AIP Human
AH receptor-interacting protein, AIP, Aryl-hydrocarbon receptor-interacting protein, HBV X-associated protein 2, XAP-2, Immunophilin homolog ARA9, XAP2, ARA9, FKBP16, FKBP37, SMTPHN.
Description
AIP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (1-330 a.a.) and having a molecular mass of 39.8kDa.
AIP is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
AH receptor-interacting protein, AIP, Aryl-hydrocarbon receptor-interacting protein, HBV X-associated protein 2, XAP-2, Immunophilin homolog ARA9, XAP2, ARA9, FKBP16, FKBP37, SMTPHN.
MGSSHHHHHH SSGLVPRGSH MADIIARLRE DGIQKRVIQE GRGELPDFQD GTKATFHYRT LHSDDEGTVL DDSRARGKPM ELIIGKKFKL PVWETIVCTM REGEIAQFLC DIKHVVLYPL VAKSLRNIAV GKDPLEGQRH CCGVAQMREH SSLGHADLDA LQQNPQPLIF HMEMLKVESP
GTYQQDPWAM TDEEKAKAVP LIHQEGNRLY REGHVKEAAA KYYDAIACLK NLQMKEQPGS PEWIQLDKQI TPLLLNYCQC KLVVEEYYEV LDHCSSILNK YDDNVKAYFK RGKAHAAVWN AQEAQADFAK VLELDPALAP VVSRELRALE ARIRQKDEED KARFRGIFSH.
Product Science Overview
Aryl Hydrocarbon Receptor Interacting Protein (AIP) is a crucial molecular chaperone that plays a significant role in the regulation of the Aryl Hydrocarbon Receptor (AhR) signaling pathway. This pathway is involved in various biological processes, including xenobiotic metabolism, immune response, and cell proliferation. AIP is particularly important in maintaining the stability and proper functioning of AhR, which is a ligand-activated transcription factor.
AIP is a protein composed of 330 amino acids and is encoded by the AIP gene located on chromosome 11q13.3. The protein contains several functional domains, including a tetratricopeptide repeat (TPR) domain, which is essential for protein-protein interactions. The TPR domain allows AIP to interact with various client proteins, including AhR, heat shock proteins (HSP90), and other co-chaperones.
The primary function of AIP is to facilitate the proper folding and stabilization of AhR. In the absence of a ligand, AhR resides in the cytoplasm in a complex with AIP, HSP90, and other co-chaperones. Upon ligand binding, AhR undergoes a conformational change, dissociates from the complex, and translocates to the nucleus, where it dimerizes with the Aryl Hydrocarbon Receptor Nuclear Translocator (ARNT). This complex then binds to xenobiotic response elements (XREs) in the DNA, leading to the transcription of target genes involved in xenobiotic metabolism and other cellular processes .
AIP has been implicated in various physiological and pathological processes. It plays a critical role in the immune system by modulating the activity of AhR, which influences the differentiation and function of immune cells. Additionally, AIP is involved in the regulation of cell proliferation and apoptosis, making it a key player in cancer biology.
Recent studies have shown that AIP is overexpressed in certain types of cancer, such as colorectal cancer, and is associated with poor prognosis. AIP overexpression has been linked to increased tumorigenic and metastatic properties, particularly in highly metastatic colorectal cancer cells. This suggests that AIP may serve as a potential therapeutic target for cancer treatment .
Recombinant AIP is produced using recombinant DNA technology, which involves the insertion of the AIP gene into an expression vector, followed by the expression of the protein in a suitable host system, such as Escherichia coli or mammalian cells. The recombinant protein is then purified using various chromatographic techniques to obtain a highly pure and biologically active form of AIP.
Recombinant AIP is widely used in research to study the molecular mechanisms of AhR signaling and its role in various biological processes. It is also used in drug discovery and development to screen for potential modulators of the AhR pathway.
