Recombinant Human NAD (+) hydrolase SARM1 (SARM1), partial

Overview

Recombinant Human NAD (+) hydrolase SARM1 (SARM1), partial is a recombinant protein reagent derived from Homo sapiens (Human) and produced in E.coli. It is commonly used to support Cell Biology research by enabling binding assays, assay development and protein–protein interaction studies in controlled in vitro settings.

Key elements and design rationale

• Expressed region: 409-702aa. Region selection can focus on functional domains, improve solubility, or isolate interaction surfaces for targeted studies.
• Expression system: E.coli. Expression host can influence folding and the presence/absence of post-translational modifications.
• Tag / fusion: N-terminal 6xHis-KSI-tagged. Tags can support purification and detection; evaluate potential tag effects when studying sensitive interactions.
• Molecular weight (reported): 48.8 kDa. Apparent size may vary with tags, processing, and gel conditions.

When comparing results across batches or platforms, interpret signals in the context of construct design (region, tags) and expression host, especially for modification-dependent interactions.

Biological background

The gene commonly associated with this target is SARM1. SARM1 refers to a protein target that is studied across multiple biological contexts; annotations and nomenclature can vary by species and isoform. This product corresponds to the Homo sapiens (Human) sequence context, which can be important when comparing homologs or orthologs across model systems. For curated functional annotations, domains, and sequence features, consult primary databases (e.g., UniProt/NCBI) and the recent literature for the specific organism and isoform.

Research relevance and current trends

• Using recombinant proteins to enable quantitative binding measurements and reagent benchmarking.
• Studying domain- and isoform-specific effects in pathway models and interaction networks.
• Developing robust, reproducible assays that connect molecular readouts to cellular phenotypes.

Relevance: NAD(+) hydrolase, which plays a key role in axonal degeneration following injury by regulating NAD(+) metabolism . Acts as a negative regulator of MYD88- and TRIF-dependent toll-like receptor signaling pathway by promoting Wallerian degeneration, an injury-induced form of programmed subcellular death which involves degeneration of an axon distal to the injury site . Wallerian degeneration is triggered by NAD(+) depletion: in response to injury, SARM1 is activated and catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR), cyclic ADPR (cADPR) and nicotinamide; NAD(+) cleavage promoting cytoskeletal degradation and axon destruction . Also able to hydrolyze NADP(+), but not other NAD(+)-related molecules . Can activate neuronal cell death in response to stress . Regulates dendritic arborization through the MAPK4-JNK pathway. Involved in innate immune response: inhibits both TICAM1/TRIF- and MYD88-dependent activation of JUN/AP-1, TRIF-dependent activation of NF-kappa-B and IRF3, and the phosphorylation of MAPK14/p38 .

Common research applications

• Assay and standard development for immunoassays or binding-based detection methods.
• Protein–protein interaction studies (e.g., receptor–ligand or complex assembly) using purified components.
• Structure–function analysis, including domain mapping or evaluation of sequence variants.

In quantitative assay development, changes in binding or activity readouts are typically interpreted relative to appropriate negative/positive controls and, where possible, orthogonal assay formats that support the same conclusion.

Notes for experimental interpretation

• Recombinant constructs may represent a defined region (domain) rather than the full-length protein; interpret results in the context of the expressed region.
• Tag or fusion elements can aid purification and detection but may influence binding surfaces or oligomerization; consider tag controls when relevant.
• Species and isoform differences can affect interaction partners and post-translational modifications; align experimental controls to the intended biological context.
• E. coli expression can limit eukaryotic post-translational modifications; for modification-dependent biology, interpret results accordingly.

• Datasheet (12932361)
• MSDS (12932361)

Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.