Render Target: STATIC
Render Timestamp: 2024-12-30T11:25:30.941Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-09-30 01:58:15.157
Product last modified at: 2024-12-17T18:57:49.777Z
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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.

CLEC12A/CLL-1 (E5T5V) Rabbit mAb #57950

Filter:
  • WB
  • IP
  • F

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 55-75
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    • F-Flow Cytometry 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:100
    Flow Cytometry (Live) 1:200 - 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

    CLEC12A/CLL-1 (E5T5V) Rabbit mAb recognizes endogenous levels of total CLEC12A/CLL-1 protein.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human CLEC12A/CLL-1 protein.

    Background

    Part of the NK gene complex, C-type lectin-like molecule 1 (MICL/DCAL-2/CLL-1/CLEC12A) encodes a type-II transmembrane glycoprotein whose expression is largely restricted to hematopoietic cells of the myeloid lineage such as monocytes, macrophages, dendritic cells, and neutrophils (1-3). Research studies have shown that CLL-1 possesses a single C-type lectin-like domain within the extracellular domain and a single ITIM motif within its short cytoplasmic tail, which facilitates association with inhibitory SH2 domain-containing tyrosine phosphatases, SHP-1 and SHP-2. It is thought that signaling through the ITIM motif of CLL-1 facilitates inhibition of myeloid cell activation (1,2). By serving as a receptor for DAMPs that become exposed on dead cells, such as uric acid crystals, CLL-1 restrains pro-inflammatory immune responses that occur in response to cell death (4). In addition to being expressed on normal differentiated myeloid cells, research studies have also demonstrated expression of CLL-1 on the surface of malignant myeloid cells (5). As a result, CLL-1 has received significant attention as a potential novel therapeutic target for AML as its expression is absent from normal hematopoietic stem cells but is highly overexpressed on AML stem cells (5-9).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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