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    CAS No. 54-12-6 Price
    Catalog No.CFN90473Purity>=98%
    Molecular Weight204.22Type of CompoundAlkaloids
    FormulaC11H12N2O2Physical DescriptionCryst.
    Download     COA    MSDSSimilar structuralComparison (Web)
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    Featured Products

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    Biological Activity
    Description: 1. Tryptophan residues at the bn+1 position does not universally disrupt cbEGF domain folding and secretion.
    2. Low thalamic Tryptophan uptake appears to be a strong, independent predictor of long survival in patients with previous glioma treatment.
    3. Tryptophan containing dipeptides are interesting ingredients for functional foods as a natural prevention for hypertension with reduced side effects due to its selective inhibition of the C-domain.
    Tryptophan Description
    Source: The seeds of Glycine max
    Solvent: Chloroform, Dichloromethane, Ethyl Acetate, DMSO, Acetone, etc.
    Storage: Providing storage is as stated on the product vial and the vial is kept tightly sealed, the product can be stored for up to 24 months(2-8C).

    Wherever possible, you should prepare and use solutions on the same day. However, if you need to make up stock solutions in advance, we recommend that you store the solution as aliquots in tightly sealed vials at -20C. Generally, these will be useable for up to two weeks. Before use, and prior to opening the vial we recommend that you allow your product to equilibrate to room temperature for at least 1 hour.

    Need more advice on solubility, usage and handling? Please email to: service@chemfaces.com

    After receiving: The packaging of the product may have turned upside down during transportation, resulting in the natural compounds adhering to the neck or cap of the vial. take the vial out of its packaging and gently shake to let the compounds fall to the bottom of the vial. for liquid products, centrifuge at 200-500 RPM to gather the liquid at the bottom of the vial. try to avoid loss or contamination during handling.
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    Recently, ChemFaces products have been cited in many studies from excellent and top scientific journals

    Cell. 2018 Jan 11;172(1-2):249-261.e12.
    doi: 10.1016/j.cell.2017.12.019.

    PMID: 29328914

    Mol Cell. 2017 Nov 16;68(4):673-685.e6.
    doi: 10.1016/j.molcel.2017.10.022.

    PMID: 29149595

    Scientific Reports 2017 Dec 11;7(1):17332.
    doi: 10.1038/s41598-017-17427-6.

    PMID: 29230013

    Molecules. 2017 Oct 27;22(11). pii: E1829.
    doi: 10.3390/molecules22111829.

    PMID: 29077044

    J Cell Biochem. 2018 Feb;119(2):2231-2239.
    doi: 10.1002/jcb.26385.

    PMID: 28857247

    Phytomedicine. 2018 Feb 1;40:37-47.
    doi: 10.1016/j.phymed.2017.12.030.

    PMID: 29496173
    Calculate Dilution Ratios(Only for Reference)
    1 mg 5 mg 10 mg 20 mg 25 mg
    1 mM 4.8967 mL 24.4834 mL 48.9668 mL 97.9336 mL 122.417 mL
    5 mM 0.9793 mL 4.8967 mL 9.7934 mL 19.5867 mL 24.4834 mL
    10 mM 0.4897 mL 2.4483 mL 4.8967 mL 9.7934 mL 12.2417 mL
    50 mM 0.0979 mL 0.4897 mL 0.9793 mL 1.9587 mL 2.4483 mL
    100 mM 0.049 mL 0.2448 mL 0.4897 mL 0.9793 mL 1.2242 mL
    * Note: If you are in the process of experiment, it's need to make the dilution ratios of the samples. The dilution data of the sheet for your reference. Normally, it's can get a better solubility within lower of Concentrations.
    Tryptophan References Information
    Citation [1]

    Exp Eye Res. 2015 Jan;130:66-72.

    Differential tolerance of 'pseudo-pathogenic' tryptophan residues in calcium-binding EGF domains of short fibulin proteins.[Pubmed: 25481286]
    Herein we tested whether the introduction of analogous, 'pseudo-pathogenic' Tryptophan mutations immediately after the bn cysteine (bn+1) in other cbEGF domains also caused protein folding/secretion challenges. We found that introduction of Tryptophan mutations into each of the four other F3 canonical cbEGF domains caused a significant reduction in protein secretion ranging from 2.7 to 56% of wild-type (WT) F3 levels. Surprisingly, an R185W mutation in the first canonical cbEGF domain of F3 yielded the highest amount of secretion among the F3 Tryptophan mutants, and its secretion defect could be rescued to near WT levels (95%) after growth temperature reduction. Interestingly, when similarly positioned Tryptophan mutations were introduced into any of the canonical cbEGF domains of the highly homologous protein, fibulin-5 (F5), there was no effect on secretion. In an attempt to make F3 tolerant of Tryptophan residues (like F5), we genetically engineered F3 to have a higher sequence homology with F5 by deleting three insert regions present in F3, but not F5. However, deletion of one or more of these regions did not have a beneficial effect on R345W F3 secretion. Overall, these results demonstrate that the introduction of Tryptophan residues at the bn+1 position does not universally disrupt cbEGF domain folding and secretion.
    Citation [2]

    Food Chem. 2015 Jan 1;166:596-602.

    Tryptophan-containing dipeptides are C-domain selective inhibitors of angiotensin converting enzyme.[Pubmed: 25053098]
    We report for the first time that Tryptophan-containing dipeptides such as Ile-Trp or Val-Trp, which were recently found in food protein hydrolysates, are selective and competitive inhibitors for the C-domain with a selectivity factor of 40 and 70, respectively. Structure-activity studies showed that an N-terminal aliphatic amino acid and a Tryptophan moiety in the P2' position are favourable structures for C-domain inhibition in dipeptides. In contrast, the lactotripeptides Ile-Pro-Pro and Val-Pro-Pro, which were widely used as ingredients for hypotensive food, showed a slight selectivity for the N-domain. Hence, Tryptophan containing dipeptides are interesting ingredients for functional foods as a natural prevention for hypertension with reduced side effects due to its selective inhibition of the C-domain.
    Citation [3]

    J Nucl Med. 2014 Oct;55(10):1605-10.

    Clinical significance of tryptophan metabolism in the nontumoral hemisphere in patients with malignant glioma.[Pubmed: 25189339]
    α-(11)C-methyl-L-Tryptophan (AMT) PET allows evaluation of brain serotonin synthesis and can also track upregulation of the immunosuppressive kynurenine pathway in tumor tissue. Increased AMT uptake is a hallmark of World Health Organization grade III-IV gliomas. Our recent study also suggested decreased frontal cortical AMT uptake in glioma patients contralateral to the tumor. The clinical significance of extratumoral Tryptophan metabolism has not been established. In the present study, we investigated clinical correlates of Tryptophan metabolic abnormalities in the nontumoral hemisphere of glioma patients. CONCLUSION: These observations provide evidence for altered Tryptophan uptake in contralateral cortical and thalamic brain regions in glioma patients after initial therapy, suggesting treatment effects on the serotonergic system. Low thalamic Tryptophan uptake appears to be a strong, independent predictor of long survival in patients with previous glioma treatment.