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Render Timestamp: 2024-12-20T12:02:17.813Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-09-30 01:59:23.443
Product last modified at: 2024-09-30T08:01:03.283Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
  1. Products /
  2. Primary Antibodies /
  3. PYGL (E4O1P) Rabbit mAb
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

PYGL (E4O1P) Rabbit mAb #42103

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H M
    SENSITIVITY Endogenous
    MW (kDa) 97
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:200

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    PYGL (E4O1P) Rabbit mAb recognizes endogenous levels of total PYGL protein. This antibody does not cross-react with PYGB or PYGM.

    Species Reactivity:

    Human, Mouse

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Asn839 of human PYGL protein.

    Background

    Glycogen phosphorylases constitute a family of metabolic enzymes that catalyze the rate-limiting step in the release of glucose-1-phosphate (G1P) from tissue glycogen stores (1,2). There are three distinct glycogen phosphorylases in vertebrates, encoded by distinct genes and characterized primarily by the tissues in which they are predominantly expressed: PYGL (liver form), PYGB (brain form), and PYGM (muscle form). All three forms are expressed as inactive monomers, which require homodimerization and site-specific phosphorylation for activation, with additional regulation possible via other post-translational modifications such as O-GlycNAcylation (3). Due to their critical role in regulating glycogen catabolism, mutations or other perturbations that impact glycogen phosphorylase activity have been identified as contributing factors to metabolic diseases (e.g., glycogen storage diseases) and other diseases with metabolic dependencies, including cancer (4,5). While PYGL is expressed predominantly in the liver, it is understood to regulate systemic (blood) glucose levels via the catabolism of liver glycogen stores, whereas PYGB and PYGM regulate glycogen metabolism specifically within brain and skeletal muscle tissues, respectively (6,7).

    Database Links

    UniProt ID: P06737


    Entrez-Gene Id: 5836


    Limited Uses

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