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Santa Cruz Biotechnology, Inc.
Rac 2 (L-10):
sc-23121
BACKGROUND
A large number of low molecular weight, GTP binding proteins of
the Ras superfamily have been identified (1). These proteins regulate
many fundamental processes in all eukaryotic cells such as growth,
vesicle traffic and cytoskeletal organization. GTPase-activating
proteins (GAPs) accelerate the intrinsic rate of GTP hydrolysis of
Ras-related proteins, resulting in downregulation of their active
form (2-6). Two proteins in this family, Rac 1 and Rac 2, are
92% identical and share GTP binding and GTP hydrolysis motifs
with other members of the Ras superfamily (7,8). Rac 1 is
expressed in a large number of different cell types. Rac 2 is
primarily expressed only in myeloid cells (8) and has been reported
to be a regulatory component of the human neutrophil NADPH
oxidase (9).
SOURCE
Rac 2 (L-10) is an affinity purified goat polyclonal antibody raised
against a peptide mapping near the carboxy terminus of Rac 2 of
human origin.
PRODUCT
Each vial contains 200 μg IgG in 1.0 ml PBS containing
0.1% sodium azide and 0.2% gelatin.
Blocking peptide is available for competition studies (sc-23121 P)
(100 μg peptide in 0.5 ml PBS with 0.1% sodium azide and
100 μg BSA).
SPECIFICITY
Rac 2 (L-10) is recommended for the detection of Rac 2 of mouse,
rat and human origin by Western blotting and immunohisto-
chemistry.
Recommended dilution range for Western blot analysis:
1:100–1:1000. Recommended starting dilution: 1:100.
STORAGE
Store at 4° C, do not freeze; stable for one year from the date of
shipment.
RESEARCH USE
For research use only, not for use in diagnostic procedures.
BACKGROUND REFERENCES
1. Hall, A. 1990. The cellular functions of small GTP-binding
proteins. Science 249: 636-640.
2. Trahey, M. and McCormick, F. 1987. A cytoplasmic protein
stimulates normal N-
ras
p21 GTPase, but does not affect
oncogenic mutants. Science 238: 542-545.
3. Martin, G.A., Viskochil, D., Bollag, G., McCabe, P.C.,
Crosier, W.J., Haubruck, H., Conroy, L., Clark, R.,
O’Connell, P., Cawthon, R.M., Innis, M.A., and McCormick, F.
1990. The GAP-related domain of the neurofibromatosis type 1
gene product interacts with
ras
p21. Cell 63: 843-849.
4. Ballester, R.M., Marchuk, D., Boguski, M., Saulino, A.,
Letcher, R., Wigler, M., and Collins, F. 1990. The NF1 locus
encodes a protein functionally related to mammalian GAP and
yeast
IRA
proteins. Cell 63: 851-859.
5. Xu, G., Lin, B., Tanaka, K., Dunn, D., Wood, D.,
Gesteland, R., White, R., Weiss, R., and Tamanoi, F. 1990. The
catalytic domain of the neurofibromatosis type 1 gene product
stimulates
ras
GTPase and complements
ira
mutants of
S.
cerevisiae
. Cell 63: 835-841.
6. Diekmann, D., Brill, S., Garrett, M.D., Totty, N., Hsuan, J.,
Monfries, C., Hall, C., Lim, L. and Hall, A. 1991.
Bcr
encodes a
GTPase-activating protein for p21
rac
. Nature 351: 400-402.
7. Sewell, J.L. and Kahn, R.A. 1988. Sequences of the bovine and
yeast ADP-ribosylation factor and comparison to other
GTP-binding proteins. Proc. Natl. Acad. Sci. USA 85: 4620-4624.
8. Didsbury, J., Weber, R.F., Bokoch, G.M., Evans, T. and
Snyderman, R. 1989.
Rac
, a novel
ras
-related family of proteins
that are botulinum toxin substrates. J. Biol. Chem.
264: 16378-16382.
9. Knaus, U.G., Heyworth, P.G., Evans, T., Curnutte, J.T., and
Bokoch, G.M. 1991. Regulation of phagocyte oxygen radical
production by the GTP-binding protein Rac2. Science
254: 1512-1515.
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