推荐产品
品質等級
化驗
≥90% (HPLC)
形狀
powder
顏色
white
溶解度
water: 50 mg/mL, clear, colorless
儲存溫度
−20°C
SMILES 字串
OC(C=O)C(O)C(OC1OC(C(OC2OC(C(O)C(O)C2O)C(O)=O)C(O)C1O)C(O)=O)C(O)C(O)=O
InChI
1S/C18H26O19/c19-1-2(20)3(21)10(9(27)14(28)29)34-18-8(26)6(24)11(13(37-18)16(32)33)35-17-7(25)4(22)5(23)12(36-17)15(30)31/h1-13,17-18,20-27H,(H,28,29)(H,30,31)(H,32,33)
InChI 密鑰
FMNDXLWVYMQMHF-UHFFFAOYSA-N
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相关类别
儲存類別代碼
11 - Combustible Solids
水污染物質分類（WGK）
WGK 3
閃點（°F）
Not applicable
閃點（°C）
Not applicable
個人防護裝備
Eyeshields, Gloves, type N95 (US)
其他客户在看
S Berensmeier et al.
Applied microbiology and biotechnology, 64(4), 560-567 (2003-12-16)
The pectate lyase gene pelA from alkaliphilic Bacillus licheniformis strain 14A was cloned and sequenced. The nucleotide sequence corresponded to an open reading frame of 1,026 bp that codes for a 39 amino acid signal peptide and a mature protein
Eduardo da Silva Martins et al.
Enzyme research, 2013, 438645-438645 (2013-10-26)
Polygalacturonases are enzymes involved in the degradation of pectic substances, being extensively used in food industries, textile processing, degumming of plant rough fibres, and treatment of pectic wastewaters. Polygalacturonase (PG) production by thermophilic fungus Thermoascus aurantiacus on solid-state fermentation was
D Wade Abbott et al.
The Journal of biological chemistry, 282(48), 35328-35336 (2007-09-21)
The family 2 pectate lyase from Yersinia enterocolitica (YePL2A), solved to 1.5A, reveals it to be the first prokaryotic protein reported to display the rare (alpha/alpha)(7) barrel fold. In addition to its apo form, we have also determined the structure
Jullien Drone et al.
Protein engineering, design & selection : PEDS, 20(1), 7-14 (2007-01-16)
The aim of this study was to develop an Escherichia coli-based metabolic selection system for the uncovering of new oligogalacturonate-active enzymes. Based on the expression of the specific permease TogMNAB, this system enabled the entry of oligogalacturonates into the cytoplasm
Judicaël Parisot et al.
Carbohydrate research, 337(16), 1427-1433 (2002-09-03)
A new exopolygalacturonate lyase (Pel) gene of the hyperthermophilic bacterium Thermotoga maritima was cloned and overexpressed in Escherichia coli cells. A 42 kDa monomeric Pel was shown to undergo N-terminal processing by cleavage at a putative site between alanine and
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