Toll-like receptor 1 Antibodies

Toll-like receptor 1 (TLR1)

Participates in the innate immune response to microbial agents. Specifically recognizes diacylated and triacylated lipopeptides.

Cooperates with TLR2 to mediate the innate immune response to bacterial lipoproteins or lipopeptides (PubMed:21078852). Types the activation cluster TLR2:TLR1:CD14 in reaction to triacylated lipopeptides, this cluster activates signaling from the cell surface and then is targeted to the Golgi in a lipid-raft dependent pathway (PubMed:16880211).

Gene Information

Human
Gene Name:	TLR1
Uniprot:	Q15399
Entrez:	7096

Family

Belongs to:
Toll-like receptor family

Alternative Names

CD281 antigen; CD281; DKFZp547I0610; DKFZp564I0682; KIAA0012MGC126311; MGC104956; MGC126312; rsc786; TIL; TIL. LPRS5; TLR1; Toll/interleukin-1 receptor-like protein; toll-like receptor 1

Molecular Weight

Mass (kDA):
90.291 kDA

Genomic Context

Human
Location:	4p14
Sequence:	4; NC_000004.12 (38791055..38806262, complement)

Tissue Specificity

Ubiquitous. Highly expressed in spleen, ovary, peripheral blood leukocytes, thymus and small intestine.

Subcellular Localizations

Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle, phagosome membrane; Single-pass type I membrane protein. Membrane raft. Golgi apparatus. Does not reside in lipid rafts before stimulation but accumulates increasingly in the raft upon the presence of the microbial ligand. In response to triacylated lipoproteins, TLR2:TLR1 heterodimers are recruited in lipid rafts, this recruitment determine the intracellular targeting to the Golgi apparatus.

Diseases

• Inflammation
• Innate Immune Response
• Infective Disorder
• Inflammatory Response
• Tuberculosis
• Bacterial Infections
• Lyme Disease
• Pneumonia
• Malignant Neoplasms
• Neoplasms
• Autoimmune Reaction
• Systemic Infection
• Communicable Diseases

• Virus Diseases
• Atherosclerosis
• Salmonella Infections
• Asthma
• Lung Diseases
• Nervousness
• Tissue Adhesions

Interacting Proteins

• TLR10
• TLR2

Pathways

• Immune Response
• Secretion
• Cytokine Production
• Innate Immune Response
• Pathogenesis
• Inflammatory Response
• Cell Activation
• Cytokine Secretion
• Phagocytosis
• Cell Proliferation
• Macrophage Activation
• Response To Lipopolysaccharide
• Aging

• Localization
• Adaptive Immune Response
• Cell Differentiation
• Virulence
• Reverse Transcription
• Chemokine Secretion
• Disease Resistance

PTMs

• Phosphorylation
• Methylation
• Acylation
• Cleavage

• Glycosylation
• Ubiquitination
• Phosphorothioation
• Citrullination

Research Areas

• Cytokine Research
• Immunology
• Innate Immunity
• Signal Transduction

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/TLR1

Best Uses Of The TLR1 Marker

This article will explain the most effective ways to utilize Pam3CSK4 or biotinylated SMUZ1 order to bind with TLR1/2. These markers can be used to improve your experiments. Use the correct buffer for blocking and concentrate your antibodies if you are using them. Additionally, Boster Bio provides a sample preparation guide to help you maximize your research.

SMU-Z1

The TLR1 Marker, used in flow cytometry, has excellent affinity to particles and cells. Researchers continue to recommend the Boster Bio brand of primary antibodies. It has a strong track record. The Boster Bio antibodies are monoclonal and polyclonal, and have been utilized in scientific research since over 25 years. We will look at some of the most effective uses of this product.

The TLR1 marker is a biotinylated molecule that binds to TLR1 protein in a concentration-dependent manner. TLR1 signals are activated through biotinylated SMUZ1 binds to TMB substrate solution. SMU-Z1 binds to TLR1 protein and triggers costimulatory molecules that produce cytokines. These cytokines stimulate CD4 and CD8 T cells, which in turn promote the proliferation of TLR1-positive cells and NK-mediated lysis of tumor cells.

SMU-Z1 binds to TLR1 as well as TLR2, activating it with EC50 values of 4.88 + 0.79 10-9 m. The compound also enhances murine splenocytes' growth, while also increasing T-cells with CD8+ and NK cells, and has a significant antitumor effect in murine leukemia models.

SMU-Z1 is an oral drug that induces the proliferation of CD8+ T-cells and NK cells in mice. It also suppresses expression of TLR1/2 inhibitor, CU-CPT2220. It also reduces the production of IL-8 and IL-1a mRNA in murine leukemia cells. SMUZ1 is also a treatment to treat a variety of inflammation-related disorders, including Rheumatoid and Rheumatoid.

Biotinylated-SMU-Z1

SMU-Z1 (Sucralose-Methionine) is a synthetic peptide that binds to TLR1 in cells. In this study, SMU-Z1 was added to cell lysates for 24 hours to test the effects on TLR1 expression. SMU-Z1 treatment significantly reduced the tumor volume , and also reduced the body weight in mice and suggests that SMUZ1 could increase antitumor immunity (in in vivo).

SMU-Z1 binds to human TLR1 protein in a concentration-dependent manner. In contrast, Pam3CSK4 competes with SMUZ1 to bind to TLR1. The TLR1 marker was also detected when SMUZ1 was added to HEK-Blue cells. This study can be used in biomedical research as SMU-Z1 has a different affinity to TLR2 or TLR1.

