Western blot analysis of Beta Actin was performed by loading 20ug of the indicated whole cell lysates and 10ul PageRuler Plus Prestained Protein Ladder (Product # 26619) per well onto a 4-20% Tris-Glycine polyacrylamide gel. Proteins were transferred to a nitrocellulose membrane using the G2 Fast Blotter (Product # 62288) and blocked with 5% Milk/TBST for at least 1 hour at room temperature. Beta-Actin was detected at 42kD using a Beta Actin mouse monoclonal antibody (Product # MA5-15739) at a dilution of 1:500 in blocking buffer overnight at 4°C on a rocking platform, followed by a goat anti-Mouse IgG-HRP secondary antibody (Product # G21040) at a dilution of 1:2,000 for at least 1 hour. Chemiluminescent detection was performed using SuperSignal West Pico (Product # 34078).
|Tested species reactivity||Rat|
|Host / Isotype||Mouse / IgG1|
|Immunogen||60 kDa disulfide linked homodimer NKR-P1|
|Storage buffer||PBS with 4-5mg/ml BSA|
|Contains||0.02% sodium azide|
|Storage Conditions||Store at 4°C short term. For long term storage, store at -20°C, avoiding freeze/thaw cycles.|
|Tested Applications||Dilution *|
|Flow Cytometry (Flow)||Assay Dependent|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
MA5-17539 targets NK cells/NKR-P1 in FACS applications and shows reactivity with Rat samples.
The MA5-17539 immunogen is 60 kDa disulfide linked homodimer NKR-P1.
Natural killer (NK) cells are lymphocytes that mediate cytotoxicity and secrete cytokines after immune stimulation. Several genes of the C-type lectin superfamily, including the rodent NKRP1 family of glycoproteins, are expressed by NK cells and may be involved in the regulation of NK cell function. The KLRB1 protein contains an extracellular domain with several motifs characteristic of C-type lectins, a transmembrane domain, and a cytoplasmic domain. The KLRB1 protein is classified as a type II membrane protein because it has an external C terminus.
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