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Key Documents

R3150

Sigma-Aldrich

Monoclonal Anti-RhoGAP (p190) antibody produced in mouse

clone D2D6, purified immunoglobulin, buffered aqueous solution

Synonym(s):

Anti-GRLF1, Anti-Glucorticoid Receptor Binding Factor 1, Anti-p190

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

D2D6, monoclonal

form

buffered aqueous solution

mol wt

antigen ~190 kDa

species reactivity

mouse, rat, monkey, human

technique(s)

immunoprecipitation (IP): 4 μg using 500 μg of a human A431 cell RIPA lysate
western blot: 0.5-2 μg/mL using RIPA lysates from human A431 cells

isotype

IgG

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... GRLF1(2909)
mouse ... Grlf1(232906)
rat ... Grlf1(306400)

Immunogen

GST fusion protein corresponding to amino acids 180-610 of rat p190 RhoGAP.

Other Notes

RhoGAP appears to couple signal transduction via Ras and Rho through its association with RasGAP.

Physical form

Solution in 0.1 M Tris-glycine, pH 7.4, containing 0.15 sodium chloride and 0.05% sodium azide.

Preparation Note

Purified using protein G.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class

10 - Combustible liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

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Brajendra K Tripathi et al.
The Journal of cell biology, 218(9), 3060-3076 (2019-07-17)
SRC and ERK kinases control many cell biological processes that promote tumorigenesis by altering the activity of oncogenic and tumor suppressor proteins. We identify here a physiological interaction between DLC1, a focal adhesion protein and tumor suppressor, with SRC and

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