Recombinant Mouse Spermine Oxidase (SMOX) Protein (His-SUMO)

Name: Recombinant Mouse Spermine Oxidase (SMOX) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-08605P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Spermine Oxidase (SMOX) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q99K82
Target Symbol	SMOX
Synonyms	Smox; SmoSpermine oxidase; EC 1.5.3.16; Polyamine oxidase 1; PAO-1; PAOh1
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MQSCESSGDSADDPLSRGLRRRGQPRVVVIGAGLAGLAAARALLEQGFTDVTVLEASSHIGGRVQSVRLGDTTFELGATWIHGSHGNPIYQLAEANGLLEETTDGERSVGRISLYSKNGVACYLTNRGCRIPKDVVEEFSDLYNEVYNMTQEFFRHGKPVNAESQNSVGVFTREKVRNRIRDDPDDTEATKRLKLAMIQQYLKVESCESSSHSIDEVSLSAFGEWTEIPGAHHIIPSGFMRVVELLAEGIPPHVIQLGKPVRCIHWDQASAHPRGPEIEPRGEGDHNHDTGEGGQSGENPQQGRWDEDEPWPVVVECEDCEVIPADHVIVTVSLGVLKRQYTSFFRPCLPTEKVAAIHRLGIGTTDKIFLEFEEPFWGPECNSLQFVWEDEAESCTLTYPPELWYRKICGFDVLYPPERYGHVLSGWICGEEALVMERCDDEAVAEICTEMLRQFTGNPNIPKPRRILRSAWGSNPYFRGSYSYTQVGSSGADVEKLAKPLPYTESSKTAPMQVLFSGEATHRKYYSTTHGALLSGQREAARLIEMYRDLFQQGP
Expression Range	1-555aa
Protein Length	Full Length
Mol. Weight	77.9kDa
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	Flavoenzyme which catalyzes the oxidation of spermine to spermidine. Can also use N(1)-acetylspermine and spermidine as substrates, with different affinity depending on the isoform (isozyme) and on the experimental conditions. Plays an important role in the regulation of polyamine intracellular concentration and has the potential to act as a determinant of cellular sensitivity to the antitumor polyamine analogs. May contribute to beta-alanine production via aldehyde dehydrogenase conversion of 3-amino-propanal.
Subcellular Location	Cytoplasm.; [Isoform 2]: Cytoplasm. Nucleus.
Protein Families	Flavin monoamine oxidase family
Database References	KEGG: mmu:228608 UniGene: PMID: 23840306 Spermine oxidase is an important regulator of muscle gene expression and fiber size. PMID: 25406264 Data (including data from studies using recombinant mutant proteins) suggest that Glu216-Ser218 is a hot spot responsible for Smox substrate specificity; Smox with mutation E216L/S218A exhibits specificity for N'-acetylspermine rather than spermine. PMID: 24854736 ROS overexposure by mSMOX delivers an earlier adaptive response to radiation PMID: 23857253 Spermine oxidase mediates the gastric cancer risk associated with Helicobacter pylori CagA. PMID: 21839041 Spermine oxidase binds spermine in a similar conformation as that observed in the yeast polyamine oxidase FMS1-spermine complex and demonstrate a major role for residues His82 and Lys367 in substrate binding and catalysis. PMID: 20839014 expression and characterization of mouse spermine oxidase PMID: 12458219 we identified a second domain that is necessary for nuclear localization of the spermine oxidase splice variant PMID: 15955064

FAQs

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.