Rabbit Polyclonal CR1AB antibody. Carrier free. Suitable for IP, ELISA, WB and reacts with Bacillus thuringiensis samples. Cited in 4 publications.
pH: 7.3
Constituents: PBS
| IP | ELISA | WB | |
|---|---|---|---|
| Bacillus thuringiensis | Expected | Expected | Expected |
| Species | Dilution info | Notes |
|---|---|---|
Species Bacillus thuringiensis | Dilution info Use at an assay dependent concentration. | Notes - |
| Species | Dilution info | Notes |
|---|---|---|
Species Bacillus thuringiensis | Dilution info Use at an assay dependent concentration. | Notes - |
| Species | Dilution info | Notes |
|---|---|---|
Species Bacillus thuringiensis | Dilution info Use at an assay dependent concentration. | Notes - |
130 kDa crystal protein, Crystaline entomocidal protoxin, Insecticidal delta endotoxin CryIA(b), Pesticidal crystal protein cry1Ab, bt2, cry 1 2, cry1A(b), cryIA(b), cryIC1
Rabbit Polyclonal CR1AB antibody. Carrier free. Suitable for IP, ELISA, WB and reacts with Bacillus thuringiensis samples. Cited in 4 publications.
pH: 7.3
Constituents: PBS
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The Bacillus thuringiensis CRY1Ab toxin also referred to as CRY1Ab protein is a crystal protein with a molecular mass of approximately 130 kDa. It is produced as an inactive protoxin in Bacillus thuringiensis and becomes active upon ingestion by target insect larvae. Once ingested the alkaline conditions of the insect gut activate the CRY1Ab toxin by proteolysis. This activation allows CRY1Ab to bind to specific receptors in the insect midgut epithelium leading to pore formation and cell lysis which ultimately kills the insect.
The CRY1Ab toxin acts as an insecticidal agent targeting Lepidoptera orders such as the European corn borer. It functions by disrupting the gut cells of susceptible insects which results in nutrient absorption issues and lethal effects. CRY1Ab proteins do not belong to any known protein complexes but exhibit remarkable efficacy independently allowing them to serve as a potent biological control tool in agriculture.
The CRY1Ab toxin integrates into the defense mechanisms of transgenic crops. It aligns with insect resistance pathways by expressing the CRY1Ab protein to combat pests directly. This mechanism involves multiple receptor proteins like cadherin which assist the binding process of CRY1Ab in the insect gut. This specific interaction ensures that CRY1Ab efficiently participates in safeguarding crops by reducing pest-related damage.
CRY1Ab toxin does not directly associate with human or mammalian diseases due to its specificity to insect gut conditions. However there are discussions about its environmental impact and potential allergenicity in relation to food safety. CRY1Ab might influence agricultural bioengineering efforts mainly in the context of pest control management strategies rather than human medical conditions creating ties with proteins related to pest resistance mechanisms in biotechnology.
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This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
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