|Calculated MW||87842 Da|
|Homology||Mouse - identical; human - 13/14 amino acid residues identical.|
|Other Names||Sodium- and chloride-dependent glycine transporter 2, GlyT-2, GlyT2, Solute carrier family 6 member 5, Slc6a5, Glyt2|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide CVIGDHPKIQIKNS, corresponding to amino acid residues 333-346 of rat Glycine Transporter 2 (Accession P58295). 2nd extracellular loop.|
|Peptide Confirmation||Confirmed by mass-spectrography and amino acid analysis.|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||50 µl or 0.2 ml deionized water, depending on the sample size.|
|Antibody Concentration After Reconstitution||0.8 mg/ml.|
|Buffer After Reconstitution||Phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.05% NaN3.|
|Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Storage After Reconstitution||The reconstituted solution can be stored at 4ºC for up to 2 weeks. For longer periods, small aliquots should be stored at -20ºC or below. Avoid multiple freezing and thawing. The further dilutions should be made using a carrier protein such as BSA (1%). Centrifuge all antibody preparations before use (10000 × g 5 min).|
|Control Antigen Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Control Antigen Reconstitution||100 µl water.|
|Control Antigen Storage After Reconstitution||-20ºC.|
|Preadsorption Control||1 µg peptide per 1 µg antibody.|
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Provided below are standard protocols that you may find useful for product applications.
Apart from its obvious biochemical functions, glycine is also an important inhibitory neurotransmitter. Following depolarization, glycine is released from synaptic vesicles, binds to glycine receptors (GlyRs) on postsynaptic membranes thereby causing hyperpolarization of postsynaptic neurons due to the massive influx of Cl- ions. Glycine is then taken up from the synaptic cleft via the glycine transporters GlyT1 and GlyT2 1. GlyT1 and GlyT2 belong to the SLC6, Na+/Cl- dependent transporter family, of which members include transporters for GABA, serotonin, dopamine and norepinephrine2. Like all SLC6 members, GlyT1 and GlyT2 have 12 transmembrane domains and intracellular N- and C-terminals. Both can be found in different splice variants3,4. SLC6 transporters undergo post-translational modifications. For instance, GlyT1 and GlyT2 are glycosylated, which is important for their membrane trafficking5. Phosphorylation of these two transporters also takes place in a PKC-dependent manner, which may lead to down regulation of both transporters6. Pharmacologically, GlyT1 and GlyT2 can be differentiated by applying sarcosine which inhibits GlyT1 but not GlyT2 7. GlyT1 and GlyT2 are broadly expressed in the nervous system; GlyT1 is concentrated in glial cells, while GlyT2 is present in glycenergic neurons in the spinal cord, brainstem and cerebellum1. GlyT1 can also be detected in the pancreas, uterus, stomach, spleen, liver and retina4. GlyT1 has become a target for the treatment of schizophrenia, although a defect of the protein is not directly associated with the disorder. Inhibiting GlyT1 should lead to the increase in glutamatergic pathways, thereby decreasing psychotic effects in schizophrenic individuals. GlyT2 has been associated with hyperekplexia, a motor disorder characterized by neonatal hypertonia and startle reflex8. Abgent is pleased to offer a highly specific antibody directed against an extracellular epitope of rat GlycineTransporter 2. Anti-Glycine Transporter 2 (GlyT2) (extracellular) antibody (#AG1229) can be used in western blot analysis and has been designed to recognize GlyT2 from rat, mouse and human samples.
References 1. Zafra, F. and Gimenez, C. (2008) IUBMB Life 60, 810. 2. Chen, N. et al. (2004) Pflugers Arch. 447, 519. 3. Supplisson, S. and Roux, M.J. (2002) FEBS Lett. 529, 93. 4. Kristensen, A.S. et al. (2011) Pharmacol. Rev. 63, 585. 5. Olivares, L. et al. (1995) J. Biol. Chem. 270, 9437. 6. Massari, S. et al. (2005) J. Biol. Chem. 280, 7388. 7. Liu, Q.R. et al. (1993) J. Biol. Chem. 268, 22802. 8. Rees, M.I. et al. (2006) Nat. Genet. 38, 801.
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