GDF15 Human, His

GDF15 is encoded by the GDF15 gene located on chromosome 19 in humans . The protein is initially synthesized as a precursor molecule that undergoes proteolytic cleavage to produce the mature, active form. The mature form of human GDF15 consists of 122 amino acids and has a predicted molecular mass of approximately 13.7 kDa . Due to glycosylation, it migrates as an approximately 18.2 kDa band in SDS-PAGE under reducing conditions .

Under normal physiological conditions, GDF15 is expressed at low levels in most tissues. However, its expression is significantly upregulated in response to tissue injury and inflammation . This upregulation is particularly notable in organs such as the liver, kidney, heart, and lung . GDF15 acts as an autocrine regulator of macrophage activation and is a downstream target of the tumor suppressor protein p53, which is involved in the cellular response to DNA damage .

The precise biological functions of GDF15 are not fully understood, but it is known to play a role in several critical processes:

• Regulation of Inflammatory Pathways: GDF15 is involved in modulating inflammatory responses, which is crucial for maintaining tissue homeostasis during injury and disease .
• Apoptosis and Cell Survival: GDF15 can promote either cell proliferation or growth arrest and differentiation, depending on the cellular context . It prevents apoptosis in cerebellar granule neurons by activating the Akt pathway and inhibiting the endogenously active ERK pathway .
• Angiogenesis and Cell Repair: GDF15 is implicated in angiogenesis (the formation of new blood vessels) and cell repair mechanisms, which are essential for tissue regeneration and recovery following injury .

Recombinant GDF15 is produced using recombinant DNA technology, where the GDF15 gene is cloned into an expression vector and introduced into a host cell system, such as Escherichia coli (E. coli) or mammalian cells. The recombinant protein is then purified and tagged with a His (histidine) tag to facilitate purification and detection .

The His tag is a short sequence of histidine residues that binds strongly to nickel ions, allowing for efficient purification of the recombinant protein using nickel-affinity chromatography. This method ensures high purity and activity of the recombinant GDF15 protein .

Recombinant GDF15 (Human, His Tag) is widely used in research to study its biological functions and potential therapeutic applications. It is particularly valuable in investigating its role in inflammatory diseases, cancer, and cardiovascular disorders. Additionally, GDF15 is being explored as a potential biomarker for various pathological conditions due to its upregulation in response to tissue injury and disease .