Betaine Aldehyde (chloride)
(Synonyms: 甲酰甲基三甲基氯化铵) 目录号 : GC42926
An intermediate in the oxidation of choline to betaine
Cas No.:7758-31-8
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >95.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Betaine aldehyde is the physiological intermediate in the oxidation of choline to betaine. This step is involved in glycine, serine, and threonine metabolism.
| Cas No. | 7758-31-8 | SDF | |
| 别名 | 甲酰甲基三甲基氯化铵 | ||
| Canonical SMILES | O=C([H])C[N+](C)(C)C.[Cl-] | ||
| 分子式 | C5H12NO•Cl | 分子量 | 137.6 |
| 溶解度 | DMSO: 1 mg/ml,PBS (pH 7.2): 5 mg/ml | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 7.2674 mL | 36.3372 mL | 72.6744 mL |
| 5 mM | 1.4535 mL | 7.2674 mL | 14.5349 mL |
| 10 mM | 0.7267 mL | 3.6337 mL | 7.2674 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Glycine Betaine Aldehyde dehydrogenase from Bacillus subtilis: characterization of an enzyme required for the synthesis of the osmoprotectant glycine betaine
Arch Microbiol 1997 Oct;168(4):282-9.PMID:9297465DOI:10.1007/s002030050500.
Production of the compatible solute glycine betaine from its precursors choline or glycine Betaine Aldehyde confers a considerable level of tolerance against high osmolarity stress to the soil bacterium Bacillus subtilis. The glycine Betaine Aldehyde dehydrogenase GbsA is an integral part of the osmoregulatory glycine betaine synthesis pathway. We strongly overproduced this enzyme in an Escherichia coli strain that expressed a plasmid-encoded gbsA gene under T7φ10 control. The recombinant GbsA protein was purified 23-fold to apparent homogeneity by fractionated ammonium sulfate precipitation, ion-exchange chromatography on Q-Sepharose, and subsequent hydrophobic interaction chromatography on phenyl-Sepharose. Molecular sieving through Superose 12 and sedimentation centrifugation through a glycerol gradient suggested that the native enzyme is a homodimer with 53.7-kDa subunits. The enzyme was specific for glycine Betaine Aldehyde and could use both NAD+ and NADP+ as cofactors, but NAD+ was strongly preferred. A kinetic analysis of the GbsA-mediated oxidation of glycine Betaine Aldehyde to glycine betaine revealed Km values of 125 microM and 143 microM for its substrates glycine Betaine Aldehyde and NAD+, respectively. Low concentrations of salts stimulated the GbsA activity, and the enzyme was highly tolerant of high ionic conditions. Even in the presence of 2.4 M KCl, 88% of the initial enzymatic activity was maintained. B. subtilis synthesizes high levels of proline when grown at high osmolarity, and the presence of this amino acid strongly stimulated the GbsA activity in vitro. The enzyme was stimulated by moderate concentrations of glycine betaine, and its activity was highly tolerant against molar concentrations of this osmolyte. The high salt tolerance and its resistance to its own reaction product are essential features of the GbsA enzyme and ensure that B. subtilis can produce high levels of the compatible solute glycine betaine under conditions of high osmolarity stress.
Betaine Aldehyde dehydrogenase from spinach leaves: purification, in vitro translation of the mRNA, and regulation by salinity
Arch Biochem Biophys 1989 May 15;271(1):56-63.PMID:2712575DOI:10.1016/0003-9861(89)90255-5.
Spinach (Spinacia oleracea L.) leaves contain a nuclear-encoded chloroplastic Betaine Aldehyde dehydrogenase (EC 1.2.1.8) which is induced several-fold by salinization. Betaine Aldehyde dehydrogenase was purified 2400-fold to homogeneity with an overall yield of 14%. The procedure included fractional precipitation with ammonium sulfate, followed by ion-exchange, hydrophobic interaction, and hydroxyapatite chromatography in open columns, and ion-exchange and hydrophobic interaction chromatography in a fast-protein liquid chromatography system. The Betaine Aldehyde dehydrogenase had a pI of 5.65, and a broad pH optimum between 7.5 and 9.5. The Km values for NAD+ and NADP+ were 20 and 320 microM, respectively; the Vmax of the reaction with NADP+ was 75% of that with NAD+. The native enzyme is a dimer with subunits of Mr 63,000. Highly specific antiserum was raised against the native enzyme, and was used in conjunction with cell-free translation of leaf poly(A)+ RNA to show (a) that Betaine Aldehyde dehydrogenase is synthesized as a precursor of Mr 1200 higher than the mature polypeptide, and (b) that both chronic salt stress and salt shock provoke a several-fold increase in the level of translatable message for the enzyme.
