MCL1 exists in multiple isoforms due to alternative splicing. The two main isoforms are:
The recombinant human MCL1 protein is typically produced in E. coli and consists of a single polypeptide chain containing 347 amino acids, with a molecular mass of approximately 37.2 kDa. It is often fused to a 20 amino acid His-tag at the N-terminus for purification purposes .
MCL1 is involved in the regulation of apoptosis versus cell survival and in the maintenance of cell viability. It mediates its effects through interactions with other regulators of apoptosis. The balance between the pro-survival and pro-apoptotic isoforms of MCL1 is critical for determining cell fate. Isoform 1 (MCL1L) inhibits apoptosis, while Isoform 2 (MCL1S) promotes apoptosis .
MCL1 is associated with various diseases, including myeloid leukemia and other hematologic cancers. Its role in inhibiting apoptosis makes it a target for cancer therapy, as cancer cells often exploit anti-apoptotic proteins to evade cell death. Therapeutic strategies aimed at inhibiting MCL1 function are being explored to induce apoptosis in cancer cells .
Recombinant human MCL1 is used in various research applications, including: