AAL Toxin TD1

CAS# 176590-35-5

AAL Toxin TD1

Catalog No. BCN1735----Order now to get a substantial discount!

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AAL Toxin TD1: 5mg Please Inquire In Stock
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Quality Control of AAL Toxin TD1

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Chemical structure

AAL Toxin TD1

3D structure

Chemical Properties of AAL Toxin TD1

Cas No. 176590-35-5 SDF Download SDF
PubChem ID 102004455 Appearance Powder
Formula C27H49NO10 M.Wt 547.68
Type of Compound Alkaloids Storage Desiccate at -20°C
Solubility Soluble in Chloroform,Dichloromethane,Ethyl Acetate,DMSO,Acetone,etc.
Chemical Name 2-[2-[(3R,4R,5S,7S,14R,16S)-17-acetamido-4,14,16-trihydroxy-3,7-dimethylheptadecan-5-yl]oxy-2-oxoethyl]butanedioic acid
SMILES CCC(C)C(C(CC(C)CCCCCCC(CC(CNC(=O)C)O)O)OC(=O)CC(CC(=O)O)C(=O)O)O
Standard InChIKey QEQNOUGFCMZARY-LAEADJPZSA-N
General tips For obtaining a higher solubility , please warm the tube at 37 ℃ and shake it in the ultrasonic bath for a while.Stock solution can be stored below -20℃ for several months.
We recommend that you prepare and use the solution on the same day. However, if the test schedule requires, the stock solutions can be prepared in advance, and the stock solution must be sealed and stored below -20℃. In general, the stock solution can be kept for several months.
Before use, we recommend that you leave the vial at room temperature for at least an hour before opening it.
About Packaging 1. The packaging of the product may be reversed during transportation, cause the high purity compounds to adhere to the neck or cap of the vial.Take the vail out of its packaging and shake gently until the compounds fall to the bottom of the vial.
2. For liquid products, please centrifuge at 500xg to gather the liquid to the bottom of the vial.
3. Try to avoid loss or contamination during the experiment.
Shipping Condition Packaging according to customer requirements(5mg, 10mg, 20mg and more). Ship via FedEx, DHL, UPS, EMS or other couriers with RT, or blue ice upon request.

Source of AAL Toxin TD1

The Alternaria alternata f. sp. lycopersici

Biological Activity of AAL Toxin TD1

Description1. AAL-toxin has a wide range of phytotoxicity, it has potential as a natural herbicide because several important weeds including jimsonweed, black nightshade, prickly sida and hemp sesbania are quite sensitive, while some crops such as cotton and maize are not affected.
TargetsAntifection

AAL Toxin TD1 Dilution Calculator

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AAL Toxin TD1 Molarity Calculator

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Preparing Stock Solutions of AAL Toxin TD1

1 mg 5 mg 10 mg 20 mg 25 mg
1 mM 1.8259 mL 9.1294 mL 18.2588 mL 36.5177 mL 45.6471 mL
5 mM 0.3652 mL 1.8259 mL 3.6518 mL 7.3035 mL 9.1294 mL
10 mM 0.1826 mL 0.9129 mL 1.8259 mL 3.6518 mL 4.5647 mL
50 mM 0.0365 mL 0.1826 mL 0.3652 mL 0.7304 mL 0.9129 mL
100 mM 0.0183 mL 0.0913 mL 0.1826 mL 0.3652 mL 0.4565 mL
* Note: If you are in the process of experiment, it's necessary to make the dilution ratios of the samples. The dilution data above is only for reference. Normally, it's can get a better solubility within lower of Concentrations.

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References on AAL Toxin TD1

The plant disease resistance gene Asc-1 prevents disruption of sphingolipid metabolism during AAL-toxin-induced programmed cell death.[Pubmed:12445127]

Plant J. 2002 Nov;32(4):561-72.

The nectrotrophic fungus Alternaria alternata f.sp. lycopersici infects tomato plants of the genotype asc/asc by utilizing a host-selective toxin, AAL-toxin(include AAL Toxin TD1), that kills the host cells by inducing programmed cell death. Asc-1 is homologous to genes found in most eukaryotes from yeast to humans, suggesting a conserved function. A yeast strain with deletions in the homologous genes LAG1 and LAC1 was functionally complemented by Asc-1, indicating that Asc-1 functions in an analogous manner to the yeast homologues. Examination of the yeast sphingolipids, which are almost absent in the lag1Deltalac1Delta mutant, showed that Asc-1 was able to restore the synthesis of sphingolipids. We therefore examined the biosynthesis of sphingolipids in tomato by labeling leaf discs with l-[3-3H]serine. In the absence of AAL-toxin(include AAL Toxin TD1), there was no detectable difference in sphingolipid labeling between leaf discs from Asc/Asc or asc/asc leaves. In the presence of pathologically significant concentrations of AAL-toxin(include AAL Toxin TD1) however, asc/asc leaf discs showed severely reduced labeling of sphingolipids and increased label in dihydrosphingosine (DHS) and 3-ketodihydrosphingosine (3-KDHS). Leaf discs from Asc/Asc leaves responded to AAL-toxin(include AAL Toxin TD1) treatment by incorporating label into different sphingolipid species. The effects of AAL-toxin on asc/asc leaflets could be partially blocked by the simultaneous application of AAL-toxin(include AAL Toxin TD1) and myriocin. Leaf discs simultaneously treated with AAL-toxin(include AAL Toxin TD1) and myriocin showed no incorporation of label into sphingolipids or long-chain bases as expected. These results indicate that the presence of Asc-1 is able to relieve an AAL-toxin-induced block on sphingolipid synthesis that would otherwise lead to programmed cell death.

AAL-Toxin-Deficient Mutants of Alternaria alternata Tomato Pathotype by Restriction Enzyme-Mediated Integration.[Pubmed:18945069]

Phytopathology. 1997 Sep;87(9):967-72.

Host-specific toxins are produced by three pathotypes of Alternaria alternata: AM-toxin, which affects apple; AK-toxin, which affects Japanese pear; and AAL-toxin(include AAL Toxin TD1), which affects tomato. Each toxin has a role in pathogenesis. To facilitate molecular genetic analysis of toxin production, isolation of toxin-deficient mutants utilizing ectopic integration of plasmid DNA has been attempted. However, the transformation frequency was low, and integration events in most transformants were complicated. Addition of a restriction enzyme during transformation has been reported to increase transformation frequencies significantly and results in simple plasmid integration events. We have, therefore, optimized this technique, known as restriction enzyme-mediated integration (REMI), for A. alternata pathotypes. Plasmid pAN7-1, conferring resistance to hygromycin B, with no detectable homology to the fungal genome was used as the transforming DNA. Among the three restriction enzymes examined, HindIII was most effective, as it increased transformation frequency two-to 10-fold depending on the pathotype, facilitating generation of several hundred transformants with a 1-day protocol. BamHI and XbaI had no significant effect on transformation frequencies in A. alternata pathotypes. Furthermore, the transforming plasmid tended to integrate as a single copy at single sites in the genome, compared with trials without addition of enzyme. Libraries of plasmid-tagged transformants obtained with and without addition of restriction enzyme were constructed for the tomato pathotype of A. alternata and were screened for toxin production. Three AAL-toxin-deficient mutants were isolated from a library of transformants obtained with addition of enzyme. These mutants did not cause symptoms on susceptible tomato, indicating that the toxin is required for pathogenicity of the fungus. Characterization of the plasmid integration sites and rescue of flanking sequences are in progress.

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