Ras-related protein Ral-A, Rala, Ral, Ral-a, RALA.
Greater than 90.0% as determined by SDS-PAGE.
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RALA Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (1-203 a.a) and having a molecular mass of 25.7kDa. RALA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Ras-related protein Ral-A, Rala, Ral, Ral-a, RALA.
MGSSHHHHHH SSGLVPRGSH MGSHMAANKP KGQNSLALHK VIMVGSGGVG KSALTLQFMY DEFVEDYEPT KADSYRKKVV LDGEEVQIDI LDTAGQEDYA AIRDNYFRSG EGFLCVFSIT EMESFAATAD FREQILRVKE DENVPFLLVG NKSDLEDKRQ VSVEEAKNRA DQWNVNYVET SAKTRANVDK VFFDLMREIR ARKMEDSKEK NGKKKRKSLA KRIRERC
The V-ral simian leukemia viral oncogene homolog A, commonly referred to as RALA, is a gene that encodes a protein belonging to the Ras superfamily of small GTPases. This protein is involved in various cellular processes, including cell proliferation, differentiation, and vesicle trafficking. The mouse recombinant version of this protein is often used in research to study its functions and implications in different biological contexts.
The RALA gene is located on chromosome 7 in humans and has a significant degree of homology with other members of the Ras family. The protein encoded by RALA shares about 50% homology with Ras proteins and is composed of 206 amino acids . The RALA protein has a high degree of identity with another protein, RALB, sharing about 85% identity .
RALA plays a crucial role in several cellular functions. One of its primary roles is in the regulation of exocyst-dependent trafficking. The exocyst is an evolutionarily conserved octameric complex involved in the post-Golgi targeting of secretory vesicles. RALA, along with RALB, regulates the assembly of the exocyst complex through interactions with specific components such as EXO84 and SEC5 .
Additionally, RALA is involved in the equal distribution of mitochondria to daughter cells during mitosis. This process requires the recruitment of the large GTPase DRP1 to the outer mitochondrial membrane and the phosphorylation of DRP1 by cyclin B-CDK1 .
RALA has been implicated in cancer biology. Suppression of PP2A A-beta expression, a tumor suppressor, allows immortalized human cell lines to achieve a tumorigenic state. Cancer-associated A-beta mutants fail to form a complex with RALA, leading to the inactivation of RALA’s transforming function . This indicates that RALA plays a role in the regulation of tumorigenesis.
The mouse recombinant version of RALA is widely used in research to study its functions and interactions. By using recombinant proteins, researchers can investigate the specific roles of RALA in various cellular processes and its implications in diseases such as cancer.