Revision 1

#74792Store at -20C

1 Kit

(8 x 20 microliters)

Cell Signaling Technology

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For Research Use Only. Not for Use in Diagnostic Procedures.
Product Includes Product # Quantity Mol. Wt Isotype/Source
Tom20 (D8T4N) Rabbit mAb 42406 20 µl 16 kDa Rabbit IgG
OPA1 (D6U6N) Rabbit mAb 80471 20 µl 80-100 kDa Rabbit IgG
DRP1 (D6C7) Rabbit mAb 8570 20 µl 78-82 kDa Rabbit IgG
Phospho-DRP1 (Ser616) (D9A1) Rabbit mAb 4494 20 µl 78-82 kDa Rabbit IgG
Phospho-DRP1 (Ser637) (D3A4) Rabbit mAb 6319 20 µl 78-82 kDa Rabbit IgG
MFF (E5W4M) XP® Rabbit mAb 84580 20 µl 25, 27, 30, 35 kDa Rabbit IgG
Mitofusin-1 (D6E2S) Rabbit mAb 14739 20 µl 82 kDa Rabbit IgG
Mitofusin-2 (D1E9) Rabbit mAb 11925 20 µl 80 kDa Rabbit IgG
Anti-rabbit IgG, HRP-linked Antibody 7074 100 µl Goat 

Please visit for individual component applications, species cross-reactivity, dilutions, protocols, and additional product information.


The Mitochondrial Dynamics Antibody Sampler Kit II provides an economical means to examine signaling involved in mitochondrial dynamics. The kit includes enough antibodies to perform two western blot experiments with each primary antibody.


Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibodies.


Import of proteins into the mitochondria is regulated by the translocase of the outer mitochondrial membrane (TOM) complex, which facilitates transport through the outer mitochondrial membrane, and a complementary translocase of the inner membrane (TIM) complex, responsible for protein transport to the mitochondrial matrix. The TOM complex consists of the receptors Tom20, Tom22, and Tom70, and the channel-forming protein Tom40 (1). Tom20 is localized in the outer mitochondrial membrane and initially recognizes precursors with a presequence to facilitate protein import across the outer mitochondrial membrane (2).
Changes in mitochondrial dynamics regulated by environmental cues affect mitochondrial size and shape and have been shown to dramatically impact mitochondrial metabolism, apoptosis, and autophagy (3). These processes are largely controlled by mitochondrial dynamin-related GTPases, including mitofusin-1, mitofusin-2, OPA1, and DRP1. DRP1 regulates mitochondrial fission, while the mitofusins and OPA1 control fusion at the outer and inner mitochondrial membrane, respectively. These proteins are tightly regulated. OPA1 activity is regulated through alternative splicing and post-translational modifications, including complex proteolytic processing by multiple proteases (4-9). In addition, OPA1 expression can be induced under conditions of metabolic demand through a pathway involving Parkin induced NF-κB activation (10). DRP1 is regulated in part through multiple phosphorylation sites (11). Phosphorylation of DRP1 at Ser616 by MAPK or during mitosis by CDKs stimulates mitochondrial fission (12-14). In contrast, PKA dependent phosphorylation of DRP1 at Ser637 inhibits its GTPase activity and mitochondrial fission (15,16). Mitochondrial fission factor (MFF) is a tail-anchored protein that resides within the outer mitochondrial membrane and is part of the mitochondrial fission complex. MFF participates in mitochondrial fission by serving as one of multiple receptors for the GTPase dynamin-related protein 1 (Drp1) (17-20). AMPK directly phosphorylates MFF at two sites to allow for enhanced recruitment of Drp1 to the mitochondria (21). 

  1. Chacinska, A. et al. (2009) Cell 138, 628-44.
  2. Saitoh, T. et al. (2007) EMBO J 26, 4777-87.
  3. Kasahara, A. and Scorrano, L. (2014) Trends Cell Biol 24, 761-70.
  4. Delettre, C. et al. (2001) Hum Genet 109, 584-91.
  5. Olichon, A. et al. (2007) Cell Death Differ 14, 682-92.
  6. Ishihara, N. et al. (2006) EMBO J 25, 2966-77.
  7. Cipolat, S. et al. (2006) Cell 126, 163-75.
  8. Griparic, L. et al. (2007) J Cell Biol 178, 757-64.
  9. Merkwirth, C. et al. (2008) Genes Dev 22, 476-88.
  10. Müller-Rischart, A.K. et al. (2013) Mol Cell 49, 908-21.
  11. Knott, A.B. et al. (2008) Nat Rev Neurosci 9, 505-18.
  12. Kashatus, J.A. et al. (2015) Mol Cell 57, 537-51.
  13. Kashatus, D.F. et al. (2011) Nat Cell Biol 13, 1108-15.
  14. Taguchi, N. et al. (2007) J Biol Chem 282, 11521-9.
  15. Chang, C.R. and Blackstone, C. (2007) J Biol Chem 282, 21583-7.
  16. Cribbs, J.T. and Strack, S. (2007) EMBO Rep 8, 939-44.
  17. Liu, R. and Chan, D.C. (2015) Mol Biol Cell 26, 4466-77.
  18. Shen, Q. et al. (2014) Mol Biol Cell 25, 145-59.
  19. Losón, O.C. et al. (2013) Mol Biol Cell 24, 659-67.
  20. Otera, H. et al. (2010) J Cell Biol 191, 1141-58.
  21. Toyama, E.Q. et al. (2016) Science 351, 275-281.

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