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Purified Mouse Anti-GluR δ2
Product Details
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BD Transduction Laboratories™
Rat (QC Testing), Mouse (Tested in Development)
Mouse IgG1
Mouse GluR δ2 aa. 665-786
Western blot (Routinely Tested), Immunohistochemistry (Tested During Development)
111 kDa
250 µg/ml
AB_398319
Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide.
RUO


Preparation And Storage

The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography. Store undiluted at -20°C.

Product Notices

  1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
  2. Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
  3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
  4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
611006 Rev. 1
Antibody Details
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48/GluRδ2

Glutamate is a major excitatory neurotransmitter of the CNS. The diversity of  glutamate is exemplified by two distinct groups of receptors: ionotropic and metabotropic. Ionotroic receptors are ligand-gated cation channels. They can be subdivided into two classes: NMDA and AMPA/kainate receptors. GluR δ2 exhibits only 25% amino acid identity to either ionotropic receptor type. It presents selective and abundant exression in cerebellar Purkinje cells. It is targeted to a subset of Purkinje cell spines and is coexpressed with ionotropic receptors. GluR δ2 is involved in motor coordination, Purkinje cell synapse formation, and cerebellar long-term depression (LTD). The latter is a decrease in the efficacy of the synaptic transmission between parallel fibers and Purkinje neurons and is a cellular basis of motor learning. In fact, mGluR δ2-deficient mice lack LTD. Additionally, an amino acid substitution in transmembrane III of δ2 is responsible for the neurodegeneration seen in Lurcher mice. This substitution is a gain of function mutation that results in disruption of Purkinje membrane potential. Thus, GluR δ2 is an important regulatory component of the Purkinje GluR channel.

611006 Rev. 1
Format Details
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Purified
Tissue culture supernatant is purified by either protein A/G or affinity purification methods. Both methods yield antibody in solution that is free of most other soluble proteins, lipids, etc. This format provides pure antibody that is suitable for a number of downstream applications including: secondary labeling for flow cytometry or microscopy, ELISA, Western blot, etc.
Purified
611006 Rev.1
Citations & References
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Development References (5)

  1. Araki K, Meguro H, Kushiya E, Takayama C, Inoue Y, Mishina M. Selective expression of the glutamate receptor channel delta 2 subunit in cerebellar Purkinje cells. Biochem Biophys Res Commun. 1993; 197(3):1267-1276. (Biology). View Reference
  2. Hirano T, Kasono K, Araki K, Mishina M. Suppression of LTD in cultured Purkinje cells deficient in the glutamate receptor delta 2 subunit. Neuroreport. 1995; 6(3):524-526. (Biology). View Reference
  3. Kashiwabuchi N, Ikeda K, Araki K. Impairment of motor coordination, Purkinje cell synapse formation, and cerebellar long-term depression in GluR delta 2 mutant mice. Cell. 1995; 81(2):245-252. (Biology). View Reference
  4. Landsend AS, Amiry-Moghaddam M, Matsubara A. Differential localization of delta glutamate receptors in the rat cerebellum: coexpression with AMPA receptors in parallel fiber-spine synapses and absence from climbing fiber-spine synapses. J Neurosci. 1997; 17(2):834-842. (Biology). View Reference
  5. Zuo J, De Jager PL, Takahashi KA, Jiang W, Linden DJ, Heintz N. Neurodegeneration in Lurcher mice caused by mutation in delta2 glutamate receptor gene. Nature. 1997; 388(6644):769-773. (Biology). View Reference
View All (5) View Less
611006 Rev. 1

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For Research Use Only. Not for use in diagnostic or therapeutic procedures.