SPB
目录号 : GC33619
SPB是肺表面活性物质的主要成分，对正常肺功能至关重要。
Cas No.:858128-57-1
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
SPB is a key component of pulmonary surfactant, essential for normal lung function.
Human SP-B gene but not mouse SP-B is expressed in the lung of hTG SP-B-C and SP-B-T mice. For infected SP-B-C mice, the levels of bioluminescence increase rapidly from 0 to 24h after infection, remains high between 24 and 32 h, and then decreases; the bioluminescence levels are significantly lower (p<0.01) in the CMC2.24 treated group from 24 to 48 h after infection. In infected SP-B-T mice, the peak time of bioluminescence is at 12 h after infection, then the level decreases slowly. Lung tissues from of infected SP-B-C mice showed more apoptotic cells compared to infected SP-B-T mice. CMC2.24 treated SP-B-C and SP-B-T mice have decreased MMP-2, -9, and -12 activities compared to their respective untreated groups[1].
[1]. Xu Y, et al. DIFFERENTIAL SUSCEPTIBILITY OF HUMAN SP-B GENETIC VARIANTS ON LUNG INJURY CAUSED BY BACTERIAL PNEUMONIA AND THE EFFECT OF A CHEMICALLY MODIFIED CURCUMIN. Shock. 2016 Apr;45(4):375-84.
| Cas No. | 858128-57-1 | SDF | |
| Canonical SMILES | O=C(ON1C(CCC1=O)=O)CCCOC2=C(O3)C(C=CC3=O)=CC4=C2OC=C4 | ||
| 分子式 | C19H15NO8 | 分子量 | 385.32 |
| 溶解度 | DMSO : ≥ 34 mg/mL (88.24 mM) | 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 | 2.5952 mL | 12.9762 mL | 25.9525 mL |
| 5 mM | 0.519 mL | 2.5952 mL | 5.1905 mL |
| 10 mM | 0.2595 mL | 1.2976 mL | 2.5952 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。
Pcp1/pericentrin controls the SPB number in fission yeast meiosis and ploidy homeostasis
J Cell Biol 2022 Jan 3;221(1):e202104099.PMID:34747981DOI:10.1083/jcb.202104099.
During sexual reproduction, the zygote must inherit exactly one centrosome (spindle pole body [SPB] in yeasts) from the gametes, which then duplicates and assembles a bipolar spindle that supports the subsequent cell division. Here, we show that in the fission yeast Schizosaccharomyces pombe, the fusion of SPBs from the gametes is blocked in polyploid zygotes. As a result, the polyploid zygotes cannot proliferate mitotically and frequently form supernumerary SPBs during subsequent meiosis, which leads to multipolar nuclear divisions and the generation of extra spores. The blockage of SPB fusion is caused by persistent SPB localization of Pcp1, which, in normal diploid zygotic meiosis, exhibits a dynamic association with the SPB. Artificially induced constitutive localization of Pcp1 on the SPB is sufficient to cause blockage of SPB fusion and formation of extra spores in diploids. Thus, Pcp1-dependent SPB quantity control is crucial for sexual reproduction and ploidy homeostasis in fission yeast.
Kinetics of plasma SPB and RAGE during mechanical ventilation in patients undergoing major vascular surgery
Respir Physiol Neurobiol 2011 Sep 15;178(2):256-60.PMID:21736957DOI:10.1016/j.resp.2011.06.019.
Receptor-of-Advanced-Glycation-End-products (RAGE) and Surfactant-Protein-type-B (SPB) are reported as lung injury markers. Unlike SPB, RAGE is secreted by several tissues, so that RAGE specificity as lung injury marker is questionable. We measured SPB and RAGE in 19 patients undergoing major vascular abdominal surgery. SPB and RAGE were measured before mechanical ventilation (T0), at 1st (T1), 2nd (T2) and, when present, 3rd (T3) hour of mechanical ventilation, and 1h after extubation (T(POST)). Last data during mechanical ventilation, either T2 or T3, are reported as T(END). SPB and RAGE values were normalized for total protein (SPB(N) and RAGE(N)). SPB(N) and RAGE(N) increments from T0 to T(END) were 56.2 [39.1] ng/mg (mean [75-25 percentile]) and 10.6[7.1] pg/mg, respectively. SPB values increased progressively during mechanical ventilation, whereas RAGE values increased at T(1) but not thereafter. SPB(N) increase (T(END)-T0), but not RAGE(N), was related to ΔPaO(2)/FiO2 changes during mechanical ventilation (r=0.575, p=0.01). Plasma RAGE(N) and SPB(N) kinetics in patients undergoing major vascular surgery are different.
