Cell Signaling Technology

Product Pathways - Cytoskeletal Signaling

Phospho-DRP1 (Ser637) Antibody #4867

DLP1   DNM1L   Dynamin-like protein 1   Dynamin-related protein 1  

No. Size Price
4867S 100 µl ( 10 western blots ) ¥3,900.00 现货查询 购买询价
4867 carrier free & custom formulation / quantityemail request
Applications Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W 1:1000 Rat, Endogenous 78-82 Rabbit
IP 1:100

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting, IP=Immunoprecipitation,


Species predicted to react based on 100% sequence homology: Human, Mouse, Monkey,

Specificity / Sensitivity

Phospho-DRP1 (Ser637) Antibody detects endogenous levels of DRP1 only when phosphorylated at Ser637.

Phospho-DRP1 (Ser637) 抗体仅识别Ser637磷酸化的内源性Diap1蛋白。

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser637 of human DRP1 protein. Antibodies are purified by protein A and peptide affinity chromatography.


Western Blotting

Western Blotting

Western blot analysis of extracts from PC-12 cells, untreated or treated with 20uM Forskolin #3828 for 1 hour, using Phospho-DRP1 (Ser637) Antibody. 使用Phospho-DRP1 (Ser637) Antibody,免疫印迹(Western Blot)分析PC-12细胞中Phospho-DRP1 (Ser637)蛋白水平。细胞分为未处理组和20uM Forskolin #3828处理1 h组。



Immunoprecipitation of PC-12 cell lysates, untreated or treated with 20 μM Forskolin #3828 for 1 hour, using Phospho-DRP1 (Ser637) Antibody. The western blot was probed using the same antibody. Lanes 1 and 2 are 5% input. 使用Phospho-DRP1 (Ser637) Antibody,免疫沉淀(Immunoprecipitation)分析PC-12细胞裂解物,细胞分为未处理组和20uM Forskolin #3828处理1 h组。使用同样的抗体进行免疫印迹(Western blot)实验。第1和2道是5% input。


Dynamin-related protein 1 (DRP1) is a member of the dynamin superfamily of GTPases. Members of this family have diverse cellular functions including vesicle scission, organelle fission, viral resistance, and intracellular trafficking (reviewed in 1). DRP1 affects mitochondrial morphology and is important in mitochondrial and peroxisomal fission in mammalian cells (2-5). The yeast ortholog of DRP1 clusters into a spiral-shaped structure on the mitochondrial membrane at the site of fission (reviewed in 6), and this structure is likely conserved in mammalian cells (3). The division of the mitochondria, which is required for apoptosis as well as normal cell growth and development, is controlled, in part, by the phosphorylation of DRP1 at Ser616 by Cdk1/cyclin B and at Ser637 by protein kinase A (PKA) (reviewed in 6). When phosphorylated at Ser616, DRP1 stimulates mitochondrial fission during mitosis. Conversely, fission is inhibited when DRP1 is phosphorylated at Ser637 (reviewed in 6). Dephosphorylation of Ser637 by calcineurin reverses this inhibition (7). In addition to phosphorylation, sumoylation of DRP1 is also an enhancer of mitochondrial fission (8). Balancing fission and fusion events is essential for proper mitochondrial function. Mitochondrial defects are seen in a variety of neurodegenerative diseases including Alzheimer's disease, Parkinson's disease, and Huntington's disease (reviewed in 6).

Dynamin-related protein 1 (DRP1)是GTPases dynamin超家族的一员。该家族的成员具有多种功能包括囊泡分离,细胞器分裂,对抗病毒以及胞内示踪(1)。DRP1影响线粒体的形态,对哺乳动物细胞中线粒体和过氧化物酶病裂变有重要作用(2-5)。DRP1的酵母同源蛋白成簇排列在线粒体分裂位置的线粒体膜螺旋状结构处(6),这个结构似乎在哺乳动物细胞中也是保守的(3)。线粒体的分裂部分通过DRP1的616位丝氨酸被Cdk1/cyclin B磷酸化和637位丝氨酸被蛋白激酶A(PKA)磷酸化调控(6),线粒体的分裂对细胞凋亡、正常细胞生长和发育都是必须的。616位丝氨酸被磷酸化后,DRP1刺激有丝分裂时的线粒体分裂。相反的,DRP1的637位丝氨酸被磷酸化后分裂受限(6)。磷酸酶去磷酸化637位丝氨酸后,抑制被翻转(7)。除了磷酸化,DRP1的SUMO化也是线粒体分裂的促进因素(8)。分裂和融合之间的平衡是正常发挥线粒体功能所必需的。研究证明线粒体缺陷会导致多种神经功能障碍包括阿尔兹海默症,帕金森病和亨廷顿症(6)。

  1. Praefcke, G.J. and McMahon, H.T. (2004) Nat Rev Mol Cell Biol 5, 133-47.
  2. Taguchi, N. et al. (2007) J Biol Chem 282, 11521-9.
  3. Smirnova, E. et al. (2001) Mol Biol Cell 12, 2245-56.
  4. Smirnova, E. et al. (1998) J Cell Biol 143, 351-8.
  5. Koch, A. et al. (2003) J Biol Chem 278, 8597-605.
  6. Knott, A.B. et al. (2008) Nat Rev Neurosci 9, 505-18.
  7. Cereghetti, G.M. et al. (2008) Proc Natl Acad Sci USA 105, 15803-8.
  8. Zunino, R. et al. (2007) J Cell Sci 120, 1178-88.

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