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AB114227

Recombinant Human Phospholamban protein (GST tag N-Terminus)

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Recombinant Human Phospholamban protein (GST tag N-Terminus) is a Human Fragment protein, in the 1 to 30 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.

View Alternative Names

PLB, PLN, Phospholamban

1 Images
SDS-PAGE - Recombinant Human Phospholamban protein (GST tag N-Terminus) (AB114227)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human Phospholamban protein (GST tag N-Terminus) (AB114227)

ab114227 analysed on a 12.5% SDS-PAGE gel stained with Coomassie Blue.

Key facts

Expression system

Wheat germ

Tags

GST tag N-Terminus

Applications

WB, SDS-PAGE, ELISA

applications

Biologically active

No

Accession

P26678

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.79% Tris HCl, 0.3% Glutathione

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

Protein concentration is above or equal to 0.05 mg/mL.

Sequence info

[{"sequence":"MEKVQYLTRSAIRRASTIEMPQQARQKLQN","proteinLength":"Fragment","predictedMolecularWeight":"28.93 kDa","actualMolecularWeight":null,"aminoAcidEnd":30,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"P26678","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

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.

Specifications

Form

Liquid

General info

Function

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).

Sequence similarities

Belongs to the phospholamban family.

Post-translational modifications

Phosphorylation by PKA abolishes the inhibition of ATP2A2-mediated calcium uptake. Phosphorylated at Thr-17 by CaMK2, and in response to beta-adrenergic stimulation. Phosphorylation by DMPK may stimulate sarcoplasmic reticulum calcium uptake in cardiomyocytes.. Palmitoylated by ZDHHC16, promoting formation of the homopentamer.. In elongated spermatids, proteolytically cleaved by SPPL2C which modulates intracellular Ca(2+) homeostasis.

Subcellular localisation

Mitochondrion membrane

Product protocols

Target data

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

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