Recombinant Mouse NAD (SARM1) Protein (His)

Name: Recombinant Mouse NAD (SARM1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00159P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse NAD (SARM1) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Activity	Not tested.
Uniprotkb	Q6PDS3
Target Symbol	SARM1
Synonyms	(NADase SARM1)(Sterile alpha and TIR motif-containing protein 1)
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	C-6His
Target Protein Sequence	VASWKEAEVQTWLQQIGFSQYCENFREQQVDGDLLLRLTDEELQTDLGMKSSITRKRFFRELTELKTFASYATCDRSNLADWLGSLDPRFRQYTYGLVSCGLDRSLLHRVSEQQLLEDCGIRLGVHRTRILSAAREMLHSPLPCTGGKLSGDTPDVFISYRRNSGSQLASLLKVHLQLHGFSVFIDVEKLEAGKFEDKLIQSVIAARNFVLVLSAGALDKCMQDHDCKDWVHKEIVTALSCGKNIVPIIDGFEWPEPQALPEDMQAVLTFNGIKWSHEYQEATIEKIIRFLQGRPSQ
Expression Range	409-705aa
Protein Length	Partial
Mol. Weight	40.7 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	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.
Subcellular Location	Cytoplasm. Cell projection, axon. Cell projection, dendrite. Cell junction, synapse. Mitochondrion.
Database References	KEGG: mmu:237868 UniGene: PMID: 28978465 This study extends the role of Sarm1 to axon degeneration seen in peripheral neuropathies and identifies it as a likely target for therapeutic development. PMID: 28485482 SARM1 deletion restrains non-alcoholic fatty liver disease induced by high fat diet (HFD) in mice. PMID: 29454967 we identify a physical interaction between the autoinhibitory N terminus and the TIR domain of SARM1, revealing a previously unrecognized direct connection between these domains that we propose mediates autoinhibition and activation upon injury. PMID: 27671644 Using steady-state and flux analysis of NAD(+) metabolites in healthy and injured mouse dorsal root ganglion axons, we find that rather than altering NAD(+) synthesis, NMNAT1 instead blocks the injury-induced, SARM1-dependent NAD(+) consumption that is central to axon degeneration. PMID: 27735788 demonstrate that the NADase activity of full-length SARM1 is required in axons to promote axonal NAD+ depletion and axonal degeneration after injury. PMID: 28334607 Genetic deletion of SARM1 decreases axonal degeneration in a mouse model of neuropathy. PMID: 27797810 SARM is a potential regulator of sepsis-induced splenocyte apoptosis. PMID: 27590237 Sarm1(-/-)mice developed fewer Beta-amyloid precursor protein aggregates in axons of corpus callosum after traumatic brain injury. PMID: 26912636 SARM1-induced depletion of NAD(+) may explain the potent axon protection in Wallerian degeneration slow (Wld(s)) mutant mice. PMID: 25908823 The findings suggest that Sarm1 regulates social behaviors and cognition. PMID: 24321214 knock-outs display altered inflammatory cytokine expression pattern in the brain neurons PMID: 23751821 Therefore, Sarm1 functions downstream of ROS to induce neuronal cell death and axon degeneration during oxidative stress. PMID: 25009267 this study identifies a new role for SARM in CCL5 expression in macrophages. PMID: 24711619 Wild-type LPS is able to upregulate SARM and to prevent SIRPalpha downregulation. PMID: 23836818 These results indicate that SARM plays an integral role in the dismantling of injured axons PMID: 23946415 data demonstrate SARM plays a role in neurodegeneration during viral CNS infection; in addition, SARM plays a positive role in cytokine production; data suggest SARM is crucial for CNS injury and cytokine production in the CNS and may provide a link between neurodegeneration and the innate immune response PMID: 23749635 Results presented in this study, for the first time, show that KA-mediated upregulation of SARM1 protein promotes Wallerian-like degeneration of retinal ganglion cells and their axons. PMID: 23518770 severed mouse Sarm1 null axons exhibit long-term survival both in vivo and in vitro, indicating Sarm1 prodegenerative signaling is conserved in mammals; results provide direct evidence that axons actively promote their own destruction after injury and identify dSarm/Sarm1 as a member of an ancient axon death signaling pathway PMID: 22678360 The N-terminal 27 amino acids (S27) of SARM, which is hydrophobic and polybasic, acts as a mitochondria-targeting signal sequence, associating SARM to the mitochondria. The S27 peptide has an inherent ability to bind to lipids and mitochondria. PMID: 22145856 Burkholderia pseudomallei modulates macrophage defense mechanisms by upregulating SARM, thus leading to the suppression of IFN-beta and iNOS needed for bacterial elimination PMID: 21555400 Sarm1, a negative regulator of innate immunity, interacts with syndecan-2 and regulates neuronal morphogenesis. PMID: 21555464 SARM functions to restrict viral infection and neuronal injury in a brain region-specific manner, possibly by modulating the activation of resident CNS inflammatory cells. PMID: 19587044

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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