ST1200
Anti-Ubiquitin Mouse mAb (FK2)
liquid, clone FK2, Calbiochem®
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About This Item
UNSPSC Code:
12352203
Recommended Products
biological source
mouse
Quality Level
antibody form
unpurified
antibody product type
primary antibodies
clone
FK2, monoclonal
form
liquid
contains
≤0.1% sodium azide as preservative
species reactivity (predicted by homology)
all
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
avoid repeated freeze/thaw cycles
isotype
IgG1
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
General description
Mouse monoclonal antibody generated by immunizing Balb/c mice with the specified immunogen and fusing splenocytes with myeloma cells. Recognizes K29-, K48-, and K63-linked polyubiquitinylated and monoubiquitinylated proteins.
Recognizes K29-, K48-, and K63-linked polyubiquitinylated and monoubiquitinylated proteins, but not free ubiquitin, in Raji cells.
This Anti-Ubiquitin Mouse mAb (FK2) is validated for use in ELISA, Immunoblotting, Immunoprecipitation, Immunofluorescence for the detection of Ubiquitin.
Immunogen
human
unpurified polyubiquitinylated lysozyme
Application
ELISA (see application references)
Immunoblotting (1:1000)
Immunoprecipitation (see application references and comments)
Immunofluorescence (see application references)
Packaging
Please refer to vial label for lot-specific concentration.
Warning
Toxicity: Standard Handling (A)
Physical form
In PBS.
Preparation Note
Raji cells
Reconstitution
Following initial thaw, aliquot and freeze (-20°C). Store diluted antibody at 4°C for up to 1 month.
Other Notes
Does not recognize free ubiquitin. For immunoprecipitation, once the antibody is immobilized, it demonstrates affinity for free ubiquitin as well as for poly- and monoubiquitinylated proteins. Antibody should be titrated for optimal results in individual systems.
Matsumoto, M., et al. 2005. Proteomics 5, 4545.
Boname, J.N., et al. 2001. Immunity 15, 627.
Campbell, V., et al. 2001. Neuron 32, 1013.
Fujimuro, M., et al. 2003. FEBS Letts. 349, 173.
Boname, J.N., et al. 2001. Immunity 15, 627.
Campbell, V., et al. 2001. Neuron 32, 1013.
Fujimuro, M., et al. 2003. FEBS Letts. 349, 173.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
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Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Yin Wu et al.
The Journal of biological chemistry, 291(23), 12370-12382 (2016-04-30)
Sepsis is one of the leading causes of death worldwide. Although the prevailing theory for the sepsis syndrome is a condition of uncontrolled inflammation in response to infection, sepsis is increasingly being recognized as an immunosuppressive state known as endotoxin
Amijai Saragovi et al.
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Systemic oxygen restriction (SOR) is prevalent in numerous clinical conditions, including chronic obstructive pulmonary disease (COPD), and is associated with increased susceptibility to viral infections. However, the influence of SOR on T cell immunity remains uncharacterized. Here we show the
Tapas Mukherjee et al.
The Journal of biological chemistry, 296, 100050-100050 (2020-11-11)
Large cytosolic protein aggregates are removed by two main cellular processes, autophagy and the ubiquitin-proteasome system, and defective clearance of these protein aggregates results in proteotoxicity and cell death. Recently, we found that the eIF2α kinase heme-regulated inhibitory (HRI) induced
Angelica Ortiz et al.
Cancer cell, 35(1), 33-45 (2019-01-16)
Tumor-derived extracellular vesicles (TEV) "educate" healthy cells to promote metastases. We found that melanoma TEV downregulated type I interferon (IFN) receptor and expression of IFN-inducible cholesterol 25-hydroxylase (CH25H). CH25H produces 25-hydroxycholesterol, which inhibited TEV uptake. Low CH25H levels in leukocytes
Katrin Stuber et al.
Nature communications, 12(1), 5939-5939 (2021-10-14)
Ubiquitin (Ub) and Ub-like proteins (Ubls) such as NEDD8 are best known for their function as covalent modifiers of other proteins but they are also themselves subject to post-translational modifications including phosphorylation. While functions of phosphorylated Ub (pUb) have been
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