Native rabbit ACT
Cat.No. : | ACT-161R |
- Specification
- Gene Information
- Related Products
Description : | Protein standard for immunoblotting, immunization and immunoassays. |
Source : | rabbit muscle |
Species : | Rabbit |
Form : | lyophilized, purified |
Molecular Mass : | 43 Kd |
Purity : | >98% |
Storage : | At 2-8 centigrade (lyoph.); at -20 centigrade (reconstituted) |
Reconstitution : | Reconstitute with 250 ul distilled water (final volume 250 ul) |
For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (20)
Ask a questionThe bio-functional toxin molecule of ACT consists of an N-terminal ~400-residue-long adenylate cyclase (AC) enzyme domain and a C-terminal ~1300-residue-long hemolytic activity.
The findings suggest that ACT may regulate the innate immune response through a signal pathway mediated by Toll-Like Receptor (TLR), particularly TLR4.
ACT stands for adenylate cyclase toxin, which is a virulence factor produced by the pathogen Bordetella pertussis, the causative agent of whooping cough
The RTX family of bacterial cytolysins is characterized by the presence of calcium-binding repeats and the ability to cause lysis of host cells
The availability of the recombinant ACT protein and the established functional assays provide a foundation for future studies on ACT. These tools can be used to investigate the protein's interactions, its impact on immune pathways, and its potential as a therapeutic target for whooping cough or other related conditions.
The ACT protein consists of an N-terminal adenylate cyclase (AC) enzyme domain and a C-terminal hemolytic activity domain.
ACT can inhibit the secretion of IL-12 and TNFα induced by LPS in mice peritoneal macrophages, while enhancing the secretion of IL-10.
ACT plays important roles in bacteria colonization and pathogenesis by producing pertussis toxin and adenylate cyclase toxin during the invasion of the host.
According to the provided information, the relevant testing method for ACT content is currently unavailable in China.
While previous studies have shown that ACT is involved in immune regulation during the invasion of the host, the exact mechanism is still unclear.
Previous studies on ACT and its interacting protein TIRAP may provide insights into the specific mechanism by which ACT influences the immune response.
The glycine- and aspartate-rich nonapeptide repeats found in ACT are characteristic of the RTX family of bacterial cytolysins. These repeats may play a role in the folding, stability, or function of the protein.
The provided information does not mention specific details about the three-dimensional structure of the ACT protein.
The N-terminal AC domain of the ACT protein exhibits adenylate cyclase activity, converting ATP into cyclic AMP (cAMP).
The hemolytic domain of the ACT protein plays a role in the pathogenicity of ACT by causing the destruction of red blood cells. This hemolytic activity can lead to tissue damage and facilitate bacterial colonization and pathogenesis.
ACT belongs to the RTX (repeat in toxin) family of bacterial cytolysins.
The ACT protein consists of an N-terminal adenylate cyclase (AC) enzyme domain and a C-terminal hemolytic activity domain. It also possesses glycine- and aspartate-rich nonapeptide repeats, which are characteristic of the RTX family of bacterial cytolysins.
The C-terminal domain of the ACT protein is responsible for its hemolytic activity, which causes the destruction of red blood cells.
Monitoring the ACT content in pertussis vaccine manufacturing ensures quality control and effectiveness of the vaccine. The European Pharmacopoeia (EP) provides guidelines for this monitoring process.
ACT belongs to the RTX (repeat in toxin) family of bacterial cytolysins. It possesses a series of glycine- and aspartate-rich nonapeptide repeats.
Customer Reviews (5)
Write a reviewThe ACT protein effectively facilitated the desired biological response in my study, validating its efficacy and performance.
The protein product had a pleasant odor-free experience during handling, ensuring a comfortable and hassle-free experiment
I obtained robust and statistically significant results using the protein product, indicating its reliability and functionality
The protein product exhibited exceptional stability, remaining active and retaining its functionality throughout my experiments
It yielded reproducible and reliable results, confirming high quality.
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