Recombinant Mouse Reticulon-3 (RTN3) Protein (His)

Name: Recombinant Mouse Reticulon-3 (RTN3) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06939P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant Mouse Reticulon-3 (RTN3) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q9ES97
Target Symbol	RTN3
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	KDQEPKNPNKVPDGEDRSALDFGQSKAEHICTYSLSPSELPVASVEKDSPESPFEVIIDKATFDREFKDLYKENPNDLGGWAAHGDRESPADLLEMNDKLFPLRNKEAGRYPSSVLLGRQFSHTTAALEEVSRCVNDMHNFTNEILTWDLDPQAKQQANKTSCTTESTGLDRSELRSEIPVINLKTNPQQKMPVCSFNGSTPITKSTGDWTEAFTEGKPVRDYLSSTKEAGGNGVPGSSQLHSELPGSMPEKWVSGSGA
Expression Range	182-440aa
Protein Length	Partial
Mol. Weight	32.5 kDa
Research Area	Cancer
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	May be involved in membrane trafficking in the early secretory pathway. Inhibits BACE1 activity and amyloid precursor protein processing. May induce caspase-8 cascade and apoptosis. May favor BCL2 translocation to the mitochondria upon endoplasmic reticulum stress. Induces the formation of endoplasmic reticulum tubules.
Subcellular Location	Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
Database References	KEGG: mmu:20168 STRING: 10090.ENSMUSP00000065810 UniGene: Mm.246990
Tissue Specificity	Isoform 1, isoform 3, isoform 4 and isoform 5 are expressed in spinal cord. Isoform 1 is present in brain, where it is expressed in the neurons of cerebral cortex, hippocampus, hypothalamus and cerebellum (at protein level).

Gene Functions References

altered RTN3 levels can impact the axonal transport of BACE1 and demonstrate that reducing axonal transport of BACE1 in axons is a viable strategy for decreasing BACE1 in axonal terminals and, perhaps, reducing amyloid deposition. PMID: 24005676
RTN3 negatively regulates autophagy to block the clearance of cytoplasmic PrP aggregates. PMID: 21119307
results show that reticulon 3 may play a role in the trafficking of the synaptic adhesion-like molecules family of adhesion molecules PMID: 19681166
cDNA of mouse reticulon 3 (mRTN3) was cloned. The gene was mapped at band B of chromosome 19. PMID: 11990451
RTN3 isoforms may contribute, by as yet unknown mechanisms, to neuronal survival and plasticity PMID: 15350194
Since other reports have shown that RTN4-A inhibits neuronal outgrowth and restricts the plasticity of the central nervous system, we speculate that RTN3-A1 might play certain roles in the central nervous system. PMID: 15946766
Transgenic mice overexpressing reticulon 3 develop neuritic abnormalities. PMID: 17476306
RTN3 co-immunoprecipitated with endogenous beta-site amyloid precursor protein-cleaving enzyme 1, confirming interactions between these two membrane proteins in the mouse brain PMID: 19284479

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.