Render Target: STATIC
Render Timestamp: 2024-12-13T12:16:11.116Z
Commit: 611277b6de3cd1bb065350b6ef8d63df412b7185
XML generation date: 2024-04-05 20:25:54.176
Product last modified at: 2024-06-27T13:36:16.911Z
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PDP - Template Name: Blocking Peptide
PDP - Template ID: *******6db2f4c

Phospho-Met (Tyr1234/1235) Blocking Peptide #1645

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Important Ordering Details

Custom Ordering Details: This product is assembled upon order. Please allow two-four weeks for your product to be processed.

    Product Information

    Product Usage Information

    Use as a blocking reagent to evaluate the specificity of antibody reactivity in western and dot blot protocols.

    Storage

    Supplied in 20 mM potassium phosphate (pH 7.0), 50 mM NaCl, 0.1 mM EDTA, 1 mg/ml BSA and 5% glycerol. 1% DMSO. Store at –20°C.

    Product Description

    This peptide is used to block Phospho-Met (Tyr1234/1235) (D26) Rabbit mAb #3077 reactivity in western and dot blot protocols.

    Quality Control

    The quality of the peptide was evaluated by reversed-phase HPLC and by mass spectrometry. The peptide blocks Phospho-Met (Tyr1234/1235) (D26) Rabbit mAb #3077 signal in western blotting and dot blot.

    Background

    Met, a high affinity tyrosine kinase receptor for hepatocyte growth factor (HGF, also known as scatter factor) is a disulfide-linked heterodimer made of 45 kDa α- and 145 kDa β-subunits (1,2). The α-subunit and the amino-terminal region of the β-subunit form the extracellular domain. The remainder of the β-chain spans the plasma membrane and contains a cytoplasmic region with tyrosine kinase activity. Interaction of Met with HGF results in autophosphorylation at multiple tyrosines, which recruit several downstream signaling components, including Gab1, c-Cbl, and PI3 kinase (3). These fundamental events are important for all of the biological functions involving Met kinase activity. The addition of a phosphate at cytoplasmic Tyr1003 is essential for Met protein ubiquitination and degradation (4). Phosphorylation at Tyr1234/1235 in the Met kinase domain is critical for kinase activation. Phosphorylation at Tyr1349 in the Met cytoplasmic domain provides a direct binding site for Gab1 (5). Research studies have shown that altered Met levels and/or tyrosine kinase activities are found in several types of tumors, including renal, colon, and breast. Thus, investigators have concluded that Met is an attractive potential cancer therapeutic and diagnostic target (6,7).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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