Recombinant Human Cardiac Phospholamban (PLN) Protein (GST)

Name: Recombinant Human Cardiac Phospholamban (PLN) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-04680P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Cardiac Phospholamban (PLN) Protein (GST) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P26678
Target Symbol	PLN
Synonyms	Cardiac phospholamban; CMD1P; CMH18; PLB; Pln; PPLA_HUMAN
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	N-GST
Target Protein Sequence	MEKVQYLTRSAIRRASTIEMPQQARQKLQNLFINFCLILICLLLICIIVMLL
Expression Range	1-52aa
Protein Length	Full Length
Mol. Weight	33.1kDa
Research Area	Cardiovascular
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Reversibly inhibits the activity of ATP2A2 in cardiac sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). 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.
Subcellular Location	Endoplasmic reticulum membrane; Single-pass membrane protein. Sarcoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein. Membrane; Single-pass membrane protein.
Protein Families	Phospholamban family
Database References	HGNC: 9080 OMIM: 172405 KEGG: hsa:5350 STRING: 9606.ENSP00000350132 UniGene: PMID: 29501609 Structure-Function Relationship of the SERCA Pump and Its Regulation by Phospholamban and Sarcolipin. PMID: 29594859 The co-transfection of VHL and PLN in HEK293 cells decreased PLN expression under oxidative stress, whereas knockdown of VHL increased PLN expression both under normal and oxidative stress conditions. PMID: 29068413 Hearts from patients with a p. Arg14del PLN mutation have a pattern of Right Ventricle Fibrofatty Replacement and Left Ventricular Fibrosis with fatty changes mostly in the posterolateral wall, independently of clinical presentation. PMID: 28365402 LMOD1, SYNPO2, PDLIM7, PLN, and SYNM down-regulation reflect the altered phenotype of smooth muscle cells in vascular disease and could be early sensitive markers of SMC dedifferentiation. PMID: 27470516 microRNAs (miRNAs) 1 and 21 bind PLN strongly and relieve PLN inhibition of SERCA to a greater extent than a similar length random sequence RNA mixture. PMID: 27531746 Data suggest phospholamban (PLN) gene is a rare cause of cardiomyopathy in African patients. PMID: 26917049 Phospholamban and sarcolipin are membrane proteins that differentially regulate SERCA function. (Review) PMID: 26743715 PLN may be a key molecular player in rigid substrate-induced cellular hypertrophy in eosinophilic esophagitis. PMID: 26542032 These data suggest that PLN is, at least partially, oligo-ubiquitinated at Lys(3) and degraded through Ser(16)-phosphorylation-mediated poly-ubiquitination during heart failure. PMID: 26966065 hereditary mutants of phospholamban are associated with heart failure [review] PMID: 25563649 PLN pentamers reduce phosphorylation of monomers at baseline and delay monomer phosphorylation upon PKA stimulation leading to increased interaction of PLN monomers with SERCA2a. PMID: 25562800 Phospholamban R14del mutation carriers are at high risk for malignant ventricular arrhythmias and end-stage heart failure, with left ventricular ejection fraction <45% and sustained or nonsustained ventricular tachycardia as independent risk factors. PMID: 24909667 Although SLN and PLB binding to SERCA have different functional outcomes on the coupling efficiency of SERCA, both proteins decrease the apparent Ca(2+) affinity of the pump, suggesting that SLN and PLB inhibit SERCA by using a similar mechanism. PMID: 25983321 Phospholamban, and its interacting partners, regulates excitation contraction coupling and myocardial contraction. [Review] PMID: 25451386 PLN mutations rarely cause cardiomyopathy PMID: 25928149 analysis of how the conformational dynamics of protein kinase A induced by a lethal mutant of phospholamban hinder phosphorylation PMID: 25775607 Aim of the present study is to determine the exact pattern of fibrosis and fatty replacement in PLN p.Arg14del mutation positive patients. PMID: 24732829 Engineered upregulation of PLB expression in hESC/iPSC-vCMs restores a positive inotropic response to beta-adrenergic stimulation. PMID: 25504561 a previously unrecognized mechanism for ESM cell contraction that depends on TGF-beta1, its receptors, and PLN. PMID: 24835503 We conclude that PLB C-terminal residues are critical for localization, oligomerization, and regulatory function. In particular, the PLB C terminus is an important determinant of the quaternary structure of the SERCA regulatory complex. PMID: 25074938 SLN and PLN are co-expressed in most fibers, which suggests that super-inhibition of SERCAs may be physiologically important in the regulation of intracellular Ca2+ in human skeletal muscle. PMID: 24358354 Report PLN mutations in dilated cardiomyopathy. PMID: 24037902 A PLN founder mutation