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SLF Sale

(Synonyms: Synthetic Ligand of FKBP) 目录号 : GC44899

A synthetic FK-506 Binding Protein (FKBP) ligand

SLF Chemical Structure

Cas No.:195513-96-3

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5 mg
¥765.00
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10 mg
¥1,428.00
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50 mg
¥5,710.00
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100 mg
¥9,483.00
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Sample solution is provided at 25 µL, 10mM.

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产品描述

FK-506 is a potent immunosuppressant that forms a high affinity complex (Ki = 0.2 nM) with FK-506 binding protein 12 (FKBP12). This complex inhibits the activity of the calcium/calmodulin-dependent protein phosphatase, calcineurin, leading to disruption of T-cell activation. Synthetic ligand of FKBP (SLF) is a cell-permeable analog of FK-506 that binds tightly to FKBP but lacks the ability to inhibit calcineurin. By itself, SLF does not exhibit a significant cellular response. However, homodimers of SLF or heterodimers with another protein ligand, provide a method to promote the dimerization of ligand-specific fusion proteins to induce signaling events within a cellular environment. For example, SLF monomers connected with a 10-atom linker activates Fas signaling via Fas-FKBP fusion proteins with an EC50 of 6 nM.

Chemical Properties

Cas No. 195513-96-3 SDF
别名 Synthetic Ligand of FKBP
Canonical SMILES COc1cc(CCC(OC(=O)[C@@H]2CCCCN2C(=O)C(=O)C(C)(C)CC)c2cccc(N)c2)ccc1OC
分子式 C30H40N2O6 分子量 524.7
溶解度 DMF: 30 mg/ml,DMSO: 30 mg/ml,Ethanol: 30 mg/ml,Ethanol:PBS (pH 7.2)(1:3): .2 mg/ml 储存条件 Store at -20°C
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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。
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1 mg 5 mg 10 mg
1 mM 1.9059 mL 9.5293 mL 19.0585 mL
5 mM 0.3812 mL 1.9059 mL 3.8117 mL
10 mM 0.1906 mL 0.9529 mL 1.9059 mL
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Research Update

Superior longitudinal fasciculus (SLF) I and II: an anatomical and functional review

J Neurosurg Sci 2021 Dec;65(6):560-565.PMID:33940781DOI:10.23736/S0390-5616.21.05327-3.

In this review, we summarize the current knowledge regarding the Superior Longitudinal Fasciculus (SLF) I and II. These fibers represent a longitudinal association tract between the parietal and frontal lobes of the brain. We highlight the anatomical representation of the SLF I and II in the primate and in the human brain. The fibers of the SLF I extend from the superior parietal lobule and precuneus, running anteriorly to reach the superior frontal gyrus and the supplementary motor area. The anatomy of the SLF I is debated in the literature, with some Authors questioning the existence of the SLF I as an individual tract. The SLF II is located inferiorly and laterally compared to the SLF I. The fibers of the SLF II extend from the inferior parietal lobule to the middle frontal gyrus. The putative functions of these tracts are reviewed, with particular regards to intraoperative findings and their relevance in applied neurosurgery. Considered together, the two tracts link associative parietal areas with premotor and supplementary motor frontal areas. The two tracts seem therefore involved in supporting the integration of sensory information and motor planning, finalized to visuospatial attention and complex motor behavior. Finally, we discuss future directions for further study of these fiber tracts, highlighting the need for more detailed anatomical study of the SLF I and additional intraoperative tests that have been suggested to explore the function of these tracts during surgery.

Signaling pathways influencing SLF and c-kit-mediated survival and proliferation

Immunol Res 2006;35(1-2):1-12.PMID:17003505DOI:10.1385/IR:35:1:1.

Steel factor (SLF) and c-Kit are a ligand-receptor pair that regulates growth and activation of a variety of hemopoietic and non-hemopoietic cells. This review describes our work investigating downstream signaling pathways activated by SLF, with particular emphasis on signaling differences associated with soluble vs membrane- bound ligand, and our identification of an important role for PLC activation and Ca2+ influx in supporting c-Kit positive cells in vitro and in vivo. This work led to the identification of a unique form of cell death termed activation enhanced cell death (AECD) that involves stimulating a cell with a growth or activation signal while concurrently blocking Ca2+ influx. Approaches that we have taken toward identifying cellular factors associated with sensitivity and resistance to AECD are summarized, as is our experience with a variety of experimental models. The use of econazole as a calcium channel blocker and its mechanism of action are described, as is its potential for development as an anticancer therapeutic.

SCF(SLF)-mediated cytosolic degradation of S-RNase is required for cross-pollen compatibility in S-RNase-based self-incompatibility in Petunia hybrida

Front Genet 2014 Jul 22;5:228.PMID:25101113DOI:10.3389/fgene.2014.00228.