Saturated ELISA: ELISAs that are saturated can detect the TLR1 marker in samples smaller than 30mg. Saturated antibodies must be used to obtain a high-affinity binding. ELISA kits that have a low binding affinity are not recommended. Use a polymer-based secondary antibodies in the event that you have an antibody of high quality. This can save you 30 minutes of IHC

SMU-Z1 - This TLR agonist has an NF-kB activation capacity that is high. It also induces IL-1b mRNA expression in human PBMC cell lines. SMUZ1 is a potent antagonist of TLR1/2 and has an EC50 value of 4.88 x10-9 millimeters.

Pam3CSK4

Research into the function of the TLR1 receptor has revealed a peptide called Pam3CSK4 as a ligand for TLR1 and TLR2 markers. The peptide is a potent ligand both for TLR1 as well as TLR2 and has antimicrobial activity. This protein has been demonstrated to enhance the antitumor effect of CTLA-4 antibodies . It's also applicable to other checkpoint antibodies of different types.

This drug binds TLR1 and TLR2, and recognizes microbial motifs activating mucosal defenses. In this study, TLR2 was expressed at an increased level in human airway epithelia following Pam3CSK4 injection and IL-8 production was three times higher than. The pattern was similar in TLR2-treated cells, but it was not statistically significance. These results indicate that TLR2 is expressed more heavily on the airway epithelia's apical surface.

The ligand triggers TLR1/2 through creating distinct patterns of protein expression in monocytes. Pam3CSK4 also induces high levels IL-10, one of the proteins that depends on the noncanonical NFkB pathway. Il-10 is a crucial antiinflammatory cytokine. The differential modulation of IL-10 may have significant implications for the immune function in mucosal areas.

These peptides were purchased from EMC Microcollection, and Peptides International both in Tubingen, Germany. For the PCR reaction it was used to create RNA as a template for first-strand cDNA synthesizing. The quantitative PCR results were obtained using TLR, HBD-2 PCR products, as well as GAPDH transcripts. Primer Express software was used to design TaqMan probes and primers.

SMU-Z1 binds to the TLR1/2 receptor

SMU-Z1 binds to human TLR2 and triggers its signaling through binding to TLR1. It is extremely specific for TLR2 and competes with its homolog Pam3CSK4 for binding to this receptor. Both proteins are crucial to the immune system, and they regulate signaling pathways in different cell types. Interestingly, SMU-Z1 was found to be a potent antitumor agent in a murine model of leukemia.

Furthermore, SMUZ1 is able to activate immune response without triggering T-cell activation in the entire population. These properties of SMU-Z1 make it a viable LRA candidate. The discovery of novel TLR1/2 Ligands should accelerate the development of its pharmacological properties. The present study has identified two major pathways that regulate TLR1/2 expression. The ligand SMUZ1 activates TLR1/6 within human lymphocytes.

SMUZ1 also helps in the recognition of HIV-1-infected cells and their elimination. This is essential for HIV-1 vaccines and neutralizing antibody treatments. The findings support SMU-Z1 as a potential candidate for a drug that inhibits HIV-1 infection. The findings suggest that SMU-Z1 could also have clinical potential for use as a potential therapeutic vaccine for HIV infection.

Additionally, SMUZ1 is a potent agonist of NF-kB. It stimulates the production IL-1b, and TNF-a in Raw 264.7 macrophage cell lines as well as human PBMC in a dose-dependent manner. The SMU-Z1 inhibits TLR2 expression in macrophages, and this reduction mirrors the decrease in phagocytosis-positive macrophages.

In a prior study, SMU-Z1 activated NK cells, which inhibit the replication of HIV-1. SMU-Z1 also activates innate immune cells like NK cells, and assists in the inhibition of HIV-1 by NK cells. SMU-Z1 also activates NK cells and could be a factor in the purging of HIV-1 reservoirs.

HEK-Blue cells that are overexpressing hTLR2

TLRs play an important function in innate immunity, in recognizing and responding to a variety of molecules of microbial origin. The chemokine, CU–T12-9, can trigger SEAP signaling in HEK–Blue cells that overexpress hTLR2, however it has little impact on HEK-Blue cells that express TLR1. TLR2 plays a key role in heterodimerization. This is an event that occurs in conjunction with TLR1.

TLR2 activates the inflammasome which results in the production of IL-1b. It is interesting to note that various PRRs can trigger different immune responses, which results in different levels of cytokine activity in cell models. Contrarily, TLR2 and CD14 blockade did not have any significant impact on the production of viral RNA in these cell models. Thus, it is possible that the inflammasome may not be the primary cause of viral infection.

We measured the number of DENV-Ag positive monoocytes in PBMCs using flow cytometry. We then added an inhibitor of TLR2 to PBMCs and DENV2 preparations to three donors. The bars represent the mean plus SEM.

To determine whether CU-CPT9a inhibits HEK-Blue cells that express hTLR2. HEK-Blue-hTLR2 cells were co-transfected with human TLR2 and the SEAP reporter gene. The SEAP reporter gene was placed under the control of an IFN-b minimal promoter , and was fused to five NFKB and AP-1 binding sites. Additionally the CD14 co-receptor gene was transfected into cells to increase the TLR2 response. The cells were later plated with HEK-Blue Detection medium, which allows for the monitoring of SEAP levels.

HEK-Blue cells that express hTLR2 more frequently than other types of monocytes are more likely to possess an antiviral effect. This suggests that the antiviral effects of TLR2 could be influenced by the various monocyte subsets. TLR2 expression is similar in healthy donors as well as acute DENV patients' PBMCs.