Render Target: STATIC
Render Timestamp: 2024-12-26T11:58:19.651Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-09-20 06:17:22.847
Product last modified at: 2024-08-02T07:06:04.012Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Phospho-LCP1 (Tyr28) Antibody #5277

Filter:
  • WB

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 70
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

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

    Protocol

    Specificity / Sensitivity

    Phospho-LCP1 (Tyr28) Antibody detects endogenous levels of LCP1 protein only when phosphorylated on Tyr28.

    Species Reactivity:

    Human

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr28 of human LCP1 protein. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    Highly conserved and widely expressed plastin proteins comprise a subset of actin-binding proteins that include proteins that promote actin bundling. Three plastins exhibiting differential expression are found in mammals and include L-plastin, T-plastin, and I-plastin. T-plastin (plastin-3) is found in cells of most solid tissues, while I-plastin (plastin-1) is expressed specifically in the kidney, colon, and small intestine (1-3). Research studies have shown that L-plastin (plastin-2) or lymphocyte cytosolic protein 1 (LCP1) is mainly expressed in hematopoietic cells and nonhematopoietic tumors, and increased expression correlates with metastatic progression in colon cancer cell lines (4). Investigators have found that overexpression of LCP1 in premetastatic cancer cell lines induces invasion and loss of E-cadherin expression, which is characteristic of metastatic cancer cell lines (5). LCP1 becomes phosphorylated at Ser5 upon stimulation through the T cell receptor/CD3 complex in association with the CD2 cell adhesion molecule or the CD28 receptor (6). Phosphorylation at Ser5 enhances the ability of LCP1 to bind to F-actin and increases cell motility (7,8).
    Phosphorylation of LCP1 on Tyr28 was identified at Cell Signaling Technology (CST) using PhosphoScan®, CST's LC-MS/MS platform for phosphorylation site discovery as well as other publications using MS technology (9). Phosphorylation of LCP1 at Tyr28 is seen in many leukemic cell lines (9-12).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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