Betaine Aldehyde dehydrogenase from Pseudomonas aeruginosa: cloning, over-expression in Escherichia coli, and regulation by choline and salt
Arch Microbiol 2006 Mar;185(1):14-22.PMID:16315011DOI:10.1007/s00203-005-0054-8.
In the human pathogen Pseudomonas aeruginosa, Betaine Aldehyde dehydrogenase (BADH) may play a dual role assimilating carbon and nitrogen from choline or choline precursors--abundant at infection sites--and producing glycine betaine, which protects the bacteria against the high-osmolarity stress prevalent in the infected tissues. We cloned the P. aeruginosa BADH gene and expressed the BADH protein in Escherichia coli. The recombinant protein appears identical to its native counterpart, as judged by Western blot, N-terminal amino acid sequence, tryptophan-fluorescence emission spectra, circular-dichroism spectroscopy, size-exclusion chromatography, and kinetic properties. Computational analysis indicated that the promoter sequence of the putative operon that includes the BADH gene has a consensus-binding site for the choline-sensing transcription repressor BetI, and putative boxes for ArcA and Lrp transcription factors but no known elements of response to osmotic stress. This is consistent with the strong induction of BADH expression by choline and with the lack of effect of NaCl. As there were significant amounts of BADH protein and activity in P. aeruginosa cells grown on glucose plus choline, as well as the BADH activity exhibiting tolerance to salt, it is likely that glycine betaine is synthesized in vivo and could play an important osmoprotectant role under conditions of infection.
Heterologous expression of Betaine Aldehyde dehydrogenase gene from Ammopiptanthus nanus confers high salt and heat tolerance to Escherichia coli
Gene 2014 Oct 1;549(1):77-84.PMID:25046139DOI:10.1016/j.gene.2014.07.049.
Betaine Aldehyde dehydrogenase (BADH) catalyzes the synthesis of glycine betaine, a regulator of osmosis, and therefore BADH is considered to play a significant role in response of plants to abiotic stresses. Here, based on the conserved residues of the deduced amino acid sequences of the homologous BADH genes, we cloned the AnBADH gene from the xerophytic leguminous plant Ammopiptanthus nanus by using reverse transcription PCR and rapid amplification of cDNA ends. The full-length cDNA is 1,868 bp long without intron, and contains an open reading frame of 1512 bp, and 3'- and 5'-untranslated regions of 294 and 62 bp. It encodes a 54.71 kDa protein of 503 amino acids. The deduced amino acid sequence shares high homology, conserved amino acid residues and sequence motifs crucial for the function with the BADHs in other leguminous species. The sequence of the open reading frame was used to construct a prokaryotic expression vector pET32a-AnBADH, and transform Escherichia coli. The transformants expressed the heterologous AnBADH gene under the induction of isopropyl β-D-thiogalactopyranoside, and demonstrated significant enhancement of salt and heat tolerance under the stress conditions of 700 mmol L(-1) NaCl and 55°C high temperature. This result suggests that the AnBADH gene might play a crucial role in adaption of A. nanus to the abiotic stresses, and have the potential to be applied to transgenic operations of commercially important crops for improvement of abiotic tolerance.
Enhanced stress tolerance in Escherichia coli and Nicotiana tabacum expressing a Betaine Aldehyde dehydrogenase/choline dehydrogenase fusion protein
Biotechnol Prog 2002 Nov-Dec;18(6):1176-82.PMID:12467448DOI:10.1021/bp020057k.
In Escherichia coli the osmoprotective compound glycine betaine is produced from choline by two enzymes; choline dehydrogenase (CDH) oxidizes choline to Betaine Aldehyde and then further on to glycine betaine, while Betaine Aldehyde dehydrogenase (BADH) facilitates the conversion of Betaine Aldehyde to glycine betaine. To evaluate the importance of BADH, a BADH/CDH fusion enzyme was constructed and expressed in E. coli and in Nicotiana tabacum. The fusion enzyme displayed both enzyme activities, and a coupled reaction could be measured. The enzyme was characterized regarding molecular weight and the dependence of the enzyme activities on environmental factors (salt, pH, and poly(ethylene glycol) addition). At high choline concentrations, E. coli cells expressing BADH/CDH were able to grow to higher final densities and to accumulate more glycine betaine than cells expressing CDH only. The intracellular glycine betaine levels were almost 5-fold higher for BADH/CDH when product concentration was related to CDH activity. Also, after culturing the cells at high NaCl concentrations, more glycine betaine was accumulated. On medium containing 20 mM choline, transgenic tobacco plants expressing BADH/CDH grew considerably faster than vector-transformed control plants.