Cell Signaling Technology

Product Pathways - Cytoskeletal Signaling

Syntaxin 6 Antibody #2417

Applications Reactivity MW (kDa) Source
W IP IF-IC H M R Mk 32 Rabbit

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

Specificity / Sensitivity

Syntaxin 6 Antibody detects endogenous levels of total Syntaxin 6 protein.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) corresponding residue surrounding Tyr140 of mouse syntaxin 6 protein. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines, using Syntaxin 6 Antibody.

IP

IP

Western blot analysis of A172 lysate (lane1) and immunoprecipitates generated in the absence or presence of A172 cell lysate (lanes 2 and 3), using Syntaxin 6 Antibody both as precipitation and probing antibody.

IF-IC

IF-IC

Confocal immunofluorescent analysis of MCF-7 cells, using Syntaxin 6 Antibody (green). Blue pseudocolor = DRAQ5™ (fluorescent DNA dye).


Background

Syntaxin 6 is a ubiquitously expressed S25C family member of the SNARE proteins (1,2). The protein has an amino-terminal H1 domain followed by an H2 SNARE domain and a carboxy-terminal membrane anchor (3). Syntaxin 6 protein is localized to the trans-Golgi and within endosomes and regulates membrane trafficking by partnering with a variety of other SNARE proteins (3-5). Depending on cell type and SNARE parter, syntaxin 6 is involved in the regulation of GLUT4 trafficking, neutrophil exocytosis and granule secretion (6-10).

  1. Bock, J.B. et al. (2001) Nature 409, 839-841.
  2. Bock, J.B. et al. (1996) J. Biol. Chem. 271, 17961-17965.
  3. Wendler, F. and Tooze, S. (2001) Traffic 2, 606-611.
  4. Bock, J.B. et al. (1997) Mol. Biol. Cell 8, 1261-1271.
  5. Mallard, F. et al. (2002) J. Cell Biol. 156, 653-664.
  6. Perera, H.K. et al. (2003) Mol. Biol. Cell 14, 2946-2958.
  7. Shewan, A.M. et al. (2003) Mol. Biol. Cell 14, 973-986.
  8. Martin-Martin, B. et al. (2000) Blood 96, 2574-25783.
  9. Wendler, F. et al. (2001) Mol. Biol. Cell 12, 1699-1709.
  10. Kuliawat, R. et al. (2004) Mol. Biol. Cell 15, 1690-1701.

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