ID1 Human

ID1 is composed of a basic helix-loop-helix (bHLH) domain, which is crucial for its interaction with other proteins. The protein’s primary function is to regulate cell growth, differentiation, and senescence. By inhibiting the DNA binding activity of other HLH proteins, ID1 plays a significant role in controlling gene expression and cellular processes .

ID1 has been implicated in various diseases, particularly in cancer and inflammatory conditions. For instance, in rheumatoid arthritis (RA), ID1 is produced by synovial fibroblasts and endothelial cells, contributing to the inflammatory environment. The protein is released from fibroblasts via exosomes and can activate signaling pathways that promote angiogenesis, vasculogenesis, and fibrosis . This makes ID1 a potential target for therapeutic interventions aimed at modulating these processes in diseases like RA .

Recombinant human ID1 is produced using techniques that involve the expression of the ID1 gene in bacterial systems such as E. coli. The recombinant protein is often tagged with a His-tag at the N-terminus to facilitate purification. The purified protein is used in various research applications to study its function and role in different cellular processes .

The recombinant human ID1 protein is typically stored in a buffer containing Tris-HCl, NaCl, glycerol, and DTT to maintain its stability. It is important to avoid freeze-thaw cycles to preserve the protein’s integrity .

Recombinant human ID1 is widely used in research to understand its role in cell growth, differentiation, and disease. It is utilized in various assays, including enzyme-linked immunosorbent assays (ELISA), Western blotting, and real-time polymerase chain reaction (RT-PCR), to study its expression and function in different cell types and conditions .