Technical Data
R1998-35
Rho, NT
Description:
Rho belongs to the Ras super family of low molecular weight GTPases. Fifteen Rho proteins have already been characterized and divided into three sub-families; the first includes Rho (A, B, C), the second, Rnd 1-3 and the third which includes Rac 1-3, RhoG, Cdc42Hs, Rho/TTF. TC10 and Chp (1-2). Rho acts as a molecular switch which turns on of off various intracellular signaling pathways such as ACK, PAKs, MEKKs ROCK (3). Rho is active when bound to GTP and inactive when bound to GDP (4). It is also known to participate in many physiological activities including cell migration, adhesion, cytokinesis, proliferation, differentiation and apoptosis and to a greater extend cell transformation (5).

Applications:
Suitable for use in Western Blot, Immunohistochemistry, Immunocytochemistry. Other applications not tested.

Recommended Dilution:
Western Blot: 1:2,000
Immunohistochemistry: 1:50-1:100
Immunocytochemistry: 1:100-1:250
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4°C for short-term only. For long-term storage, store at -20°C. Aliquots are stable for at least 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
TypeIsotypeCloneGrade
MabIgG9E528Supernatant
SizeStorageShippingSourceHost
100ul-20°CBlue IceHumanRabbit
Concentration:
Not determined
Immunogen:
A synthetic peptide corresponding to residues in the N-term of human Rho.
Purity:
Supernatant
Form
Supplied as a liquid in 50 mM Tris-Glycine, pH 7.4, 0.15 M sodium chloride, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
Specificity:
Recognizes human Rho, NT. Species ccrossreactivity: mouse and rat. Species sequence Homology: RhoA, RhoB and RhoC.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Murphy et al. Nature. 384:427-432 2. Yeramian P, Chardin P, Madaule P, Tavitian A.Nucleic
Acids Res. 1987 Feb 25;15(4):1869. 3. Maekawa et al. Science 285: 895-898, 1999. 4. Boguski, M.S., and F. McCormick. 1993. Nature. 366:643- 654 5. Khosravi-Far, R., P.A. Solski, G.J. Clark, M.S. Kinch, and
C.J. Der. 1995. Mol. Cell. Biol. 15:6443-6453.