Recombinant Human LDAH Protein: Properties & Research Use
Recombinant Human LDAH Protein: Properties & Research Use
Recombinant Human LDAH Protein is a recombinantly expressed form of lipid droplet-associated hydrolase, a serine hydrolase implicated in intracellular lipid droplet homeostasis and neutral lipid metabolism, produced for use as a research reagent in biochemical and cell biology applications.
- Protein Name
- Lipid Droplet-Associated Hydrolase (LDAH)
- Protein Type
- Recombinant human serine hydrolase
- Primary Function
- Hydrolysis of neutral lipids associated with lipid droplets
- Subcellular Localization
- Lipid droplet surface
- Research Relevance
- Lipid metabolism, lipid droplet biology, metabolic disease
- Product SKU
- rp372990
What Is LDAH? Gene and Protein Background
Lipid Droplet-Associated Hydrolase (LDAH), also referred to in the literature by its gene designation, is a member of the serine hydrolase superfamily. It localizes to the surface of intracellular lipid droplets (LDs), organelles that serve as the primary storage depots for neutral lipids such as triacylglycerols and cholesterol esters.
LDAH has been identified as a hydrolase capable of acting on lipid substrates at the lipid droplet interface. Its enzymatic activity and LD localization position it as a potentially important regulator of intracellular lipid homeostasis. Dysregulation of lipid droplet biology is associated with metabolic disorders including obesity, non-alcoholic fatty liver disease (NAFLD), and atherosclerosis, making LDAH a protein of significant research interest.
Biochemical Properties of Recombinant Human LDAH Protein
Recombinant Human LDAH Protein is produced using recombinant expression systems to yield a well-characterized, research-grade reagent. As a serine hydrolase, LDAH contains a catalytic serine residue essential for its hydrolytic activity. The recombinant protein is designed to faithfully recapitulate the biochemical properties of the native human LDAH protein.
Key biochemical attributes include its classification as a serine hydrolase, its association with hydrophobic lipid droplet surfaces via specific structural domains, and its enzymatic capacity to hydrolyze neutral lipid substrates. Researchers should consult the product datasheet (absea#PP-6936) for confirmed specifications such as molecular weight, purity, formulation buffer, and storage conditions relevant to their experimental design.
Research Applications
Recombinant Human LDAH Protein supports a broad range of research applications in lipid biology and metabolic science:
- Enzyme Activity Assays: Characterizing the substrate specificity and kinetic parameters of LDAH hydrolase activity using defined lipid substrates.
- Protein–Protein Interaction Studies: Identifying binding partners at the lipid droplet surface that regulate LDAH function or recruitment.
- Structural Biology: Providing purified protein material for crystallography or cryo-EM studies aimed at resolving the three-dimensional structure of LDAH.
- Antibody Validation: Serving as a positive control antigen for validating LDAH-specific antibodies in Western blotting, ELISA, or immunofluorescence.
- Drug Discovery: Supporting inhibitor screening campaigns targeting LDAH activity in the context of metabolic disease research.
These applications position Recombinant Human LDAH Protein as a versatile reagent for researchers investigating lipid droplet biology, neutral lipid metabolism, and related metabolic pathways.
Handling, Storage, and Quality Considerations
To maintain the integrity and activity of Recombinant Human LDAH Protein, researchers should adhere to recommended handling and storage guidelines provided in the product datasheet. General best practices for recombinant proteins apply:
- Avoid repeated freeze–thaw cycles; aliquot the protein upon first thaw to preserve activity.
- Store at the temperature specified on the datasheet, typically –20 °C or –80 °C for long-term storage.
- Centrifuge the vial briefly before opening to consolidate contents.
- Use appropriate protein stabilizers or carrier proteins (e.g., BSA) if working at low concentrations.
Purity, formulation, endotoxin levels, and biological activity data specific to lot rp372990 should be verified against the certificate of analysis (CoA) provided with the product. Contact Aladdin Scientific technical support for application-specific guidance or custom requirements.
Frequently asked questions
What is LDAH and why is it a research target?
LDAH (Lipid Droplet-Associated Hydrolase) is a serine hydrolase that localizes to the surface of intracellular lipid droplets and acts on neutral lipid substrates. It is of research interest because lipid droplet dysregulation is linked to metabolic diseases such as obesity, NAFLD, and atherosclerosis, making LDAH a candidate target for understanding and potentially modulating lipid storage.
What applications is Recombinant Human LDAH Protein suitable for?
Recombinant Human LDAH Protein (SKU: rp372990) is suitable for enzyme activity assays, protein–protein interaction studies, structural biology research, antibody validation, and inhibitor screening in drug discovery programs focused on lipid metabolism and metabolic disease.
How should Recombinant Human LDAH Protein be stored to maintain activity?
The protein should be stored at the temperature specified in the product datasheet (typically –20 °C or –80 °C). Repeated freeze–thaw cycles should be avoided; aliquoting upon first thaw is strongly recommended. Always refer to the certificate of analysis for lot-specific storage and formulation details.
Where can I find purity and activity specifications for this product?
Purity, biological activity, endotoxin levels, and formulation details are provided in the certificate of analysis (CoA) accompanying each lot of rp372990. The product datasheet (reference absea#PP-6936) also contains key specifications. Contact Aladdin Scientific support if you require additional technical information.
References
- Serrano-Gomez SJ et al. Lipid droplet-associated hydrolase (LDAH): emerging roles in lipid homeostasis. [Review — details to be verified]
- Thul PJ et al. A subcellular map of the human proteome. Science. 2017;356(6340):eaal3321. doi:10.1126/science.aal3321
- Olzmann JA, Carvalho P. Dynamics and functions of lipid droplets. Nat Rev Mol Cell Biol. 2019;20(3):137–155. doi:10.1038/s41580-018-0085-z
Products are supplied for research and development use only. Not for use in humans, animals, diagnosis, or therapy.
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