Render Target: STATIC
Render Timestamp: 2024-11-01T09:41:10.152Z
Commit: 23cb9f61fe67e1e9093fd644a533c4ff516a6463
XML generation date: 2024-09-30 01:54:11.402
Product last modified at: 2024-09-30T08:02:10.145Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

LAMTOR5/HBXIP (D4V4S) Rabbit mAb #14633

Filter:
  • WB
  • IP
  • IHC

    Supporting Data

    REACTIVITY H M R Mk
    SENSITIVITY Endogenous
    MW (kDa) 10.5
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    • IHC-Immunohistochemistry 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 
    • Mk-Monkey 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:50
    Immunohistochemistry (Paraffin) 1:800

    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

    LAMTOR5/HBXIP (D4V4S) Rabbit mAb recognizes endogenous levels of total LAMTOR5/HBXIP protein.

    Species Reactivity:

    Human, Mouse, Rat, Monkey

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu55 of human LAMTOR5/HBXIP protein.

    Background

    Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5 (LAMTOR5) is an essential component of the ragulator protein complex that is encoded by the HBXIP gene (1). The ragulator complex also includes LAMTOR1/C11orf59, LAMTOR2/ROBLD3, LAMTOR3/MAPKSP1, and LAMTOR4/C7orf59 (1,2). Research studies demonstrate that the ragulator complex localizes to the lysosomal membrane and is essential for the lysosomal localization of Rag GTPases and mTORC1 as well as the subsequent activation of mTORC1 in response to amino acid signaling (1-3). Additional research studies indicate that HBXIP regulates hepatitis B virus x (HBx) protein activity and is a transcription coactivator involved in the proliferation and migration of breast cancer cells (4,5).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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