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Pectate Lyase (Aspergillus sp.)

Pectate Lyase Aspergillus sp E-PCLYAN
Product code: E-PCLYAN

7,000 Units in 50% aqueous glycerol

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Content: 7,000 Units in 50% aqueous glycerol
Shipping Temperature: Ambient
Storage Temperature: Below -10oC
Formulation: In 50% (v/v) glycerol
Physical Form: Solution
Stability: > 4 years at 4oC or below -10oC
Enzyme Activity: Pectate Lyase
EC Number:
CAZy Family: PL1
CAS Number: 9015-75-2
Synonyms: pectate lyase; (1→4)-alpha-D-galacturonan lyase
Source: Aspergillus sp.
Molecular Weight: 45,000
Concentration: Supplied at ~ 1,400 U/mL
Expression: Purified from Aspergillus sp.
Specificity: Eliminative cleavage of (1,4)-α-D-galacturonan to give oligosaccharides with 4-deoxy-α-D-galact-4-enuronosyl groups at their non-reducing ends.
Specific Activity: ~ 180 U/mg (40oC, pH 8.0 on polygalacturonic acid)
Unit Definition: One Unit of pectate lyase activity is defined as the amount of enzyme required to release one µmole of galacturonic acid from polygalacturonic acid (2.5 mg/mL) per min in Tris.HCl buffer (50 mM), pH 8.0 at 40oC.
Temperature Optima: 55oC
pH Optima: 8
Application examples: Suitable for pectin identification according to USP method [Pectin 9000-69-5]; Pectin Identification Procedure. Applications in carbohydrate and biofuels research.

High purity Pectate lyase (Aspergillus sp.) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.

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Safety Data Sheet
Isolation and manipulation of protoplasts from the unicellular green alga Penium margaritaceum.

Raimundo, S. C., Sørensen, I., Tinaz, B., Ritter, E., Rose, J. K. & Domozych, D. S. (2018). Plant Methods, 14(1), 18.

Background: The unicellular charophycean green alga Penium margaritaceum has emerged as an appealing experimental organism in plant cell wall and cell biology research. Innovative practical approaches in the manipulation and maintenance of this unicellular model alga are needed in order to probe the complexities of its subcellular and molecular machinery. Protoplast isolation and manipulation expedites a new range of experimental possibilities for Penium-based studies. These include enhanced means of isolation of subcellular components and macromolecules, application of intracellular probes for high resolution microscopy of live cells, transformation studies and analysis of the fundamental mechanisms of plant cell expansion and wall polymer deposition. Results: We present a methodology for enzyme-based digestion of the Penium cell wall and the isolation of protoplasts. The subcellular events associated with this technology are presented using multiple microscopy-based techniques. We also provide protocols for applying an array of intracellular dyes that can be used as markers for specific organelles and membrane microdomains in live cells. Finally, we present a protocol for the purification of a nuclei-rich fraction from protoplasts, which can be used for the isolation of nuclear DNA. Conclusion: Protoplast isolation, culturing and manipulation provide valuable means for molecular and cellular studies of Penium. The protocol described here offers a rapid and effective mechanism for fast and effective production of protoplasts. Subsequently, the protoplasts may be used for microscopy-based studies of specific subcellular components and the isolation of organelles and nuclear DNA. These methods offer a new practical methodology for future studies of this model organism in cell and molecular biology.

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Heterogeneous distribution of pectin and hemicellulose epitopes in the phloem of four hardwood species.

Kim, J. S. & Daniel, G. (2017). Trees, 1-22.

Using immunolocalization methods combined with monoclonal antibodies, the distribution of pectin and hemicellulose epitopes was examined in the secondary phloem of two diffuse porous (birch, aspen)- and two ring porous (oak, ash) hardwoods with a focus on sieve tube elements (SEs), companion cells (CCs), axial/ray parenchyma cells, and sclerenchyma cells (sclereids and phloem fibers). In all tree species, rhamnogalacturonan-I (RG-I), homogalacturonan (HG), and xyloglucan epitopes were common in cell walls of SEs, CCs, and axial/ray parenchyma cells. However, the amount of these epitopes varied greatly between cell types and between hardwood species. Apart from aspen, heteroxylan or/and heteromannan epitopes were detected in SEs, but were not detected in CCs and parenchyma cells. With sclerenchyma cells, RG-I, HG, and xyloglucan epitopes were common in compound middle lamellae (CML) of sclereids and phloem fibers. Except for oak, heteromannan epitopes were also detected in CML of sclereids. Distributional patterns of epitopes in CML of birch and ash sclereids varied greatly depending on anatomical structure of CML. Secondary cell walls of sclereids and phloem fibers revealed abundant heteroxylan epitopes, but showed no heteromannan epitopes. Some phloem fibers also showed sparse xyloglucan epitopes in secondary cell walls. Together, results suggest that there are great variations in distributional patterns of pectin and hemicellulose epitopes in hardwood phloem between cell types and between tree species.

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Differences in structure, allergenic protein content and pectate lyase enzyme activity of some Cupressaceae pollen.

Şahin, A. A., Aslım, B., Tan, S., Alan, Ş. & Pınar, N. M. (2017). Turkish Journal of Biochemistry, In Press.

Objective: Cupressaceae pollen has commonly been reported to be an important aeroallergen and causal factor of spring, autumn and winter pollinosis in many countries. The aim of this study was to compare of the structure and allergenic protein content of Cupressus arizonica Greene. Cupressus sempervirens L. and Juniperus oxycedrus L. pollen in detail and contribute to Cupressaceae pollen allergen diagnosis and therapy studies in Turkey. Methods: The pollen structure were examined by LM and SEM. Pollen protein content was investigated by Bradford protein assay, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), Western blot analysis and two-dimensional polyacrylamide gel electrophoresis (2DE PAGE), respectively. Pectate lyase (PL) enzyme activities were compared. Immunoblotting was carried out by using extracts of the three taxa pollen collected from Turkey. Results: All three taxa was found very similar in terms of pollen morphology however, intine thickness was prominently different. Cupressus arizonica pollen extracts showed the lowest PL activity. Five sera specific IgE of all allergic subjects showed reaction with only C. arizonica pollen extracts. Conclusions: As a conclusion, the pollen structure, protein function or protein structure and isoforms of allergens could affects allergenic properties of the pollen. This study also may help to improve the Cupressaceae pollen allergen diagnosis and therapy.

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Safety Information
Symbol : Not Applicable
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Hazard Statements : Not Applicable
Precautionary Statements : Not Applicable
Safety Data Sheet
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