Recombinant Human Excitatory Amino Acid Transporter 1 (SLC1A3) Protein (His)

Beta LifeScience SKU/CAT #: BLC-07268P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Excitatory Amino Acid Transporter 1 (SLC1A3) Protein (His)

Beta LifeScience SKU/CAT #: BLC-07268P
Regular price $659.00 Sale price $349.00Save $310
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Product Overview

Description Recombinant Human Excitatory Amino Acid Transporter 1 (SLC1A3) Protein (His) is produced by our Yeast expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P43003
Target Symbol SLC1A3
Species Homo sapiens (Human)
Expression System Yeast
Tag C-6His
Target Protein Sequence HPGKGTKENMHREGKIVRVTAADAFLDLIRNMFPPNLVEACFKQFKTNYEKRSFKVPIQANETLVGAVINNVSEAMETLTRITEELVPVPG
Expression Range 146-236aa
Protein Length Partial
Mol. Weight 11.7 kDa
Research Area Neuroscience
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 Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport. Plays a redundant role in the rapid removal of released glutamate from the synaptic cleft, which is essential for terminating the postsynaptic action of glutamate.
Subcellular Location Cell membrane; Multi-pass membrane protein.
Protein Families Dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family, SLC1A3 subfamily
Database References
Associated Diseases Episodic ataxia 6 (EA6)
Tissue Specificity Detected in brain. Detected at very much lower levels in heart, lung, placenta and skeletal muscle. Highly expressed in cerebellum, but also found in frontal cortex, hippocampus and basal ganglia.

