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Zapalog Sale

目录号 : GC66370

Zapalog 是一种光可裂解的小分子异二聚体,可用于重复启动和瞬间终止两种靶蛋白之间的物理相互作用。 Zapalog 对用 FKBP 和 DHFR 结构域标记的任何两种蛋白质进行二聚化,直到暴露于光下导致其光解。

Zapalog Chemical Structure

Cas No.:1708091-24-0

规格 价格 库存 购买数量
5mg
¥13,050.00
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产品描述

Zapalog is a photocleavable small-molecule heterodimerizer that can be used to repeatedly initiate, and instantaneously terminate, a physical interaction between two target proteins. Zapalog dimerizes any two proteins tagged with the FKBP and DHFR domains until exposure to light causes its photolysis[1].

Chemical Properties

Cas No. 1708091-24-0 SDF Download SDF
分子式 C58H73N7O15 分子量 1108.24
溶解度 DMSO : 100 mg/mL (90.23 mM; Need ultrasonic) 储存条件 Store at -20°C
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1 mM 0.9023 mL 4.5117 mL 9.0233 mL
5 mM 0.1805 mL 0.9023 mL 1.8047 mL
10 mM 0.0902 mL 0.4512 mL 0.9023 mL
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Research Update

The light-sensitive dimerizer Zapalog reveals distinct modes of immobilization for axonal mitochondria

Nat Cell Biol 2019 Jun;21(6):768-777.PMID:31061466DOI:10.1038/s41556-019-0317-2.

Controlling cellular processes with light can help elucidate their underlying mechanisms. Here we present Zapalog, a small-molecule dimerizer that undergoes photolysis when exposed to blue light. Zapalog dimerizes any two proteins tagged with the FKBP and DHFR domains until exposure to light causes its photolysis. Dimerization can be repeatedly restored with uncleaved Zapalog. We implement this method to investigate mitochondrial motility and positioning in cultured neurons. Using Zapalog, we tether mitochondria to constitutively active kinesin motors, forcing them down the axon towards microtubule (+) ends until their instantaneous release via blue light, which results in full restoration of their endogenous motility. We find that one-third of stationary mitochondria cannot be pulled away from their position and that these firmly anchored mitochondria preferentially localize to VGLUT1-positive presynapses. Furthermore, inhibition of actin polymerization with latrunculin A reduces this firmly anchored pool. On release from exogenous motors, mitochondria are preferentially recaptured at presynapses.

Spatial and Temporal Control of Protein Secretion with Light

Methods Mol Biol 2022;2473:29-45.PMID:35819757DOI:10.1007/978-1-0716-2209-4_4.

How newly synthesized integral membrane proteins and secreted factors are sorted and trafficked to the appropriate location in different cell types remains an important problem in cell biology. One powerful approach for elucidating the trafficking route of a specific protein is to sequester it following synthesis in the endoplasmic reticulum and trigger its release with an externally applied cue. Combined with fluorescent probes, this approach can be used to directly visualize each trafficking step as cargo molecules progress through the different organelles of the secretory network. Here, we discuss design strategies and practical implementation of an inducible protein secretion system we recently developed (Zapalog mediated ER trap: zapERtrap) that allows one to use light to initiate secretory trafficking from targeted cells or subcellular domains. We provide detailed protocols for experiments using this approach to visualize protein trafficking from the endoplasmic reticulum to the plasma membrane in fibroblast cell lines and primary cultured neurons.