SPIN1 Human

Spindlin-1 is a full-length protein consisting of 262 amino acids and has a molecular weight of approximately 32 kDa . It is expressed in various tissues and is particularly noted for its high expression in several human cancers . The recombinant form of Spindlin-1 is typically expressed in Escherichia coli and purified to a high degree of purity (>90%) for research purposes .

Spindlin-1 functions as a chromatin reader, specifically recognizing and binding to histone H3 that is trimethylated at lysine 4 (H3K4me3) and asymmetrically dimethylated at arginine 8 (H3R8me2a) . This binding activity allows Spindlin-1 to play a crucial role in the regulation of gene expression. One of its significant roles is as an activator of the Wnt signaling pathway downstream of PRMT2 .

Spindlin-1 has been implicated in tumorigenesis and cancer progression. It is highly expressed in various cancers, including breast cancer, where it has been shown to enhance resistance to chemotherapy drugs like Adriamycin . The mechanism behind this involves the upregulation of drug-metabolizing enzymes and transporters, which are major determinants of chemoresistance in tumor cells . Additionally, Spindlin-1 is negatively regulated by the miR-148/152 family of microRNAs, which can decrease its expression and subsequently reduce drug resistance .

Recombinant Spindlin-1 is widely used in research to study its role in gene regulation and cancer biology. It is suitable for applications such as SDS-PAGE and mass spectrometry (MS) due to its high purity and stability . Researchers utilize recombinant Spindlin-1 to investigate its interactions with chromatin and its impact on gene expression and cellular processes.