MKHHHHHHAS VAVDPQPSVV TRVVNLPLVS STYDLMSSAY LSTKDQYPYL KSVCEMAENG VKTITSVAMT SALPIIQKLE PQIAVANTYA CKGLDRIEER LPILNQPSTQ IVANAKGAVT GAKDAVTTTV TGAKDSVAST ITGVMDKTKG AVTGSVEKTK SVVSGSINTV LGSRMMQLVS SGVENALTKS ELLVEQYLPL TEEELEKEAK KVEGFDLVQK PSYYVRLGSL STKLHSRAYQ QALSRVKEAK QKSQQTISQL HSTVHLIEFA RKNVYSANQK IQDAQDKLYL SWVEWKRSIG YDDTDESHCA EHIESRTLAI ARNLTQQLQT TCHTLLSNIQ GVPQNIQDQA KHMGVMAGDI YSVFRNAASF KEVSDSLLTS SKGQLQKMKE SLDDVMDYLV NNTPLNWLVG PFYPQLTESQ NAQDQGAEMD KSSQETQRSEHKTH.
ADRP is a non-glycosylated polypeptide chain consisting of 444 amino acids, with a molecular mass of approximately 49 kDa . The protein contains an extra 8 amino acid His tag at the N-terminus when produced recombinantly in E. coli . The amino acid sequence of ADRP is identical to the UniProtKB/Swiss-Prot entry Q99541 amino acids 4–437 .
ADRP is primarily associated with lipid droplets in various cell types, including adipocytes, hepatocytes, and macrophages. It plays a significant role in the formation and stabilization of lipid droplets, which are essential for lipid storage and metabolism. The expression of ADRP is upregulated during adipocyte differentiation, making it a marker for this process .
In addition to its role in lipid storage, ADRP is involved in several physiological and pathological processes:
The expression of ADRP is regulated by several factors, including hormonal signals and transcription factors. For instance, peroxisome proliferator-activated receptor gamma (PPARγ) and CCAAT/enhancer-binding protein alpha (C/EBPα) are key transcription factors that upregulate ADRP expression during adipogenesis .
Human recombinant ADRP is produced in E. coli and purified using proprietary chromatographic techniques. The recombinant protein is typically lyophilized from a solution containing 20mM Tris pH-7.5 and 20mM NaCl . It is available in various quantities for research purposes and is used to study lipid metabolism, adipocyte differentiation, and related biological processes.