Cell Signaling Technology

Product Pathways - Cytoskeletal Signaling

Rac1/2/3 (L129) Antibody #2467

Applications Reactivity MW (kDa) Source
W IF-IC H M R Mk B 21 Rabbit

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

Specificity / Sensitivity

Rac 1/2/3 (L129) Antibody detects endogenous levels of total Rac1/2/3 proteins.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide corresponding to the sequence of human Rac1/2/3. Antibodies are purified using protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines, using Rac1/2/3 (L129) Antibody.

IF-IC

IF-IC

Immunofluorescent analysis of HUVEC cells, using Rac1/2/3 (L129) Antibody (left) or phalloidin (right).

Background

Rac and Cdc42 are members of the Rho-GTPase family. In mammals, Rac exists as three isoforms, Rac1, Rac2 and Rac3, which are highly similar in sequence. Rac1 and Cdc42, the most widely studied of this group, are ubiquitously expressed. Rac2 is expressed in cells of hematopoietic origin, and Rac3, while highly expressed in brain, is also found in many other tissues. Rac and Cdc42 play key signaling roles in cytoskeletal reorganization, membrane trafficking, transcriptional regulation, cell growth and development (1). GTP binding stimulates the activity of Rac/Cdc42, and the hydrolysis of GTP to GDP through the protein's intrinsic GTPase activity, rendering it inactive. GTP hydrolysis is aided by GTPase activating proteins (GAPs), while exchange of GDP for GTP is facilitated by guanine nucleotide exchange factors (GEFs). Another level of regulation is achieved through the binding of RhoGDI, a guanine nucleotide dissociation inhibitor, which retains Rho family GTPases, including Rac and Cdc42, in their inactive GDP-bound state (2,3).

  1. Wennerberg, K. and Der, C.J. (2004) J. Cell Sci. 117, 1301-1312.
  2. Bernards, A. and Settleman, J. (2004) Trends Cell Biol. 14, 377-385.
  3. Rossman, K.L. et al. (2005) Nat. Rev. Mol. Cell Biol. 6, 167-180.

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