M6697
Anti-MLKL (58-70) antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
Synonym(s):
Anti-mixed lineage kinase domain-like (Homo sapiens)
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
Recommended Products
biological source
rabbit
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~54 kDa
species reactivity
human
technique(s)
western blot: 1:250-1:500
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... MLKL(197259)
General description
MLKL (mixed lineage kinase domain-like) is a protein that belongs to the protein kinase superfamily. It facilitates necrosis signaling downstream of the kinase RIP3 (receptor-interacting serine-threonine kinase 3) . Anti-MLKL (58-70) antibody can be used in western blotting. Rabbit anti- MLKL (58-70) antibody reacts specifically with MLKL protein.
MLKL is encoded by the gene mapped to human chromosome 16q23. Activated MLKL is localized on the cell membrane.
Immunogen
synthetic peptide corresponding to amino acids 58-70 of human MLKL.
Application
Anti-MLKL (58-70) antibody produced in rabbit has been used in western blotting.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunocytochemistry (1 paper)
Immunocytochemistry (1 paper)
Yale Center for High Throughput Cell Biology IF-tested antibodies. Each antibody is tested by immunofluorescence against HUVEC cells using the Yale HTCB IF protocol. To learn more about us and Yale Center for High Throughput Cell Biology partnership, visit sigma.com/htcb-if.
western blot: 1:250-1:500
Biochem/physiol Actions
Mixed lineage kinase domain-like protein (MLKL) primarily causes receptor-interacting protein (RIP) kinase-dependent necroptosis. However, during hepatitis, it results in programmed hepatocellular necrosis, which is independent of RIPK3. MLKL also participates in endosomal trafficking and in the formation of extracellular vesicles.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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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Sara R Oliveira et al.
Cell death discovery, 4, 10-10 (2018-08-01)
Necroptosis is a regulated form of necrosis, which may be critical in the pathogenesis of neurodegenerative diseases. Neuroinflammation, characterized by the activation of glial cells such as microglia, is closely linked with neurodegenerative pathways and constitutes a major mechanism of
Characterization of RIPK3-mediated phosphorylation of the activation loop of MLKL during necroptosis.
Rodriguez DA, et al.
Cell Death and Differentiation, 23(1), 76-76 (2016)
Tommaso Selmi et al.
BMC cancer, 15, 357-357 (2015-05-06)
ZFP36 is an mRNA binding protein that exerts anti-tumor activity in glioblastoma by triggering cell death, associated to an increase in the stability of the kinase RIP1. We used cell death assays, size exclusion chromatography, Co-Immunoprecipitation, shRNA lentivectors and glioma
ZFP36 stabilizes RIP1 via degradation of XIAP and cIAP2 thereby promoting ripoptosome assembly.
Selmi T, et al.
BMC Cancer, 15(1), 357-357 (2015)
MLKL activation triggers NLRP3-mediated processing and release of IL-β independently of gasdermin-D
Gutierrez KD, et al.
Journal of Immunology, 47(1), 1601757-1601757 (2017)
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