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SARM Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IF, ICC, E |
|---|---|
| Primary Accession | Q6SZW1 |
| Other Accession | NP_055892, 23098 |
| Reactivity | Human, Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | IgG |
| Calculated MW | Predicted: 80 kDa Observed: 85 kDa |
| Application Notes | SARM antibody can be used for detection of SARM by Western blot at 0.5 to 1 μg/mL. Antibody can also be used for immunocytochemistry starting at 2 μg/mL. For immunofluorescence start at 2 μg/mL. |
| Gene ID | 23098 |
|---|---|
| Other Names | SARM Antibody: SARM, SAMD2, MyD88-5, KIAA0524, SARM, Sterile alpha and TIR motif-containing protein 1, Sterile alpha and Armadillo repeat protein, sterile alpha and TIR motif containing 1 |
| Target/Specificity | SARM antibody was raised against a peptide corresponding to 14 amino acids near the C-terminus of human SARM. The immunogen is located within amino acids 640 - 690 of SARM. |
| Reconstitution & Storage | SARM antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures. |
| Precautions | SARM Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | SARM1 |
|---|---|
| Function | NAD(+) hydrolase, which plays a key role in axonal degeneration following injury by regulating NAD(+) metabolism (PubMed:25908823, PubMed:27671644, PubMed:28334607). 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 (PubMed:15123841, PubMed:16964262, PubMed:20306472, PubMed:25908823). 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 (PubMed:25908823, PubMed:28334607, PubMed:30333228, PubMed:31128467, PubMed:31439792, PubMed:31439793, PubMed:32049506, PubMed:32828421, PubMed:33053563). Also able to hydrolyze NADP(+), but not other NAD(+)-related molecules (PubMed:29395922). Can activate neuronal cell death in response to stress (PubMed:20306472). Regulates dendritic arborization through the MAPK4-JNK pathway (By similarity). 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 (PubMed:16964262). |
| Cellular Location | Cytoplasm. Cell projection, axon {ECO:0000250|UniProtKB:Q6PDS3}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q6PDS3}. Synapse {ECO:0000250|UniProtKB:Q6PDS3}. Mitochondrion Note=Associated with microtubules. {ECO:0000250|UniProtKB:Q6PDS3} |
| Tissue Location | Predominantly expressed in brain, kidney and liver. Expressed at lower level in placenta. |
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Provided below are standard protocols that you may find useful for product applications.
Background
SARM Antibody: Toll-like receptors (TLRs) are signaling molecules that recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses. SARM (SAM and ARM-containing protein), along with other molecules such as TIRP, TRIF, TIRAP, and MyD88, is thought to serve as an adaptor protein for the TLRs that allows for the activation of downstream kinases and NF-κB, and ultimately the expression of proteins involved in host defense. While SARM has not been conclusively shown to associate directly with TLRs, the presence of a Toll-interluekin-1 (TIR) domain in SARM is consistent with a role as a signaling molecule.
References
Vogel SN, Fitzgerald KA, and Fenton MJ. TLRs: differential adapter utilization by toll-like receptors mediates TLR-specific patterns of gene expression. Mol. Interv. 2003; 3:466-77.
Takeda K, Kaisho T, and Akira S. Toll-like receptors. Annu. Rev. Immunol. 2003; 21:335-76.
Janeway CA Jr and Medzhitov R. Innate immune recognition. Annu. Rev. Immunol. 2002; 20:197-216.
O’Neill LAJ, Fitzgerald FA, and Bowie AG. The Toll-IL-1 receptor adaptor family grows to five members. Trends in Imm. 2003; 24:286-9.
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