Many flowering plants adopt self-incompatibility (SI) to maintain their genetic diversity. In species of Solanaceae, Plantaginaceae, and Rosaceae, SI is genetically controlled by a single S-locus with multiple haplotypes. The S-locus has been shown to encode S-RNases expressed in pistil and multiple SLF (S-locus F-box) proteins in pollen controlling the female and male specificity of SI, respectively. S-RNases appear to function as a cytotoxin to reject self-pollen. In addition, SLFs have been shown to form SCF (SKP1/Cullin1/F-box) complexes to serve as putative E3 ubiquitin ligase to interact with S-RNases. Previously, two different mechanisms, the S-RNase degradation and the S-RNase compartmentalization, have been proposed as the restriction mechanisms of S-RNase cytotoxicity allowing compatible pollination. In this study, we have provided several lines of evidence in support of the S-RNase degradation mechanism by a combination of cellular, biochemical and molecular biology approaches. First, both immunogold labeling and subcellular fractionation assays showed that two key pollen SI factors, PhS3L-SLF1 and PhSSK1 (SLF-interacting SKP1-like1) from Petunia hybrida, a Solanaceous species, are co-localized in cytosols of both pollen grains and tubes. Second, PhS3L-RNases are mainly detected in the cytosols of both self and non-self-pollen tubes after pollination. Third, we found that PhS-RNases selectively interact with PhSLFs by yeast two-hybrid and co-immunoprecipitation assays. Fourth, S-RNases are specifically degraded in compatible pollen tubes by non-self SLF action. Taken together, our results demonstrate that SCF(SLF-mediated) non-self S-RNase degradation occurs in the cytosol of pollen tube through the ubiquitin/26S proteasome system serving as the major mechanism to neutralize S-RNase cytotoxicity during compatible pollination in P. hybrida.

Identification of a canonical SCF(SLF) complex involved in S-RNase-based self-incompatibility of Pyrus (Rosaceae)

Plant Mol Biol 2013 Feb;81(3):245-57.PMID:23263858DOI:10.1007/s11103-012-9995-x.

S-RNase-based self-incompatibility (SI) is an intraspecific reproductive barrier to prevent self-fertilization found in many species of the Solanaceae, Plantaginaceae and Rosaceae. In this system, S-RNase and SLF/SFB (S-locus F-box) genes have been shown to control the pistil and pollen SI specificity, respectively. Recent studies have shown that the SLF functions as a substrate receptor of a SCF (Skp1/Cullin1/F-box)-type E3 ubiquitin ligase complex to target S-RNases in Solanaceae and Plantaginaceae, but its role in Rosaceae remains largely undefined. Here we report the identification of two pollen-specific SLF-interacting Skp1-like (SSK) proteins, PbSSK1 and PbSSK2, in Pyrus bretschneideri from the tribe Pyreae of Rosaceae. Both yeast two-hybrid and pull-down assays demonstrated that they could connect PbSLFs to PbCUL1 to form a putative canonical SCF(SLF) (SSK/CUL1/SLF) complex in Pyrus. Furthermore, pull-down assays showed that the SSK proteins could bind SLF and CUL1 in a cross-species manner between Pyrus and Petunia. Additionally, phylogenetic analysis revealed that the SSK-like proteins from Solanaceae, Plantaginaceae and Rosaceae form a monoclade group, hinting their shared evolutionary origin. Taken together, with the recent identification of a canonical SCF(SFB) complex in Prunus of the tribe Amygdaleae of Rosaceae, our results show that a conserved canonical SCF(SLF/SFB) complex is present in Solanaceae, Plantaginaceae and Rosaceae, implying that S-RNase-based self-incompatibility shares a similar molecular and biochemical mechanism.

Size distributions of particle-generated hydroxyl radical (·OH) in surrogate lung fluid (SLF) solution and their potential sources

Environ Pollut 2021 Jan 1;268(Pt B):115582.PMID:33017744DOI:10.1016/j.envpol.2020.115582.

Although it is known that increases in ambient particulate matter (PM) levels are associated with elevated occurrence of adverse health outcomes, the understanding of the mechanisms of PM-related health effects is limited by our knowledge of how particle size and composition are altered subsequent to inhalation through respiratory-deposited processing. Here we present a particle-generated hydroxyl radical (·OH) study of the size-resolved particles as particles are inhaled in the human respiratory tract (RT), and we show that accumulation-mode particles are significant factors (71-75%) in ·OH generation of lung-deposited particles using Multiple-Path Particle Dosimetry (MPPD) model. The ability of PM to catalyze ·OH generation is mainly related to transition metals, particularly towards the upper regions of the RT (75%), and to quinones deeper in the lung (42-46%). Identification of this generation ability induced by chemical composition has shown that four potential sources (biomass burning, incomplete combustion, mobile & industry, and mineral dust) are responsible for ·OH generation. With ·OH-forming ability after PM inhalation implicated as the first step towards revealing the subsequent toxic processes, this work draws a connection between the detailed ·OH chemistry occurring on size-resolved particles and a possible toxicological mechanism based on chemical composition and sources.