and LMNA mutations were most prevalent and often demonstrated a specific phenotype in dilated cardiomyopathy patients PMID: 23349452 PLN mutation carriers have ARVD/C characteristics, including important right ventricular involvement, and additionally more often low-voltage electrocardiograms, inverted T waves in the left precordial leads, and left ventricular involvement. PMID: 23871674 In the context of data on PLN/SERCA interaction and on Ca(2+) accumulation in the sarcoplasmic reticulum the present results are consistent with the view that PLN channel activity could participate in the balancing of charge during Ca(2+) uptake. PMID: 23308118 The researchers found evidence of an association between the phospholamban R14del and the presence of dilated or arrhythmogenic cardiomyopathies in a group of patients. PMID: 22820313 1,014 patients with heart failure screened for mutations in PLN gene; identified 4 unrelated patients with PLN mutations, 3 in same amino acid residue (R9); conclude mutations in PLN gene are rare cause of heart failure, present almost exclusively in patients with dilated cardiomyopathy etiology; Arg9 and Leu39 residues are leading location of mutations described to date PMID: 22137083 human PLN-R14Del is misrouted to the sarcolemma, in the absence of endogenous PLN, and alters NKA activity, leading to cardiac remodeling. PMID: 22155237 Hydrophobic imbalance in the cytoplasmic domain of phospholamban is a determinant for lethal dilated cardiomyopathy. PMID: 22427649 TOAC spin labels placed on the WT-PLB transmembrane domain showed highly restricted motion with more than 100ns rotational correlation time (tau(c)); whereas the loop, and the cytoplasmic regions each consists of two distinct motional dynamics PMID: 22172806 Characterizing phospholamban to sarco(endo)plasmic reticulum Ca2+-ATPase 2a (SERCA2a) protein binding interactions in human cardiac sarcoplasmic reticulum vesicles using chemical cross-linking. PMID: 22247554 PLN generates canonical ion channel fluctuations with two conductance levels and a moderate cation selectivity PMID: 21687864 both topology and function of PLN are shaped by the interactions with lipids, which fine-tune the regulation of SERCA PMID: 21576492 PLN gene mutations were not found to be associated with HCM in the study group. PMID: 21332051 Lethal Arg9Cys phospholamban mutation hinders Ca2+-ATPase regulation and phosphorylation by protein kinase A. PMID: 21282613 Mutations in PLN are rare in frequency, yet the small size of the genetic locus may make it amenable to inclusion on HCM gene test panels. PMID: 21167350 In this study, they investigated the effects of PLB phosphorylation and mutation on the interaction between a PLB oligomer and SERCA in the context of 2D crystals. PMID: 21108950 Study conclude that PLN is enriched in the ER due to COP I-mediated transport that is dependent on its intact di-arginine motif and that the N-terminal di-arginine motif may act as a general ER retrieval sequence. PMID: 20634894 sarcolipin binds to phospholamban and inhibits polymerization PMID: 12032137 phosphorylation of phospholamban does not affect its structure and gives it more loose helical packing than if not phosphorylated PMID: 12080135 Modeling of the inhibitory interaction of phospholamban with the Ca2+ ATPase. PMID: 12525698 report that an inherited human dilated cardiomyopathy with refractory congestive heart failure is caused by a dominant Arg --> Cys missense mutation at residue 9 (R9C) in phospholamban PMID: 12610310 role in regulating sarco(endo)plasmic reticulum Ca2+-ATPase by binding to transmembrane helices in conjunction with sarcolipin PMID: 12692302 Mutation of the phospholamban promoter associated with hypertrophic cardiomyopathy. PMID: 12705874 SERCA2a and phospholamban bind to S100A1 in the human heart PMID: 12804600 The frequency-dependent phosphorylation of Ser16-PLB may favor an increase in Ca2+ transient and force generation in humans. PMID: 14530977 This study concludes that phospholamban (PLB) increases the maximal activity (Vmax) of calcium (Ca2+)-ATPase, and that the magnitude of this effect is sensitive to mutation. A region of mutant PLB responsible for this regulatory property is identified. PMID: 15736939 The unusual bellflower-like assembly is held together by leucine/isoleucine zipper motifs along the membrane-spanning helices. PMID: 16043693 the nonreversible superinhibitory function of mutant PLN-R14Del may lead to inherited dilated cardiomyopathy and premature death in both humans and mice PMID: 16432188

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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Recombinant Human Cardiac Phospholamban (PLN) Protein (GST)

Recombinant Human Cardiac Phospholamban (PLN) Protein (GST)

Product Overview

Target Details

FAQs