外形
产品由磷酸盐缓冲盐、牛血清白蛋白和琼胶酶配制而成。 总蛋白质含量范围在10 – 30% w/w之间。
其他说明
一个单位将在40°C 、 pH 6.0 下每分钟从琼脂产生 1.0μg 还原糖(以 D -半乳糖测量)。
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
常规特殊物品
此项目有
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Applied and environmental microbiology, 78(9), 3051-3058 (2012-02-22)
Autotransporters have been employed as the anchoring scaffold for cell surface display by replacing their passenger domains with heterologous proteins to be displayed. We adopted an autotransporter (YfaL) of Escherichia coli for the cell surface display system. The critical regions
Young Hoon Oh et al.
Journal of microbiology and biotechnology, 21(8), 818-821 (2011-08-31)
An agar-degrading bacterium was isolated from the guts of spiny turban shells. It was identified as a Pseudoalteromonas species and named Pseudoalteromonas sp. JYBCL 1. The viscosity of the inoculated agar medium decreased by more than 60% after 20 h
Construction of an expression system for the secretory production of recombinant α-agarase in yeast.
Ji-Hwan Seok et al.
Biotechnology letters, 34(6), 1041-1049 (2012-02-09)
α-Agarase hydrolyzes the α-1,3 linkage of agarose yielding agaro-oligosaccharides. It is less well characterized than β-agarase. AgaA gene (2.3 kb ORF), encoding the α-agarase from Thalassomonas JAMB A33, was subcloned into both a constitutive and an inducible expression vector. Both
Michael-Paul Vockenhuber et al.
Microbiology (Reading, England), 158(Pt 2), 424-435 (2011-11-15)
Transcriptional regulation of primary and secondary metabolism is well-studied in Streptomyces coelicolor, a model organism for antibiotic production and cell differentiation. In contrast, little is known about post-transcriptional regulation and the potential functions of small non-coding RNAs (sRNAs) in this
Uyangaa Temuujin et al.
Applied microbiology and biotechnology, 92(4), 749-759 (2011-06-10)
The DagA product of Streptomyces coelicolor is an agarase with a primary translation product (35 kDa) of 309 amino acids, including a 30-amino acid signal peptide. Although dagA expression in Streptomyces lividans under the control of its own set of
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