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FITC标记的肾上腺素能受体β2/β2-AR抗体

文字:[大][中][小] 2017-5-2    浏览次数:929    

                                     FITC标记的肾上腺素能受体β2/β2-AR抗体                                                                                                                                              
英文名称Anti-ADRB2/FITC
中文名称:FITC标记的肾上腺素能受体β2/β2-AR抗体
别    名Beta 2-adrenergic receptor; beta 2 Adrenergic Receptor; ADRB2; ADRB2R; ADRBR; ADRB2_HUMAN; Adrenergic beta 2 receptor surface; B2AR; BAR; beta 2 adrenoceptor; Beta 2 adrenoreceptor; BETA2AR; Catecholamine receptor; beta2-adrenergic receptor. 

详细介绍:


 
规格:100ul 
说 明 书100ul  
研究领域肿瘤  细胞生物  神经生物学  细胞膜受体  
抗体来源Rabbit
克隆类型Polyclonal
交叉反应 Human, Mouse, Rat, Dog, Rabbit, 
产品应用Flow-Cyt=1:50-200 IF=1:50-200  
not yet tested in other applications.
optimal dilutions/concentrations should be determined by the end user.
分 子 量46kDa
细胞定位细胞膜 
性    状Lyophilized or Liquid
浓    度1mg/ml
免 疫 原KLH conjugated synthetic peptide derived from human beta 2 Adrenergic Receptor
亚    型IgG
纯化方法affinity purified by Protein A
储 存 液0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol.
保存条件Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. The lyophilized antibody is stable at room temperature for at least one month and for greater than a year when kept at -20°C. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C.

相关资料:


产品介绍background:
Beta 2 Adrenergic Receptor is a member of the G protein coupled receptor superfamily. This receptor is directly associated with one of its ultimate effectors, the class C L type calcium channel Ca(V)1.2. This receptor channel complex also contains a G protein, an adenylyl cyclase, cAMP dependent kinase, and the counterbalancing phosphatase, PP2A. The assembly of the signaling complex provides a mechanism that ensures specific and rapid signaling by this G protein coupled receptor. This gene contains no introns in either its coding or untranslated sequences. Different polymorphic forms, point mutations, and/or downregulation of this gene are associated with nocturnal asthma, obesity and type 2 diabetes. Expression of the beta 2 Adrenergic Receptor has been reported in adipose, blood, brain, heart, lung, nose, pancreas, skeletal muscle, skin, and vessel

Function:
Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine.

Subunit:
Binds SLC9A3R1 and GPRASP1. Interacts with ARRB1 and ARRB2. Interacts with SRC, USP20 and USP33. Interacts with VHL; the interaction, which is increased on hydroxylation of ADRB2, ubiquitinates ADRB2 leading to its degradation. Interacts with EGLN3; the interaction hydroxylates ADRB2 facilitating VHL-E3 ligase-mediated ubiquitination.

Subcellular Location:
Cell membrane; Multi-pass membrane protein. Note=Colocalizes with VHL at the cell membrane.

Post-translational modifications:
Palmitoylated; may reduce accessibility of Ser-345 and Ser-346 by anchoring Cys-341 to the plasma membrane. Agonist stimulation promotes depalmitoylation and further allows Ser-345 and Ser-346 phosphorylation. 
Phosphorylated by PKA and BARK upon agonist stimulation, which mediates homologous desensitization of the receptor. PKA-mediated phosphorylation seems to facilitate phosphorylation by BARK. 
Phosphorylation of Tyr-141 is induced by insulin and leads to supersensitization of the receptor. 
Polyubiquitinated. Agonist-induced ubiquitination leads to sort internalized receptors to the lysosomes for degradation. Deubiquitination by USP20 and USP33, leads to ADRB2 recycling and resensitization after prolonged agonist stimulation. USP20 and USP33 are constitutively associated and are dissociated immediately after agonist stimulation. Ubiquitination by the VHL-E3 ligase complex is oxygen-dependent. 
Hydroxylation by EGLN3 occurs only under normoxia and increases the interaction with VHL and the subsequent ubiquitination and degradation of ADRB2.

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