Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02 % sodium azide and 50 % glycerol.
Konservierungsmittel
Sodium azide
Vorsichtsmaßnahmen
WARNING: Reagents contain sodium azide. Sodium azide is very toxic if ingested or inhaled. Avoid contact with skin, eyes, or clothing. Wear eye or face protection when handling. If skin or eye contact occurs, wash with copious amounts of water. If ingested or inhaled, contact a physician immediately. Sodium azide yields toxic hydrazoic acid under acidic conditions. Dilute azide-containing compounds in running water before discarding to avoid accumulation of potentially explosive deposits in lead or copper plumbing.
Lagerung
4 °C,-20 °C
Burgon, Lee, Nixon, Peralta, Casey: "Phosphorylation and nuclear translocation of a regulator of G protein signaling (RGS10)." in: The Journal of biological chemistry, Vol. 276, Issue 35, pp. 32828-34, (2001) (PubMed).
Chatterjee, Fisher: "Cytoplasmic, nuclear, and golgi localization of RGS proteins. Evidence for N-terminal and RGS domain sequences as intracellular targeting motifs." in: The Journal of biological chemistry, Vol. 275, Issue 31, pp. 24013-21, (2000) (PubMed).
Hunt, Fields, Casey, Peralta: "RGS10 is a selective activator of G alpha i GTPase activity." in: Nature, Vol. 383, Issue 6596, pp. 175-7, (1996) (PubMed).
Target
RGS10
(Regulator of G-Protein Signaling 10 (RGS10))
MGC82511 antikoerper, RGS10 antikoerper, 2310010N19Rik antikoerper, regulator of G-protein signaling 10 antikoerper, regulator of G-protein signaling 10 L homeolog antikoerper, regulator of G protein signaling 10 antikoerper, regulator of G-protein signalling 10 antikoerper, RGS10 antikoerper, rgs10.L antikoerper, rgs10 antikoerper, Rgs10 antikoerper
Hintergrund
Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Associates specifically with the activated forms of the G protein subunits G(i)-alpha and G(z)- alpha but fails to interact with the structurally and functionally distinct G(s)-alpha subunit. Activity on G(z)-alpha is inhibited by palmitoylation of the G-protein.