Recombinant Rat Vesicular Glutamate Transporter 3 (SLC17A8) Protein (His)

Beta LifeScience SKU/CAT #: BLC-06608P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Rat Vesicular Glutamate Transporter 3 (SLC17A8) Protein (His)

Beta LifeScience SKU/CAT #: BLC-06608P
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Product Overview

Description Recombinant Rat Vesicular Glutamate Transporter 3 (SLC17A8) Protein (His) is produced by our Yeast expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb Q7TSF2
Target Symbol SLC17A8
Synonyms (VGluT3)(Solute carrier family 17 member 8)
Species Rattus norvegicus (Rat)
Expression System Yeast
Tag C-6His
Target Protein Sequence MPFNAFDTFKEKILKPGKEGVKNAVGDSLGILQRKLDGTNEEGDAIELSEEGRPVQTSRARAPVCDCSCCGIPKRY
Expression Range 1-76aa
Protein Length Partial
Mol. Weight 9.8 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 Mediates the uptake of glutamate into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells. May also mediate the transport of inorganic phosphate.
Subcellular Location Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane. Membrane; Multi-pass membrane protein. Cell junction, synapse, synaptosome.
Protein Families Major facilitator superfamily, Sodium/anion cotransporter family, VGLUT subfamily
Database References
Tissue Specificity Expressed in brain, kidney and liver. Expressed within the amygdala, brainstem, cerberal cortex, dorsal root ganglia, dorsal spinal cord, hippocampus, hypothalamus, retina, striatum and ventral spinal cord. Expressed within neurons of the caudate-putamen,

Gene Functions References

  1. Chronic voluntary wheel running results in increased gene expression of VGLUT3 (and GLT-1) in the frontal cortex without changes in other glutamate transporter subtypes. PMID: 29375045
  2. VGLUT3 is involved in the pathogenesis of visceral hyperalgesia in a rat model of irritable bowel syndrome. PMID: 25780293
  3. VGLUT3 likely has developmental and physiological roles in the rat cochlea during postnatal development as well as later in life PMID: 24064385
  4. The results of this study rat brains showing that small, clear, and round synaptic vesicles in gamma-aminobutyric acid (GABA)-ergic nerve terminals contain labeling for both VGLUT3 and the vesicular GABA transporter . PMID: 23633129
  5. VGLUT3-immunoreactive boutons in the lateral sinus form two different, disproportionate, populations of synaptic contacts with their target neurons. PMID: 22374223
  6. VGLUT3 localizes to a distinct set of synaptic-like microvesicles in perisynaptic astroglial processes and may be important for glutamate release from astrocytes. PMID: 22573606
  7. The periodontal Ruffini endings of rat incisors show both VGluT1 and VGluT2, and lack VGluT3. PMID: 21957077
  8. projections between the arcuate nucleus and ventrolateral periaqueductal gray are available to participate in prolonged modulation by electroacupuncture and that VGLUT3-containing neurons are an important neuronal phenotype involved in this process PMID: 20836994
  9. These results suggest that VGLUT3-expressing nonserotonergic neurons in the midbrain raphe nuclei are preferentially distributed in the DRDSh and modulate many brain regions with the neurotransmitter glutamate via ascending axons. PMID: 20034056
  10. Taken together, these findings indicate locally collateralizing glutamate neurons responsive to substance P contain VGLUT3. PMID: 19467322
  11. dendritic expression of VGLUT3 by particular neurons also indicates the potential for retrograde synaptic signaling PMID: 12388773
  12. In the rat retina, the dendrites of vGluT3 amacrine cells form a dendritic tree that is bistratified in the inner plexiform layer. The vGluT3 cells have a dendritic overlap and form a regular mosaic, suggesting a single type of amacrine cell. PMID: 14648683
  13. Weak expression of VGLUT3 mRNA is only detected in deep laminae of lumbar spinal cord. PMID: 14681932
  14. Neurons containing VGLUT3 transcript are essentially observed in the caudate-putamen, the olfactory tubercle, the nucleus accumbens, the hippocampus, the interpeduncular nucleus and the dorsal and medial raphe nuclei. PMID: 14751290
  15. The results suggest that boutons coexpressing VGLUT3, CCK and GAD originate from CCK-positive basket cells, which are VIP-immunonegative. PMID: 14984406
  16. VGLUT3-expressing GABAergic interneurons form a chemically specific circuit within the preprotachykinin B-producing interneuron group. PMID: 15142960
  17. The developmental pattern of Vglut3 in the olivary nucleus was studied. PMID: 15714284
  18. These findings support our hypothesis that neurons and fibers containing VGLUT3 lie in close proximity to those containing nNOS and that both proteins colocalize in some neurons and fibers in the NTS. PMID: 15820620
  19. Between P1 and P15, VGLUT3 is observed in the frontal brain and in the caudal brain During a second phase extending from P15 to adulthood, the labeling of the caudal brain fades away. The adult pattern is reached at P21. PMID: 16182324
  20. VGLUT3 identifies a novel excitatory terminal subset that contributes to the tuning of DA cell excitability in the substantia nigra. PMID: 16519671
  21. Intense VGluT3 immunoreactivity was detected in large number of sensory epithelia cells PMID: 17612597
  22. The present study shows that midbrain raphe-derived 5-HT fibers can be classified into two subtypes depending on co-expression with VGLUT3 staining in the forebrain. PMID: 18222609
  23. Expression of VGLUT3 was first observed at postnatal day 10 (P10) in amacrine cell soma and some processes, which extensively arborized in both the ON and OFF sublamina of the inner plexiform later by P15. PMID: 18482716
  24. distribution of VGLUT3-ir structures in the lateral septum were systematically analyzed revealing PMID: 18611437
  25. A large number of retrogradely labeled cells in the caudal linear and interpeduncular nuclei projecting to the medial septum are found to contain VGLUT3. PMID: 18925658
  26. VGLUT3 is localized within neurons containing the NK1 receptor in several areas of the forebrain. PMID: 19699779

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.

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