The liquid-liquid extractive fermentation of L-lactic acid in a novel semi-partition bioreactor (SPB)
J Biotechnol 2022 Dec 10;360:55-61.PMID:36330925DOI:10.1016/j.jbiotec.2022.10.017.
Fermentation technology is commonly used as a mature process to produce numerous products with the help of micro-organisms. However, these organisms are sometimes inhibited by the accumulation of these products or their by-products. One route to circumvent this is via extractive fermentation, which combines the fermentation process with extraction. To facilitate this, novel bioreactor designs are required, such as the semi-partition bioreactor (SPB) which has been recently proposed for in-situ extractive fermentation. The latter combines a fermentation and an extraction unit into a single vessel using a mixer-settler principle. Where the bioproduct is produced in the mixer and removed continuous in the settler. As the SPB functionality is a subject of interest, this study builds on demonstrating different process conditions in the production of a sample bioprocess (lactic acid (LA)) which is susceptible to product inhibition. The results showed a 34.5 g/L LA concentration was obtained in the pH-controlled condition. While LA production can suffer from product inhibition, neutralizing agents can be easily used to curb inhibitory problems, however, the LA fermentation is a simple (and well-studied) example, which can demonstrate an alternative route to avoiding product inhibition (for systems which cannot be rescued using pH control). Hence, to replicate a scenario of product inhibition, two different process conditions were investigated, no pH control with no extraction (non-integrated), and no pH control with integrated extractive fermentation. Key findings showed higher LA concentration in integrated (25.10 g/L) as compared to the non-integrated (14.94 g/L) case with improved yield (0.75 gg-1 (integrated) versus 0.60 gg-1 (non-integrated)) and overall productivity (0.35 gL-1h-1(integrated) versus 0.20 gL-1h-1(non-integrated)) likewise. This is the first demonstration of an SP bioreactor, and shows how the reactor can be applied to improve productivity. Based on these results, the SPB design can be applied to produce any product liable to product inhibition.
The fission yeast SPB component Dms1 is required to initiate forespore membrane formation and maintain meiotic SPB components
PLoS One 2018 May 29;13(5):e0197879.PMID:29813128DOI:10.1371/journal.pone.0197879.
The spindle pole body (SPB) plays a central role in spore plasma membrane formation in addition to its recognized role in microtubule organization. During meiosis, a biomembrane called the forespore membrane (FSM) is newly formed at the SPB. Although several SPB proteins essential for the initiation of FSM formation (meiotic SPB components) have been identified, the molecular mechanism is still unknown. Here, we report the isolation and functional characterization of Dms1 as a component of the SPB. We show that FSM formation does not initiate in dms1Δ cells. Dms1 protein is constitutively expressed throughout the life cycle and localizes to the SPB and the nuclear envelope. The predicted Dms1 protein has a transmembrane domain, which is required for correct localization at the SPB. Dms1 is essential for the proper localization of three meiotic SPB components, Spo15, Spo2, and Spo13, but these components do not affect localization of Dms1. Collectively, these results suggest that Dms1 anchors these meiotic SPB components to the SPB, thereby facilitating the initiation of FSM formation.
Localization of core spindle pole body (SPB) components during SPB duplication in Saccharomyces cerevisiae
J Cell Biol 1999 May 17;145(4):809-23.PMID:10330408DOI:10.1083/jcb.145.4.809.
We have examined the process of spindle pole body (SPB) duplication in Saccharomyces cerevisiae by electron microscopy and found several stages. These include the assembly, probably from the satellite, of a large plaque-like structure, the duplication plaque, on the cytoplasmic face of the half-bridge and its insertion into the nuclear envelope. We analyzed the role of the main SPB components in the formation of these structures by identifying them from an SPB core fraction by mass spectrometry. Temperature-sensitive mutants for two of the components, Spc29p and Nud1p, were prepared to partly define their function. The composition of two of the intermediates in SPB duplication, the satellite and the duplication plaque, was examined by immunoelectron microscopy. Both contain cytoplasmic SPB components showing that duplication has already been partly achieved by the end of the preceding cell cycle when the satellite is formed. We show that by overexpression of SPB components the structure of the satellite can be changed and SPB duplication inhibited by disrupting the attachment of the plaque-like intermediate to the half-bridge. We present a model for SPB duplication where binding of SPB components to either end of the bridge structure ensures two separate SPBs.