Recombinant Mouse Beta-Synuclein (SNCB)

Name: Recombinant Mouse Beta-Synuclein (SNCB)
Brand: Beta LifeScience
SKU: BLC-08777P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins, Recombinant proteins fall special offers - full-length proteins, Recombinant proteins fall special offers - tag-free proteins

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Product Overview

Description	Recombinant Mouse Beta-Synuclein (SNCB) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q91ZZ3
Target Symbol	SNCB
Synonyms	Sncb; Beta-synuclein
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	Tag-Free
Target Protein Sequence	MDVFMKGLSMAKEGVVAAAEKTKQGVTEAAEKTKEGVLYVGSKTSGVVQGVASVAEKTKEQASHLGGAVFSGAGNIAAATGLVKKEEFPTDLKPEEVAQEAAEEPLIEPLMEPEGESYEDSPQEEYQEYEPEA
Expression Range	1-133aa
Protein Length	Full Length
Mol. Weight	14.1 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	May be involved in neuronal plasticity.
Subcellular Location	Cytoplasm.
Protein Families	Synuclein family
Database References	KEGG: mmu:104069 STRING: 10090.ENSMUSP00000043074 UniGene: Mm.200843
Tissue Specificity	Highly expressed in the brain.

Gene Functions References

the expression patterns of neuronal maturation markers in the brain of a mouse model of dementia with Lewy body-linked mutant beta-synuclein (betaS), especially in the hippocampus. PMID: 29976232
These results suggest that synucleins are important orchestrators of presynaptic terminal topography. PMID: 28052246
Immunoblot analysis of beta-synuclein and Akt levels in the mice reveals selective increases in beta-synuclein and phosphorylated Akt levels in ventral midbrain PMID: 21304957
Synuclein-alpha, -beta, and -gamma are important in regulating neurotransmitter release from specific populations of midbrain dopamine neurons through mechanisms that differ from those reported in other neurons. PMID: 21593311
late onset phenotypes in synuclein null mice were not due to a loss of synapses or neurons but rather reflect specific changes in synaptic protein composition and axonal structure PMID: 20974939
Beta-synuclein decreased formation of Lewy bodies by 40%, and prevented functional deficits associated with overexpression of alpha-synuclein. This is a preliminary in vivo proof of antiaggregatory function of beta-synuclein. PMID: 12212795
Accelerated accumulation of beta-synuclein is found in axonal spheroids of gracile axonal dystrophy mice, which do not express ubiquitin carboxyl-terminal hydrolase L1. PMID: 15306232
beta-synuclein knockout mice show that synucleins are not essential components of the basic machinery for neurotransmitter release but may contribute to the long-term regulation and/or maintenance of presynaptic function. PMID: 15465911
Developmentally, gamma-synuclein can be seen in the region of the outer hair cells by E19, while alpha- and beta-synuclein do not clearly appear there until approximately P10 PMID: 18665422

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.