Ral GPS Anticuerpos

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Vea tambiénRal GPS Antibodies incluyendo, Ral GPS1, Ral GPS2

NOMBRE DEL PRODUCTO	NÚMERO DEL CATÁLOGO:	ISOTIPO	EPíTOPO	APLICACIONES	ESPECIES
Ral GPS1 (D-16)	sc-162074	cabra IgG	Internal (h)	WB, IF, ELISA	m, r, h, e, c, b, p, a
Ral GPS1 (N-15)	sc-162075	cabra IgG	N-terminal (h)	WB, IF, ELISA	m, r, h, e, c, b, p
Ral GPS2 (FE-63)	sc-81899	ratón IgG_2a	FL (h)	WB, IP, IF, ELISA	humano

Ral GPS silenciadores génicos siARN, Plásmidos de shARN y Partículas Lentivirales shRNA incluyendo:

siRNAs	Plásmidos shRNA	shRNA partículas antivirales
Ral GPS1 siRNA (h): sc-92962	Ral GPS1 shRNA Plasmid (h): sc-92962-SH	Ral GPS1 shRNA (h) Partículas Lentiviral :sc-92962-V
Ral GPS1 siRNA (m): sc-152689	Ral GPS1 shRNA Plasmid (m): sc-152689-SH	Ral GPS1 shRNA (m) Partículas Lentiviral :sc-152689-V
Ral GPS2 siRNA (h): sc-88634	Ral GPS2 shRNA Plasmid (h): sc-88634-SH	Ral GPS2 shRNA (h) Partículas Lentiviral :sc-88634-V
Ral GPS2 siRNA (m): sc-152690	Ral GPS2 shRNA Plasmid (m): sc-152690-SH	Ral GPS2 shRNA (m) Partículas Lentiviral :sc-152690-V

Ral GPS1 (Ral GEF with PH domain and SH3-binding motif 1), also known as RalGEF 2 (Ral guanine nucleotide exchange factor 2), is a 557 amino acid guanine nucleotide exchange factor for Ral A. Localized to cytoplasm, Ral GPS1 contains one PH domain, which associates with the cell membrane, and one Ras-GEF domain. Ral GPS1 may play a role in cytoskeletal organization as well as the stimulation of transcription in a Ras-independent manner. Ral GPS1 has been found to interact with the SH3 domains of SRC-1, NCK1, PLC γ1 and GRB2. Ral GPS2 (Ral GEF with PH domain and SH3 binding motif 2) is a 583 amino acid member of the Ral GPS family and functions as a guanine nucleotide-exchange factor (GEF) for the small GTPase Ral A. Members of the Ral GPS family of GEFs are distinct from other Ral GEFs in that they lack the Ras-GTP-binding domain and are therefore activated in a Ras-independent manner. Expressed in testis and brain, Ral GPS2 localizes to the cytoplasm and contains one Ras-GEF domain and one PH domain.