Nicotinic Acetylcholine Receptor alpha 4 (CHRNA4) Rabbit Polyclonal Antibody

CAT#: TA328607

Rabbit Polyclonal Anti-Nicotinic Acetylcholine Receptor alpha 4 (extracellular


USD 850.00

3 Weeks*

Size
    • 50 ul

Product Images

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Purified recombinant protein of Human cholinergic receptor, nicotinic, alpha 4 (CHRNA4), full length, with C-terminal MYC/DDK tag, expressed in HEK293 cells, 20 µg
    • 20 ug

USD 867.00

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Specifications

Product Data
Applications FC, IHC, WB
Recommended Dilution WB: 1:200-1:2000; IHC: 1:100-1:3,000; FC: 1:50-1:600
Reactivities Human, Mouse, Rat
Host Rabbit
Clonality Polyclonal
Immunogen Peptide (C)DLVNMHSRVDQLD, corresponding to amino acid residues 190-202 of human nAChRa4. Extracellular, N-terminus.
Formulation Lyophilized. Concentration before lyophilization ~0.8mg/ml (lot dependent, please refer to CoA along with shipment for actual concentration). Buffer before lyophilization: Phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.025% NaN3.
Reconstitution Method Add 50 ul double distilled water (DDW) to the lyophilized powder.
Purification Affinity purified on immobilized antigen.
Conjugation Unconjugated
Storage Store at -20°C as received.
Stability Stable for 12 months from date of receipt.
Gene Name cholinergic receptor nicotinic alpha 4 subunit
Background Acetylcholine, released by cholinergic neurons, activates two groups of acetylcholine receptors (AChRs); muscarinic AChRs (mAChRs) which belong to the superfamily of G-protein coupled receptors (GPCRs) and nicotinic AChRs (nAChRs) which belong to the ligand-gated ion channel superfamily. nAChRs also respond to nicotine, hence their name. These channel receptors are usually non-selective cation channels activated upon ligand binding which ultimately leads to the depolarization of postsynaptic cell membranes. To date, 17 different but related subunits of nAChRs have been identified and cloned. They consist of a subunits (a1-10), which is responsible for the binding of ligands. In fact, this subunit includes a Cys-loop in the first extracellular domain that is required for agonist binding. The other subunits responsible for making up the active receptor are the Ã? (Ã?1-4), ?, d and e subunits. Structurally, all subunits have the following: a conserved large extracellular N-terminal domain, 3 conserved transmembrane domains, a variable cytoplasmic loop and a fourth transmembrane domain with a short extracellular C-terminal domain. An active nAChR is generally a heteropentamer (homopentamers also exist) of these various subunits organized around a central pore. All a subunits are expressed in neuronal cells except for the a1 subunit which is specifically expressed in skeletal muscle. They are also expressed in non-neuronal cells such as bronchial epithelial cells, as well lymphocytes. The diversity of these receptors and their functional organization gives rise to unique properties and functions. The a4Ã?2 receptor composition makes up a high affinity nicotinic receptor. In fact, its upregulation (mainly expressed by the increase of functional receptors at the membrane and not expression per se) is responsible for the increased appearance of binding sites following nicotine administration. Animal studies have shown that nAChR-related mechanisms are involved in attention function. Indeed a4Ã?2 nAChR seems to also be involved in attention-deficit hyperactivity disorder (ADHD), a disease distinguished by a lack of attention, distractibility and hyperactivity. The a4Ã?2 and a7 nAChRs appear to be critical in rats for attention and working memory. Also, a a4Ã?2 specific agonist was shown to reduce impulsivity, hyperactivity and attention deficits in adults with ADHD. This same receptor subtype may also be involved in Parkinsonâ??s disease (PD) as smoking and a4Ã?2 nAChR agonists show beneficial effects in PD.
Synonyms BFNC; EBN; EBN1; NACHR; NACHRA4; NACRA4
Reference Data
Protein Families Druggable Genome, Ion Channels: Cys-loop Receptors, Transmembrane

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