane receptors that can be expressed on either the cell surface or internally, on endosomes (1,2). TLR8 is an endosomal receptor and is activated by pathogenic single stranded (ss) RNA (1-3). TLR8 is located on the X chromosome and is expressed mostly in monocytes/macrophages, neutrophils, and myeloid dendritic cells (1-3). Structurally, TLR8 consists of an extracellular domain, a cysteine-rich region, and transmembrane domain, and a Toll/Interleukin-1 receptor homology (TIR) domain (3,4). The extracellular domain contains a N-terminal leucine rich repeat (LRRNT) and a C-terminal LRR (LRRCT) which have 26 LRRs between them, each approximately 20-30 amino acids (aa), and a Z-loop between LRR14 and LRR15 (3). The primary isoform of the human TLR8 is synthesized as a protein 1041 aa in length with a theoretical molecular weight of ~120 kDa (4).
TLR8 is highly similar to TLR7 and both pathways are mediated by the adapter protein MyD88 to signal through IFN regulatory factor 7 (IRF7) and nuclear factor (NF)-kappaB (1-3,5). However, TLR7 recognizes guanosine and GU-rich ssRNA, while TLR8 recognizes uridine and AU-rich sequences (2,5). TLR7/TLR8 agonists, including derivatives of the immunostimulatory imiquimod, have been shown to be a promising cancer therapy capable of providing anticancer signals to antigen presenting cells (APCs), with many agonists being tested in both pre-clinical and clinical trials (6). Similarly, studies suggest that agonists for TLR8, in combination with other individual TLR agonists and antagonists, may also be useful for treating inflammatory allergic diseases, such as allergic rhinitis (7).
References
1. Sakaniwa, K., & Shimizu, T. (2020). Targeting the innate immune receptor TLR8 using small-molecule agents. Acta crystallographica. Section D, Structural biology, 76(Pt 7). https://doi.org/10.1107/S2059798320006518
2. Cervantes, J. L., Weinerman, B., Basole, C., & Salazar, J. C. (2012). TLR8: the forgotten relative revindicated. Cellular & molecular immunology. https://doi.org/10.1038/cmi.2012.38
3. Ohto, U., Tanji, H., & Shimizu, T. (2014). Structure and function of toll-like receptor 8. Microbes and infection. https://doi.org/10.1016/j.micinf.2014.01.007
4. Uniprot (Q9NR97)
5. Jannuzzi, G. P., de Almeida, J., Paulo, L., de Almeida, S. R., & Ferreira, K. S. (2020). Intracellular PRRs Activation in Targeting the Immune Response Against Fungal Infections. Frontiers in cellular and infection microbiology. https://doi.org/10.3389/fcimb.2020.591970
6. Frega, G., Wu, Q., Le Naour, J., Vacchelli, E., Galluzzi, L., Kroemer, G., & Kepp, O. (2020). Trial Watch: experimental TLR7/TLR8 agonists for oncological indications. Oncoimmunology. https://doi.org/10.1080/2162402X.2020.1796002
7. Golshiri-Isfahani, A., Amizadeh, M., & Arababadi, M. K. (2018). The roles of toll like receptor 3, 7 and 8 in allergic rhinitis pathogenesis. Allergologia et immunopathologia. https://doi.org/10.1016/j.aller.2017.09.026
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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