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AB126174

Anti-Phospholamban抗体

Anti-Phospholamban antibody

4

(1 Review)

|

(2 Publications)

Rabbit Polyclonal Phospholamban antibody. Suitable for WB and reacts with Mouse, Rat samples. Cited in 2 publications. Immunogen corresponding to Recombinant Fragment Protein within Human PLN aa 1-50.

查看别名

PLB, PLN, Phospholamban

1 Images
Western blot - Anti-Phospholamban antibody (AB126174)
  • WB

Supplier Data

Western blot - Anti-Phospholamban antibody (AB126174)

Samples were separated by 15% SDS-PAGE.

All lanes:

Western blot - Anti-Phospholamban antibody (ab126174) at 1/10000 dilution

Lane 1:

Mouse heart tissue extract at 50 µg

Lane 2:

Rat heart tissue extracts at 50 µg

Secondary

All lanes:

HRP-conjugated anti-rabbit IgG antibody

Predicted band size: 6 kDa

false

关键信息

宿主种属

Rabbit

克隆

Polyclonal

亚型

IgG

不含载体蛋白

No

反应种属

Mouse, Rat

应用

WB

applications

免疫原

Recombinant Fragment Protein within Human PLN aa 1-50. The exact immunogen used to generate this antibody is proprietary information.

P26678

反应性数据

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性能和储存信息

形式
Liquid
纯化工艺
Affinity purification Immunogen
存储溶液
pH: 7 Preservative: 0.01% Thimerosal (merthiolate) Constituents: PBS, 20% Glycerol (glycerin, glycerine), 1% BSA
运输条件
Blue Ice
推荐的短期储存条件
+4°C
推荐的长期储存条件
-20°C
分装信息
Upon delivery aliquot
储存信息
Avoid freeze / thaw cycle

补充信息

This supplementary information is collated from multiple sources and compiled automatically.

Phospholamban abbreviated as PLN is an important regulatory protein in cardiac muscle cells often referred to interchangeably with its phosphorylated form phospho-phospholamban. This protein with a molecular mass of about 6 kDa is primarily expressed in cardiac and skeletal muscles. It functions mechanically by regulating the calcium pump (SERCA2a) in the sarcoplasmic reticulum modulating calcium uptake during muscle relaxation. In its unphosphorylated state phospholamban inhibits the activity of SERCA2a reducing calcium uptake and affecting muscle contractility.
Biological function summary

Phospholamban serves as an important mediator in the control of cardiac muscle contraction and relaxation. It is a component of the calcium cycling process within heart cells and associates directly with SERCA2a to form a regulatory complex. This association allows phospholamban to influence calcium homeostasis significantly affecting myocardial contractility and relaxation. Phosphorylation of phospholamban typically induced by beta-adrenergic signaling results in diminished interaction with SERCA2a enhancing calcium uptake into the sarcoplasmic reticulum.

Pathways

Several important pathways involve phospholamban including the adrenergic signaling pathway in cardiomyocytes and calcium signaling pathways. Phospholamban's role in these pathways is linked with proteins like SERCA2a and Protein Kinase A (PKA). PKA phosphorylates phospholamban an important step in the beta-adrenergic cascade that leads to increased heart muscle contractility. This phosphorylation event highlights phospholamban's participation in modulating cardiac output under sympathetic nervous system influence.

Phospholamban's regulation of calcium homeostasis connects it directly to conditions like heart failure and cardiomyopathy. In heart failure the dysregulation of phospholamban phosphorylation can lead to impaired cardiac function due to disrupted calcium cycling reducing cardiac output. Mutations in the phospholamban gene can lead to dilated cardiomyopathy a condition characterized by the enlargement and weakening of the heart muscle. These mutations affect the interaction with SERCA2a highlighting the role of phospholamban in maintaining cardiac muscle health.

产品实验方案

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靶点信息

Reversibly inhibits the activity of ATP2A2/SERCA2 in cardiac sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+) (PubMed : 28890335). Binds preferentially to the ATP-bound E1 conformational form of ATP2A2 which predominates at low Ca(2+) concentrations during the diastolic phase of the cardiac cycle (By similarity). Inhibits ATP2A2 Ca(2+) affinity by disrupting its allosteric activation by ATP (By similarity). Modulates the contractility of the heart muscle in response to physiological stimuli via its effects on ATP2A2. Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in the heart muscle. The degree of ATP2A2 inhibition depends on the oligomeric state of PLN. ATP2A2 inhibition is alleviated by PLN phosphorylation (By similarity). Also inhibits the activity of ATP2A3/SERCA3 (By similarity). Controls intracellular Ca(2+) levels in elongated spermatids and may play a role in germ cell differentiation (By similarity). In the thalamic reticular nucleus of the brain, plays a role in the regulation of sleep patterns and executive functioning (By similarity).
See full target information PLN

文献 (2)

Recent publications for all applications. Explore the full list and refine your search

Circulation 146:1758-1778 PubMed36259389

2022

Mutant Phosphodiesterase 3A Protects From Hypertension-Induced Cardiac Damage.

Applications

Unspecified application

Species

Unspecified reactive species

Maria Ercu,Michael B Mücke,Tamara Pallien,Lajos Markó,Anastasiia Sholokh,Carolin Schächterle,Atakan Aydin,Alexa Kidd,Stephan Walter,Yasmin Esmati,Brandon J McMurray,Daniella F Lato,Daniele Yumi Sunaga-Franze,Philip H Dierks,Barbara Isabel Montesinos Flores,Ryan Walker-Gray,Maolian Gong,Claudia Merticariu,Kerstin Zühlke,Michael Russwurm,Tiannan Liu,Theda U P Batolomaeus,Sabine Pautz,Stefanie Schelenz,Martin Taube,Hanna Napieczynska,Arnd Heuser,Jenny Eichhorst,Martin Lehmann,Duncan C Miller,Sebastian Diecke,Fatimunnisa Qadri,Elena Popova,Reika Langanki,Matthew A Movsesian,Friedrich W Herberg,Sofia K Forslund,Dominik N Müller,Tatiana Borodina,Philipp G Maass,Sylvia Bähring,Norbert Hübner,Michael Bader,Enno Klussmann

Circulation research 124:712-726 PubMed30566039

2018

SPEG Controls Calcium Reuptake Into the Sarcoplasmic Reticulum Through Regulating SERCA2a by Its Second Kinase-Domain.

Applications

Unspecified application

Species

Unspecified reactive species

Chao Quan,Min Li,Qian Du,Qiaoli Chen,Hong Wang,David Campbell,Lei Fang,Bin Xue,Carol MacKintosh,Xiang Gao,Kunfu Ouyang,Hong Yu Wang,Shuai Chen
View all publications

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