Datasheet

生物学的記述

Specificity	RALA Antibody [G17M6] detects endogenous levels of total RALA protein.
Background	RalA is a Ras‑related small GTPase that cycles between GDP‑ and GTP‑bound states and functions as a membrane‑associated molecular switch downstream of Ras and RalGEFs to control exocyst‑dependent vesicle trafficking, cytokinesis, and oncogenic signaling programs that support proliferation, survival, and metastasis in multiple tumor types. The protein shares the conserved GTP‑binding P‑loop, switch I/II regions, and C‑terminal hypervariable tail with lipidation motifs typical of Ras‑superfamily members, which anchor RalA to specific membrane microdomains and allow GTP‑dependent engagement of effectors such as the exocyst components Sec5 and Exo84, RalBP1/RLIP76, and phospholipase D1, thereby coupling nucleotide state to exocytosis, endocytosis, and actin cytoskeletal regulation. In the canonical Ras pathway, active Ras binds and activates RalGEFs (RalGDS, RGL1–3), which in turn load GTP onto RalA; expression of constitutively active RalA enhances the transforming activity of oncogenic Ras and Raf, while dominant‑negative RalA suppresses Ras‑ and Raf‑driven transformation, demonstrating that a Ras–RalGEF–RalA branch operates in parallel to Raf–MEK–ERK to potentiate oncogenic output. RalA activation promotes exocyst assembly at the plasma membrane and centrosomes, regulates polarized delivery of cargo vesicles, and contributes to successful completion of cytokinesis, and RalA‑dependent exocyst signaling also influences receptor recycling and integrin trafficking, providing a mechanistic route by which RalA can control adhesion, migration, and invasion. Genetic and functional studies in human cancer models show that RalA is required for Ras‑induced tumorigenesis: knockdown or inhibition of RalA in Ras‑mutant cancer cells impairs anchorage‑independent growth, tumor formation, and maintenance of established xenografts, whereas loss of RalB has distinct, more prominent effects on survival and autophagy, highlighting isoform‑specific contributions to the oncogenic Ras network. In triple‑negative breast cancer, elevated RalA activity correlates with aggressive clinical behavior, and experimental silencing of RalA reduces primary tumor growth, limits metastatic colonization, and diminishes cancer stem–like cell properties, positioning RalA as a critical driver of progression and metastasis in this subtype and an attractive target for isoform‑selective inhibition.

Specificity

RALA Antibody [G17M6] detects endogenous levels of total RALA protein.

Background

RalA is a Ras‑related small GTPase that cycles between GDP‑ and GTP‑bound states and functions as a membrane‑associated molecular switch downstream of Ras and RalGEFs to control exocyst‑dependent vesicle trafficking, cytokinesis, and oncogenic signaling programs that support proliferation, survival, and metastasis in multiple tumor types. The protein shares the conserved GTP‑binding P‑loop, switch I/II regions, and C‑terminal hypervariable tail with lipidation motifs typical of Ras‑superfamily members, which anchor RalA to specific membrane microdomains and allow GTP‑dependent engagement of effectors such as the exocyst components Sec5 and Exo84, RalBP1/RLIP76, and phospholipase D1, thereby coupling nucleotide state to exocytosis, endocytosis, and actin cytoskeletal regulation. In the canonical Ras pathway, active Ras binds and activates RalGEFs (RalGDS, RGL1–3), which in turn load GTP onto RalA; expression of constitutively active RalA enhances the transforming activity of oncogenic Ras and Raf, while dominant‑negative RalA suppresses Ras‑ and Raf‑driven transformation, demonstrating that a Ras–RalGEF–RalA branch operates in parallel to Raf–MEK–ERK to potentiate oncogenic output. RalA activation promotes exocyst assembly at the plasma membrane and centrosomes, regulates polarized delivery of cargo vesicles, and contributes to successful completion of cytokinesis, and RalA‑dependent exocyst signaling also influences receptor recycling and integrin trafficking, providing a mechanistic route by which RalA can control adhesion, migration, and invasion. Genetic and functional studies in human cancer models show that RalA is required for Ras‑induced tumorigenesis: knockdown or inhibition of RalA in Ras‑mutant cancer cells impairs anchorage‑independent growth, tumor formation, and maintenance of established xenografts, whereas loss of RalB has distinct, more prominent effects on survival and autophagy, highlighting isoform‑specific contributions to the oncogenic Ras network. In triple‑negative breast cancer, elevated RalA activity correlates with aggressive clinical behavior, and experimental silencing of RalA reduces primary tumor growth, limits metastatic colonization, and diminishes cancer stem–like cell properties, positioning RalA as a critical driver of progression and metastasis in this subtype and an attractive target for isoform‑selective inhibition.

使用情報

Application

WB

Dilution

WB

1:1000

Reactivity

Human, Mouse, Rat, Monkey

Source

Rabbit Monoclonal Antibody

MW

24 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

プロトコール

References

https://pubmed.ncbi.nlm.nih.gov/25219551/
https://pubmed.ncbi.nlm.nih.gov/15950903/

RALA Antibody [G17M6]

生物学的記述

使用情報

References

Application Data