Recombinant Human ASPHD1 protein

**Background of ASPH Recombinant Protein**

Aspartate β-hydroxylase (ASPH) is a transmembrane enzyme that catalyzes the post-translational hydroxylation of specific aspartyl and asparaginyl residues in epidermal growth factor-like domains (EGFDs) of proteins. Initially identified for its role in calcium-binding protein modifications, ASPH has gained significant attention due to its overexpression in various cancers, including hepatocellular carcinoma, breast cancer, and pancreatic cancer. This enzyme is implicated in promoting tumor progression, metastasis, and angiogenesis by activating signaling pathways such as Notch, Wnt/β-catenin, and PI3K/Akt, which are critical for cell proliferation, survival, and invasion.

Recombinant ASPH proteins are engineered to study its biochemical functions, structure, and therapeutic potential. Produced via heterologous expression systems (e.g., *E. coli*, mammalian cells), these proteins retain key domains, such as the catalytic β-hydroxylase domain, enabling researchers to investigate enzyme kinetics, substrate specificity, and inhibitor screening. Purification techniques like affinity chromatography ensure high-purity yields for functional assays.

ASPH is considered a promising therapeutic target, driving the development of small-molecule inhibitors, monoclonal antibodies, and immunotherapies. Recombinant ASPH also aids in diagnostic applications, as elevated ASPH levels correlate with poor prognosis in cancer patients. Structural studies using recombinant variants have elucidated mechanisms of substrate recognition and catalysis, guiding rational drug design.

In summary, ASPH recombinant proteins serve as vital tools for unraveling the enzyme’s oncogenic roles, validating therapeutic strategies, and advancing translational research in oncology and beyond.

ASPHD1 (Aspartate Beta-Hydroxylase Domain-Containing Protein 1) is a less-studied member of the α-ketoglutarate-dependent dioxygenase family, which is implicated in post-translational modifications and epigenetic regulation. The protein contains a conserved aspartyl β-hydroxylase domain, structurally similar to enzymes that catalyze hydroxylation reactions, though its precise biochemical activity remains under investigation. ASPHD1 is encoded by the ASPHD1 gene located on human chromosome 16 and is expressed in various tissues, with notable presence in the brain, liver, and reproductive organs. Emerging evidence links ASPHD1 to cellular processes such as differentiation, apoptosis, and chromatin remodeling, potentially through interactions with histone-modifying complexes or hydroxylation of specific substrates.

Recombinant ASPHD1 protein is engineered for in vitro studies to elucidate its molecular functions. It is typically produced using heterologous expression systems like Escherichia coli or mammalian cell lines, followed by affinity chromatography purification (e.g., His-tag or GST-tag systems). The recombinant protein enables researchers to analyze enzymatic activity, substrate specificity, and structural features via techniques like crystallography or enzyme kinetics assays. Notably, ASPHD1 has been associated with human diseases, including neurodevelopmental disorders and cancers. For example, aberrant ASPHD1 expression is observed in glioblastoma and hepatocellular carcinoma, suggesting a role in tumor progression. In neurodegenerative contexts, it may influence pathways related to Alzheimer’s disease, though mechanistic insights are limited.

Current research leverages recombinant ASPHD1 to develop targeted inhibitors or probes, aiming to dissect its physiological relevance and therapeutic potential. Challenges include clarifying its endogenous substrates and reconciling conflicting data about its hydroxylation targets versus non-enzymatic roles. Overall, ASPHD1 recombinant protein serves as a critical tool for bridging gaps in understanding its contribution to epigenetics and disease.