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PLN Antibody (N-term)

Purified Rabbit Polyclonal Antibody (Pab)

     
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  • 1 - PLN Antibody (N-term) AP20550a
    Western blot analysis of lysate from U266 cell line,using PLN Antibody (N-term)(Cat. #AP20550a).AP20550a was diluted at 1:1000 at each lane. A goat anti-rabbit IgG H&L(HRP) at 1:5000 dilution was used as the secondary antibody.Lysate at 35ug per lane.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession P26678
Reactivity Human, Rat, Mouse
Host Rabbit
Clonality Polyclonal
Isotype Rabbit IgG
Calculated MW 6109 Da
Additional Information
Gene ID 5350
Other Names Cardiac phospholamban, PLB, PLN, PLB
Target/Specificity This PLN antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 1-22 amino acids from the N-terminal region of human PLN.
Dilution WB~~1:1000
E~~Use at an assay dependent concentration.
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsPLN Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name PLN (HGNC:9080)
Synonyms PLB
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).
Cellular Location Endoplasmic reticulum membrane; Single-pass membrane protein. Sarcoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane {ECO:0000250|UniProtKB:A4IFH6}; Single-pass membrane protein. Membrane {ECO:0000250|UniProtKB:P61014}; Single-pass membrane protein. Note=Colocalizes with HAX1 at the endoplasmic reticulum (PubMed:17241641). Colocalizes with DMPK at the sarcoplasmic reticulum (PubMed:15598648).
Tissue Location Heart muscle (at protein level).
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

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.

REFERENCES

Fujii J.,et al.J. Biol. Chem. 266:11669-11675(1991).
Salvatore C.A.,et al.Submitted (MAR-1991) to the EMBL/GenBank/DDBJ databases.
McTiernan C.F.,et al.J. Mol. Cell. Cardiol. 31:679-692(1999).
Minamisawa S.,et al.Biochem. Biophys. Res. Commun. 304:1-4(2003).
Kaliman P.,et al.J. Biol. Chem. 280:8016-8021(2005).

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