Recombinant Rat Vesicular Glutamate Transporter 1 (SLC17A7) Protein (His)

Name: Recombinant Rat Vesicular Glutamate Transporter 1 (SLC17A7) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06491P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Rat Vesicular Glutamate Transporter 1 (SLC17A7) Protein (His) is produced by our Yeast expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q62634
Target Symbol	SLC17A7
Species	Rattus norvegicus (Rat)
Expression System	Yeast
Tag	C-6His
Target Protein Sequence	MEFRQEEFRKLAGRALGRLHRLLEKRQEGAETLELSADGRPVTTHTRDPPVVDCTCFGLPRRY
Expression Range	1-63aa
Protein Length	Partial
Mol. Weight	8.8 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	KEGG: rno:116638 STRING: 10116.ENSRNOP00000063604 UniGene: PMID: 28238468 VGLUT1 was transiently down-regulated in ipsilateral dorsal root ganglia and contralateral spinal cord in a model of spared nerve injury. PMID: 27210824 In previously unstressed rats, vGluT1 siRNA significantly enhanced ACTH and corticosterone secretion. Compared with chronic variable stress (CVS) animals receiving the green fluorescent protein control vector, the vGluT1 siRNA further increased basal and stress-induced corticosterone release. Further analysis revealed enhanced adrenal responsiveness in CVS rats treated with vGluT1 siRNA. PMID: 28938481 results indicated that VGLUT1v exists in a functional state in rat photosensitive cells and is involved in glutamatergic chemical transmission PMID: 28188742 vGlut1 has a strong influence on the kinetics of retrieval of half of the known SV cargos and that specifically impairing the endocytosis PMID: 26224632 The results indicated that glutamatergic spinal trigeminal nucleus neurons sending their axons to the cerebellar cortical regions mainly express VGLUT1. PMID: 23380804 Following peripheral nerve injury, 62% of VGLUT1 synapses are lost on spinal motor neuron dendrites. PMID: 24599449 VGLUT1 contains multiple sorting signals that engage distinct trafficking mechanisms PMID: 23804088 These results suggest that BDNF regulates VGLUT expression during development and its effect on VGLUT1 may contribute to enhance glutamate release in LTP PMID: 23326507 Up-regulation of VGLUT1 is important for development of presynaptic terminals in the cortex. PMID: 23226425 VGluT1 immunoreactions are localized within the cytoplasm for all sizes of trigeminal neurons, although predominantly in medium-large trigeminal neurons. PMID: 21957077 VGLUT1 labeling is concentrated in astrocytic processes from wild type, and not in VGLUT1 knockout hippocampus. PMID: 22009457 Expression of VGLUT2 precedes that of VGLUT1 during olfactory bulb morphogenesis, suggesting differential contribution of the two VGLUT subtypes to glutamate-mediated embryonic events. PMID: 21609737 After nerve injuries synapses are stripped from motoneurons, other excitatory and inhibitory inputs eventually recover but VGLUT1 synapses are permanently lost on the cell body (75-95% synaptic losses) and on the proximal 100 mum of dendrite (50% loss). PMID: 21832035 The VGLUT1 upstream promoter and the first intron, fused to the basal promoter, both support glutamatergic-specific expression in rat postrhinal cortex. PMID: 21172319 The vesicular glutamate transporter-1 (VGLUT1)promoter supports expression in VGLUT1-containing glutamatergic neurons in rat postrhinal cortex. PMID: 20849834 Most of the glutamatergic neurons that expressed glutamate vesicular transporter 1 also co-expressed choline acetyltransferase. PMID: 20632124 There are regionally significant correlations between VGLUT1 concentration and cognitive scores between different dementia groups and those with stroke who do not develop dementia. PMID: 21079182 observed a biphasic and bilateral change in the protein expression levels of both VGLUTs in the striatum of hemi-Parkinson rats indicative for a different and time-dependent change in glutamatergic neurotransmission from two types of striatal afferents PMID: 20450947 The study suggested that VGLUT enhances transmitter storage in nonglutamatergic neurons. PMID: 20519538 The presence of the glutamate markers VGLUT1 and VGLUT2 in distinct populations of peptide