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LRSAM1 Antibody [K13D2]

Cat.No.: F7125

    Application: Reactivity:

    Usage Information

    Dilution
    1:1000
    Application
    WB
    Reactivity
    Human, Mouse, Rat, Monkey
    Source
    Rabbit Monoclonal Antibody
    Storage Buffer
    PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3
    Storage (from the date of receipt)
    -20°C (avoid freeze-thaw cycles), 2 years
    Predicted MW
    84 kDa
    Positive Control A-431 cells; MCF7 cells; 786-0 cells; CCRF-CEM cells; RPMI 8226 cells; PC-3 ells; Hepa 1-6 cells; H-4-II-E cells; COS-7 cells
    Negative Control

    Datasheet & SDS

    Biological Description

    Specificity
    LRSAM1 (D1O5S) Rabbit mAb detects endogenous levels of total LRSAM1 protein.
    Clone
    K13D2
    Synonym(s)
    E3 ubiquitin-protein ligase LRSAM1; Leucine-rich repeat and sterile alpha motif-containing protein 1; RING-type E3 ubiquitin transferase LRSAM1; Tsg101-associated ligase; hTAL; LRSAM1; TAL
    Background
    LRSAM1, also known as Leucine-rich repeat and sterile alpha motif-containing 1 or hTALL, is an E3 ubiquitin ligase from the RING finger family that regulates protein ubiquitination for intracellular trafficking, bacterial clearance, and neuronal integrity. This protein, about 750 amino acids long, has N-terminal leucine-rich repeats for recognizing substrates and cytosolic bacteria, an ERM domain for cytoskeletal interactions, a coiled-coil region, a SAM domain that enables self-association and interactions with partner proteins, and a C-terminal RING domain with key cysteine and histidine residues that catalyzes both mono- and polyubiquitination. LRSAM1’s main function is to use its leucine-rich repeats to identify invading cytosolic bacteria like Salmonella, then trigger RING-dependent ubiquitination of the ESCRT-I component TSG101, which disrupts endosomal sorting, promotes epidermal growth factor receptor accumulation, and aids in xenophagy by recruiting autophagic adaptors for the lysosomal degradation of pathogens. It also ubiquitinates specific lysines in TSG101’s stability box, influencing endolysosomal trafficking and proteasomal degradation, and self-ubiquitinates through interactions between its SAM and RING domains to regulate its own activity. LRSAM1 is crucial for maintaining axonal integrity and membrane dynamics, and mutations, especially in the RING or leucine-rich repeat domains, impair its ubiquitination function, leading to Charcot-Marie-Tooth disease type 2P, which is characterized by peripheral axonal neuropathy.
    References
    • https://pubmed.ncbi.nlm.nih.gov/30826859/
    • https://pubmed.ncbi.nlm.nih.gov/23245317/

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