Gene Functions References

  1. EAAT1 rs2731880 SNP is associated with amygdala functional connectivity in bipolar disorder. PMID: 30073554
  2. Episodic ataxias 6 is caused by heterozygous mutations in SLC1A3, which encodes a subunit of a glial excitatory amino acid transporter, EAAT1. PMID: 29891059
  3. a novel missense mutation, c.383T>G (p.Met128Arg) in SLC1A3, in an episodic ataxia patient by whole-exome sequencing. PMID: 29208948
  4. This is the first study to link SLC1A3 and EPHB2 to clinically relevant vertebral osteoporosis phenotypes. PMID: 27476799
  5. crystal structures of a thermostabilized human SLC1 transporter, the excitatory amino acid transporter 1 (EAAT1), with and without allosteric and competitive inhibitors bound PMID: 28424515
  6. This study demonstrated that the cytopathology and episodic paralysis in our Drosophila EA6 model stem from a gain-of-function chloride channelopathy of glial cells.. PMID: 27445142
  7. Starvation of Muller cells increased the glutamate uptake capacity as well as the expression of the most abundant glutamate transporter, EAAT1. PMID: 27196320
  8. A heterozygous SLC1A3 c.1177G4A mutation has been detected in a patient with late-onset episodic ataxia. Same heterozygous mutation was identified in one clinically affected family member and two asymptomatic members. PMID: 27829685
  9. We consider an association between SLC1A3 and the behavioural problems which can also be considered a contributing factor to behavioural problems in larger duplications overlapping the 5p13 microduplication syndrome region. PMID: 27296938
  10. In combination with other nearby residues, Arg-388 coordinates anion channel gating and forms part of the missing structural link between the anion conducting and substrate transport states in EAAT1. PMID: 26683197
  11. There was no association between pyramidal cell EAAT1 splice variant expression and schizophrenia. PMID: 26057049
  12. data provide additional insights into the mechanism by which substrates gate the anion conductance in EAATs and suggest that in EAAT1, Arg-388 is a critical element for the structural coupling between the substrate translocation and the gating mechanisms PMID: 26203187
  13. discovering compounds that can enhance EAAT1 expression and activity may be a novel strategy for therapeutic treatment of glaucoma. PMID: 25789968
  14. EAAT1 polymorphism which is involved in the Regulation of extracellular glutamate concentrations, influences Cognitive performances with a detrimental effect of T/T homozygosis. PMID: 25660734
  15. Its dysregulation may contribute to the pathology and possibly affect the onset of fragile X-associated tremor/ataxia syndrome. PMID: 24332449
  16. Increased SLC1A3 expression in the cerebellum of elderly schizophrenia patients indicates facilitated transport and may result in reduced glutamate neurotransmission. PMID: 22424243
  17. Plasma membrane EAAT1 (and NCX1)are both involved in glutamate-induced ATP synthesis. PMID: 23913256
  18. Decreased expression of EAAT1 protein remodels glutamate neurotransmission in the superior temporal gyrus in schizophrenia. PMID: 23356950
  19. Episodic ataxia type 6 represents the first human disease found to be associated with altered function of excitatory amino acid transporter anion channels. PMID: 23107647
  20. Close functional similarities of the GLAST/EAAT-1 promoter regions in man and rat exist which point to a species-specific function of the GLAST/EAAT-1 3'-UTR in constitutive and regulated GLAST/EAAT-1 expression. PMID: 22252783
  21. EAAT-1 expression was found in 91% of choroid plexus tumors and was absent in endolymphatic sac tumors. PMID: 22706862
  22. Letter: report expression of dishevelled-3 and EAAT1 and glutamine metabolism in malignant pleural mesothelioma. PMID: 22569537
  23. The accessibility in the external part of the TM5 of the glutamate transporter EAAT1 is conformationally sensitive during the transport cycle. PMID: 22292083
  24. These results indicate that E219D is a functional SLC1A3 variant that is presented in a small number of individuals with Tourette syndrome. PMID: 21233784
  25. water and urea permeation properties of wild-type EAAT1 and two mutant transporters were measured to identify which permeation pathway facilitates the movement of these molecules PMID: 21732909
  26. A series of single cysteine substitutions in the helical hairpin HP2 of excitatory amino acid transporter 1 form intersubunit disulfide cross-links within the trimer. PMID: 21876140
  27. There is no association between SLC1A3 and normal tension glaucoma (NTG), suggesting that the SLC1A3 gene may not be an associated factor in NTG pathogenesis. PMID: 21528001
  28. Dose-dependent modulation of EAAT1-mediated aspartate transport by benzodiazepines suggests a role of glial as well as neuronal transporters in drug action. PMID: 11792462
  29. EAAT1 was strongly expressed in a subset of cortical pyramidal neurons in dementia cases showing Alzheimer-type pathology. In addition, tau (which is a marker of neurofibrillary pathology) colocalized to those same pyramidal cells that expressed EAAT1 PMID: 11826152
  30. Data show that excitatory amino acid transporter (EAAT)-1 was expressed by activated macrophages/microglia in all HIV-infected cases but not in HIV-negative controls. PMID: 12769187
  31. To test whether Nedd4-2, SGK1, SGK3 and protein kinase B regulate EAAT1, cRNA encoding EAAT1 was injected into Xenopus oocytes with or without injection of Nedd4-2, constitutively active[CA] S422DSGK1, inactive K127NSGK1, SGK3 and/or CA T308D,S473DPKB PMID: 12911626
  32. Transcriptional regulation of human excitatory amino acid transporter 1 (EAAT1): cloning of the EAAT1 promoter and characterization of its basal and inducible activity in human astrocytes. PMID: 14713304
  33. We observed decreased glutamate uptake V(max), without modification of transporter affinity, in aging, which could be linked to the selective decrease of EAAT1 expression and mRNA. Moreover, in AD patients we found a further EAAT1 reduction. PMID: 14749132
  34. Only activated macrophages/microglia (AMM) expressed EAAT-1. Proportion of AMM expressing EAAT-1 did not correlate with severity of neuronal apoptosis, spongiosis, astrocytosis, microgliosis, or PrP deposition, but only with disease duration. PMID: 15535133
  35. EAAT1 parameters were mutually correlated (p<0.01) and correlations were shown with dementia severity (p<0.05 MMSE-expression, p<0.005 MMSE-mRNA). PMID: 15718040
  36. Genetic variation in SLC1A3 may contribute to susceptibility to ADHD. PMID: 15950021
  37. EAAT1ex9skip splice variant is a negative regulator of full-length EAAT1 function in the human brain PMID: 16042756
  38. Our data show that a heterozygous mutation in EAAT1 can lead to decreased glutamate uptake, which can contribute to neuronal hyperexcitability to cause seizures, hemiplegia, and episodic ataxia. PMID: 16116111
  39. the activity of glutamate transporter GLAST/EAAT1 can effectively regulate the cell surface expression of glutamine/neutral amino acid transporter ASCT2 in human fetal astrocytes PMID: 16516348
  40. Rearrangements in the tertiary structure of the EAAT1 translocation pore during transport provide constraints for modeling the structural dynamics associated with transport. PMID: 16877378
  41. SLC1A3 is unlikely to be a major susceptibility gene for schizophrenia in the Japanese population. PMID: 17221839
  42. Activity of GLAST directs FXYD2 protein/gamma subunit to the cell surface, that leads to the activation of the astroglial sodium pump. PMID: 17316900
  43. Continued expression of GLAST by neural progenitor cells in the transgenic mouse brain raises the possibility that GLAST may have an unanticipated role in regulating their behavior. PMID: 17581948
  44. We documented for the first time the expression of the mGluR5 and EAAT1 in MG-63 cells, as well as the ability of dexamethasone to upregulate the expression of the mGluR5 and EAAT1 in the MG-63 cells. PMID: 17627080
  45. Mutations in transmembrane domains 5 and 7 of the human excitatory amino acid transporter 1 affect the substrate-activated anion channel PMID: 17676873
  46. No pathogenic mutation were identified in SLC1A3. PMID: 18446307
  47. increased expression in the prefrontal cortex of chronic alcoholics PMID: 18657127
  48. analysis of the importance of Leu-303 or its counterpart Leu-391 in human EAAT1 (hEAAT1) PMID: 18678877
  49. We broadened the clinical spectrum associated with SLC1A3 mutations to include milder manifestations of EA without seizures or alternating hemiplegia. The severity of EA6 symptoms is related to the extent of glutamate transporter dysfunction. PMID: 19139306

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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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