hormone-secreting hypophysial cells highly indicates the involvement of endogenous glutamate release in autocrine/paracrine regulatory mechanisms PMID: 20025917 These findings show the specific lingual pattern of distribution for VGluts and suggest that only VGlut 1 takes part in glutamatergic regulation of epithelial and taste cells within the tongue in physiological conditions. PMID: 19952853 VGLUT1 immunoreactivity was detected in the sensory endings on the equatorial and juxta-equatarial regions of intrafusal fibers as well as in many axon terminals within lamina IX of the spinal cord. PMID: 15157812 VGLUT1 provides a specific marker for glutamatergic neuronal elements in the septal hippocampus. PMID: 15224985 The developmental pattern of Vglut1 in the olivary nucleus was studied. PMID: 15714284 the coupling of zinc transporter 3 and Vglut1 transport mechanisms regulates neurotransmitter content in secretory vesicles PMID: 15860731 A newly proposed mechanism for altering the strength of glutamatergic synapses based on the recently identified vesicular glutamate transporter VGLUT1. PMID: 15987952 a high proportion of cardiac neurones appear to be glutamatergic, but differ from other vagal afferents in expressing vesicular glutamate transporter 1 PMID: 16084661 VGLUT1-ir was found in extrinsic as well as intrinsic innervation of the rat esophagus. PMID: 16231188 Overall, the discovery of endophilin as a partner for VGLUT1 in nerve terminals strongly suggests the existence of functional differences between VGLUT1 and -2 terminals in their abilities to replenish vesicle pools. PMID: 16606361 VGLUT1 and endophilins may interact to play an important role affecting the vesicular sequestration and synaptic release of glutamate. PMID: 16710756 Lamina I and IIo displayed a moderate density of small VGLUT1 varicosities at all spinal levels. Corticospinal tract axons displayed VGLUT1, indicating that the corticospinal tract is an important source of small VGLUT1 varicosities. PMID: 16786558 After stimulation, inhibition of the AP3 pathway prevents the full recovery of VGLUT1 by endocytosis, implicating the AP3 pathway specifically in compensatory endocytosis. PMID: 16815333 These data indicate that VGLUT1 is expressed in both the central axon terminals and the peripheral sensory endings of Vmes neurons, although no VGLUT1 immunoreactivity was detectable in the cell bodies of Vmes neurons in adult rats. PMID: 16856164 In situ hybridization with variant-specific probes showed expression of VGLUT1v in the inner segment layer of photoreceptor cells. PMID: 16987242 No significant change in either VGLUT1 or GlyT2 labeling of sacrocaudal motoneurons at any of the time points examined. PMID: 17134699 There was a striking loss of mossy cells during the latent period, demonstrated by a long-term decrease of VGLUT1 mRNA-containing hilar neurons and associated loss of VGLUT1-containing terminals in the dentate gyrus. PMID: 17503488 VGluT1 was localized to partial neurons of VG and to the putative primary afferent fibers innervating vestibular end-organs. PMID: 17612597 Histological analysis revealed that intensities of VGLUT1 hybridization signal and immunostaining drastically increase by postnatal day (P) 7 in pinal gland. PMID: 18291592 Results showed numerous VGLUT1 immunolabeled terminals in the central nucleus, lateral cortex and dorsal cortex, and Results showed numerous VGLUT1 and 2 immunolabeled terminals in the central nucleus, lateral cortex and dorsal cortex. PMID: 18436385 In rat retina, VGLUT1 was initially detected at postnatal day (P5) in photoreceptor terminals and P6 in bipolar terminals. PMID: 18482716 In the present study observed a higher expression of vglut1 mRNA in the left cingulate cortex. This suggests a hemispheric asymmetry in the strength of the cortico-subcortical glutamatergic system. PMID: 19626270 In cortical cultures and layer V cortical terminals VGLUT1 is coexpressed with vesicular transporter VGAT in the same population of synaptic vesicles. PMID: 19627441

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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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