Cell Signaling Technology

Product Pathways - Cytoskeletal Signaling

NSF Antibody #2145

Applications Reactivity Sensitivity MW (kDa) Source
W IP IF-F H M R Hm Mk Endogenous 78 Rabbit

Applications Key:  W=Western Blotting  IP=Immunoprecipitation  IF-F=Immunofluorescence (Frozen)
Reactivity Key:  H=Human  M=Mouse  R=Rat  Hm=Hamster  Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

NSF Antibody detects endogenous levels of total NSF protein.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu524 of human NSF. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from SHSY5Y, Neuro2A, PC12 and CHO cells using NSF Antibody.

IP

IP

Immunoprecipitation of NSF from untreated HeLa cell extracts using NSF antibody (Lane 3). Lane 1: Input control. Lane 2: No antibody control.

IF-F

IF-F

Confocal immunofluorescent analysis of normal rat brain using NSF Antibody (red) and GFAP (GA5) Mouse mAb #3670 (green) showing cytoplasmic localization in neurons in the deep cerebellar nuclei (left) and the pons (right). Blue pseudocolor = DRAQ5® (fluorescent DNA dye).


Background

Several protein-protein interactions are essential to membrane fusion during endocytosis. Membrane fusion requires interaction among SNARE1 proteins associated with both donor and acceptor membranes (1,2). Following membrane fusion, the α-SNAP cytoplasmic adapter protein binds to the SNARE complex. N-ethylmaleimide-sensitive factor (NSF), a hexameric ATPase, then associates with the α-SNAP/SNARE complex to mediate SNARE disassembly during membrane fusion (3,4). The ATPase activity of NSF induces a conformational change in the α-SNAP/SNARE complex that leads to its dissociation from the membrane, membrane fusion and eventual recycling of the SNARE complex for subsequent membrane fusion (3,4).

  1. Ungermann, C. and Langosch, D. (2005) J Cell Sci 118, 3819-28.
  2. Leabu, M. (2006) J Cell Mol Med 10, 423-7.
  3. May, A.P. et al. (2001) J Biol Chem 276, 21991-4.
  4. Dalal, S. et al. (2004) Mol Biol Cell 15, 637-48.

Application References

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Companion Products

For Research Use Only. Not For Use In Diagnostic Procedures.

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