SAB3500022
Anti-CEP164 antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
Synonym(s):
Anti-Centrosomal protein 164
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About This Item
UNSPSC Code:
12352203
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
species reactivity
mouse, human, rat
technique(s)
immunohistochemistry: suitable
indirect ELISA: suitable
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
Gene Information
human ... CEP164(22897)
Immunogen
CEP164 antibody was raised against an 18 amino acid peptide near the amino terminus of human CEP164.
Application
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunofluorescence (1 paper)
Immunofluorescence (1 paper)
Features and Benefits
Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.
Target description
CEP164 was initially identified as a centrosomal protein, but other studies have indicated that it also plays a role in the formation of primary cilia, the microtubule-based sensory antennae projecting from the surface of many eukaryotic cells as well as in DNA damage response acting as a mediator protein. CEP164 interacts with both ATR and ATM, proteins that trigger a number of cellular responses including the initiation of DNA damaged-induced cell cycle checkpoints. It is phosphorylated upon replication stress, ultraviolet (UV) radiation, and ionizing radiation; silencing of CEP164 significantly reduces the DNA damage-induced phosphorylation of several proteins in the DNA damage-activated signaling cascade and compromises cell survival after UV damage. At least two isoforms of CEP164 are known to exist.
Linkage
The action of this antibody can be blocked using blocking peptide SBP3500022.
Physical form
Supplied at approx. 1 mg/mL in phosphate buffered saline containing 0.02% 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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Product No.
Description
Pricing
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
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Chengbing Wang et al.
The Journal of biological chemistry, 288(41), 29518-29529 (2013-08-21)
The primary cilium is required for Hedgehog signaling. So far, all known ciliogenic proteins regulate Hedgehog signaling through their role in ciliogenesis. Here we show that the mouse DZIP1 regulates Hedgehog signaling through two mechanisms. First, DZIP1 interacts with GLI3
Claudio R Cortés et al.
Scientific reports, 6, 24083-24083 (2016-04-21)
Ciliopathies are a group of genetic disorders caused by defective assembly or dysfunction of the primary cilium, a microtubule-based cellular organelle that plays a key role in developmental signalling. Ciliopathies are clinically grouped in a large number of overlapping disorders
Hao Yan et al.
Nature communications, 11(1), 2196-2196 (2020-05-06)
Transition fibers (TFs) regulate cilia gating and make the primary cilium a distinct functional entity. However, molecular insights into the biogenesis of a functional cilia gate remain elusive. In a forward genetic screen in Caenorhabditis elegans, we uncover that TALP-3
Hao Lu et al.
Nature genetics, 49(7), 1025-1034 (2017-05-23)
Autosomal recessive polycystic kidney disease (ARPKD), usually considered to be a genetically homogeneous disease caused by mutations in PKHD1, has been associated with ciliary dysfunction. Here, we describe mutations in DZIP1L, which encodes DAZ interacting protein 1-like, in patients with
Chuan Chen et al.
Science advances, 7(26) (2021-06-25)
Mutation of ciliopathy protein HYLS1 causes the perinatal lethal hydrolethalus syndrome (HLS), yet the underlying molecular etiology and pathogenesis remain elusive. Here, we reveal unexpected mechanistic insights into the role of mammalian HYLS1 in regulating primary cilia. HYLS1 is recruited
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