THBS1 Specific Neutra™ Antibody Products
Product listAccelerate Your Research and Development!
Are you currently facing difficulties in precise quantitation of THBS1, distinguishing between active and latent TGF-β signaling, or navigating complex vascular and fibrotic research models? Creative Biolabs' THBS1 Specific Neutra™ Antibody Products help you achieve unparalleled specificity in THBS1 research, characterize the critical THBS1-CD47 axis, and modulate TGF-β activation through innovative protein targeting techniques.
Contact our team to get an inquiry now!
Introduction of THBS1
Thrombospondin 1 (TSP1, encoded by THBS1) is a large, non-collagenous glycoprotein secreted by cells and incorporated into the extracellular matrix (ECM). It functions as a homotrimer, composed of subunits featuring key domains, notably the Type 1 (TS-1) repeats. These TS-1 repeats are functionally critical: they bind the latency-associated peptide (LAP) of TGF-β, which is the main mechanism by which THBS1 activates this latent pro-fibrotic cytokine. The resulting SMAD signaling drives cell proliferation, differentiation, and ECM deposition. Furthermore, TS-1 repeats bind the cell surface receptor CD47, mediating essential cell-to-cell communication for migration and immune evasion. THBS1's roles in activating TGF-β and its potent anti-angiogenic activity centrally implicate it in serious human diseases, including various forms of organ fibrosis (e.g., lung, liver, kidney), cancer progression, and cardiovascular pathology, reinforcing its high-value as a research target.
Fig.1 Thrombospondin 1 (TSP1) is produced by many nucleated cells, including antigen presenting cells and parenchymal cells.1
Antibodies Against THBS1
Antibodies targeting THBS1 are essential reagents for academic research and pharmaceutical development. Creative Biolabs' Neutra™ line prioritizes functional utility over simple detection.
Applications in Research and Drug Discovery:
- Mechanistic Studies of Fibrosis: Given THBS1's direct link to TGF-β activation, Neutra™ antibodies can isolate the THBS1 pathway's contribution to fibrotic responses like fibroblast activation and collagen deposition in vitro.
- Investigating the Tumor Microenvironment (TME): Anti-THBS1 antibodies delineate the pro-survival THBS1-CD47 signaling axis, a key area of immuno-oncology research. Functional blocking antibodies effectively interrupt this cascade, revealing therapeutic vulnerabilities in cancer models.
- Vascular and Thrombosis Research: For cardiovascular studies, these antibodies are vital for investigating THBS1's role in platelet aggregation, smooth muscle cell migration, and atherosclerotic plaque development, using techniques like flow cytometry to assess platelet binding kinetics.
- Immunoprecipitation and Protein Characterization: High-affinity Neutra™ antibodies are vital for isolating THBS1 and its interacting partners from complex cellular lysates to map novel signaling complexes via mass spectrometry or co-immunoprecipitation.
Selecting a high-quality, validated anti-THBS1 antibody is paramount for obtaining interpretable data and driving informed decisions in target validation and preclinical testing.
Why Choose Us?
Creative Biolabs provides specialized THBS1 Neutra™ Antibodies, built on two decades of experience, as trusted tools for functional analysis. Our key advantages are:
- Exceptional Functional Neutralization, blocking critical interactions like TGF-β activation and CD47 binding;
- High Specificity against other Thrombospondin family members;
- Rigorous Multi-Assay Validation and Unmatched Lot-to-Lot Consistency for reliable, reproducible results;
- Expert Technical Support.
Leveraging these antibodies grants a competitive edge in modulating and analyzing this critical signaling node in disease biology.
FAQs
Q: How can I ensure the antibody detects the biologically active form, not just the total protein?
A: To focus on functional impact, select neutralizing monoclonals or antibodies targeting a known functional epitope (e.g., TGF-β activation site). Always validate detection via a functional assay alongside standard Western Blotting to correlate binding with biological activity.
Q: What is the optimal concentration range for using this specific antibody in complex tissue staining (e.g., fibrotic organ samples)?
A: Optimal working concentrations depend on the sample type and expression level. For challenging fibrotic tissue staining, an initial IHC titration range of 0.5 to 5.0 μg/mL is usually recommended. Dilution optimization is essential to ensure a high signal-to-noise ratio.
Q: My research involves multiple Thrombospondin family members. How can I confirm there is no unintended cross-reactivity?
A: Specificity is critical. Confirm a lack of cross-reactivity with homologous family members (THBS2, THBS3, etc.) using competitive binding assays or ELISA documentation. Monoclonal antibodies, especially those developed against unique domain epitopes, offer the highest assurance against unintended binding.
Q: Are these reagents suitable for live-cell functional assays (e.g., adhesion or migration)?
A: Yes. Many high-purity, low-endotoxin monoclonal antibodies are specifically designed for functional use. Look for the 'Neutralizing' designation, confirming the antibody's ability to inhibit a specific extracellular function (e.g., blocking CD47). Ensure the product is sterile-filtered for cell culture compatibility.
Q: When developing an ELISA for target quantification in plasma, what is the major precaution for selecting a capture antibody?
A: The main precaution is minimizing interference from the complex plasma matrix. The capture antibody requires exceptional affinity and its epitope must be distant from the detection antibody (sandwich ELISA). This two-site recognition strategy, combined with high-quality coating, achieves the necessary sensitivity and robustness.
Access the Creative Biolabs Edge – Request Your Quote Now
REFERENCE
- Kale, Atharva et al. "Thrombospondin-1 CD47 Signalling: From Mechanisms to Medicine." International journal of molecular sciences vol. 22,8 4062. 14 Apr. 2021, Distributed under Open Access license CC BY 4.0, without modification. https://doi.org/10.3390/ijms22084062
