LD78-beta, also known as CCL3L1, is a member of the CC chemokine family. Chemokines are small cytokines or signaling proteins secreted by cells. The primary function of chemokines is to induce chemotaxis in nearby responsive cells, particularly immune cells. LD78-beta is closely related to macrophage inflammatory protein 1-alpha (MIP-1α) and plays a significant role in inflammatory and immunoregulatory processes .
The gene encoding LD78-beta is located on the q-arm of chromosome 17. This gene is part of a cluster of cytokine genes. The protein encoded by this gene binds to several chemokine receptors, including chemokine binding protein 2 and chemokine (C-C motif) receptor 5 (CCR5). The CCR5 receptor is notably a co-receptor for HIV, and binding of LD78-beta to CCR5 inhibits HIV entry .
Recombinant human LD78-beta is a 7.7 kDa protein containing 70 amino acid residues, including the four conserved cysteine residues present in CC chemokines. The protein is typically expressed in Escherichia coli (E. coli) and purified to a high degree of purity, often greater than 98% as determined by SDS-PAGE and HPLC analyses .
Recombinant LD78-beta is typically produced using bacterial expression systems, such as E. coli. The gene encoding LD78-beta is cloned into an expression vector, which is then introduced into E. coli cells. The bacteria are cultured, and the recombinant protein is expressed. Following expression, the protein is purified using techniques such as affinity chromatography, which exploits the His tag attached to the protein for purification .
LD78-beta is used in various research applications, including: