Overview
- Peptide (C)KTKVFSDIGAIQSLKR, corresponding to amino acid residues 361 - 376 of mouse SARM1 (Accession Q6PDS3). Intracellular (ARM 8 repeat).
SARM1 Blocking Peptide (#BLP-NR138)
- Western blot analysis of newborn rat brain lysates (lanes 1 and 3) and mouse brain lysates (lanes 2 and 4):1-2. Anti-SARM1 Antibody (#ANR-138), (1:200).
3-4. Anti-SARM1 Antibody, preincubated with SARM1 Blocking Peptide (#BLP-NR138). - Western blot analysis of human SHSY-5Y neuroblastoma cell line lysate (lanes 1 and 4), human ARPE-19 retinal epithelial cell line lysate (lanes 2 and 5) and human LNCaP prostate carcinoma cell line lysate (lanes 3 and 6):1-3. Anti-SARM1 Antibody (#ANR-138), (1:200).
4-6. Anti-SARM1 Antibody, preincubated with SARM1 Blocking Peptide (#BLP-NR138).
- Expression of SARM1 in rat hippocampusImmunohistochemical staining of perfusion-fixed frozen rat brain sections using Anti-SARM1 Antibody (#ANR-138), (1:300), followed by goat anti-rabbit-AlexaFluor-488. A. Staining in the rat hippocampal dentate gyrus region, showed immunoreactivity (green) in neuronal outlines (arrows). B. Pre-incubation of the antibody with SARM1 Blocking Peptide (#BLP-NR138), suppressed staining. Cell nuclei are stained with DAPI (blue). H = hilus, G = granule layer.
- Osterloh, J.M. et al. (2012) Science, 337, 481–484.
- Shi, Y. et al. (2022) Mol Cell, 82, 1643–1659.
- Gerdts, J. et al. (2015) Science, 348, 453–457.
- Essuman, K. et al. (2017) Science, 355, 602–606.
- Turkiew, E. et al. (2017) J Neurosci Res, 95, 1039–1052.
The sterile alpha and TIR motif-containing protein 1 (SARM1) belongs to the family of Toll/interleukin-1 receptor (TIR)-domain-containing proteins1. This protein is characterized by its multidomain structure, including N-terminal Armadillo repeats (ARM), tandem sterile alpha motif (SAM) domains, and a C-terminal catalytic TIR domain2. SARM1 is an intracellular protein predominantly localized in the axons of neurons. It plays a critical role in axonal self-destruction through its NAD+ glycohydrolase activity, which is initiated under pathological conditions such as axonal injury2,3.
SARM1 expression is prominent in neuronal populations, particularly within the central and peripheral nervous systems. It is upregulated under stress conditions, such as hypoxia and neuroinflammatory states3. The activation of SARM1 is regulated by nicotinamide mononucleotide (NMN), which disrupts the interaction between the ARM and TIR domains, leading to the formation of TIR-domain assemblies that execute NAD+ cleavage2,4.
Biologically, SARM1 is implicated in Wallerian degeneration, a process of axonal degeneration triggered by trauma or neuropathies. It also mediates axonal degeneration in metabolic and toxic neuropathies, such as those induced by high-fat diets or chemotherapy agents like paclitaxel3,5. In vitro studies have shown that genetic deletion of SARM1 protects neurons from degeneration by maintaining NAD+ levels. Similarly, in vivo studies reveal its role in preserving axonal integrity in models of traumatic, toxic, and metabolic insults3,5. Dysregulation of SARM1 activity is associated with various neurodegenerative conditions, including peripheral neuropathies, glaucoma, and traumatic brain injuries2,3.
Application key:
Species reactivity key:
Anti-SARM1 Antibody (#ANR-138) is a highly specific antibody directed against an epitope of the mouse protein. The antibody can be used in western blot and immunohistochemistry applications. It has been designed to recognize SARM1 from mouse, rat and human samples.