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This product has been discontinued
|Stability:||> 8 years under recommended storage conditions|
|Substrate For (Enzyme):||endo-Cellulase, Xyloglucanase|
|Assay Format:||Spectrophotometer, Petri-dish (Qualitative)|
|Reproducibility (%):||~ 7%|
This product has been discontinued (read more).
High purity dyed, soluble Azo-Xyloglucan (Tamarind) for the measurement of enzyme activity, for research, biochemical enzyme assays and in vitro diagnostic analysis.
A soluble chromogenic substrate for the assay of endo-cellulase.
Please note the video above shows the protocol for assay of endo-cellulase using Azo-CM cellulose. The procedure for the assays of endo-Cellulase and xyloglucanase using Azo-Xyloglucan (Tamarind) is equivalent to this.
More soluble chromogenic substrates available.
hoi, H. W., Kim, N. H., Lee, Y. K. & Hwang, B. K. (2013). Plant Physiology, 161(1), 384-396.
Plants produce various proteinaceous inhibitors to protect themselves against microbial pathogen attack. A xyloglucan-specific endo-β-1,4-glucanase inhibitor1 gene, CaXEGIP1, was isolated and functionally characterized in pepper (Capsicum annuum) plants. CaXEGIP1 was rapidly and strongly induced in pepper leaves infected with avirulent Xanthomonas campestris pv vesicatoria, and purified CaXEGIP1 protein significantly inhibited the hydrolytic activity of the glycoside hydrolase74 family xyloglucan-specific endo-β-1,4-glucanase from Clostridium thermocellum. Soluble-modified green fluorescent protein-tagged CaXEGIP1 proteins were mainly localized to the apoplast of onion (Allium cepa) epidermal cells. Agrobacterium tumefaciens-mediated overexpression of CaXEGIP1 triggered pathogen-independent, spontaneous cell death in pepper and Nicotiana benthamiana leaves. CaXEGIP1 silencing in pepper conferred enhanced susceptibility to virulent and avirulent X. campestris pv vesicatoria, accompanied by a compromised hypersensitive response and lowered expression of defense-related genes. Overexpression of dexamethasone: CaXEGIP1 in Arabidopsis (Arabidopsis thaliana) enhanced resistance to Hyaloperonospora arabidopsidis infection. Comparative histochemical and proteomic analyses revealed that CaXEGIP1 overexpression induced a spontaneous cell death response and also increased the expression of some defense-related proteins in transgenic Arabidopsis leaves. This response was also accompanied by cell wall thickening and darkening. Together, these results suggest that pathogen-inducible CaXEGIP1 positively regulates cell death-mediated defense responses in plants.Hide Abstract