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anti-Human CLIP1 Antibodies:
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Human Polyclonal CLIP1 Primary Antibody for ELISA, WB - ABIN1002149
Bilbe, Delabie, Brüggen, Richener, Asselbergs, Cerletti, Sorg, Odink, Tarcsay, Wiesendanger: Restin: a novel intermediate filament-associated protein highly expressed in the Reed-Sternberg cells of Hodgkin's disease. in The EMBO journal 1992
Show all 3 Pubmed References
Human Polyclonal CLIP1 Primary Antibody for ChIP, IHC (p) - ABIN451789
Tanenbaum, Macůrek, Galjart, Medema: Dynein, Lis1 and CLIP-170 counteract Eg5-dependent centrosome separation during bipolar spindle assembly. in The EMBO journal 2008
finding that CLIP-170 has multiple non-CAP-Gly EB1-binding modules may explain why autoinhibition of CLIP-170 GAP-Gly domains does not fully abrogate its microtubule plus-end localization. This work expands our understanding of EB1-binding motifs and their multivalent networks.
we report an unexpected finding that CLIP170 negatively regulates TLR4 signaling by the targeted ubiquitination and degradation of TIRAP. Furthermore, we observed that CLIP170 expression is modulated by LPS to maintain the cellular homeostasis.
ASK1- induced phosphorylation of EB1 not only increases its plus end-tracking ability, but also promotes its recruitment of CLIP170 and p150glued to astral microtubules.
single-molecule fluorescence microscopy showed that the microtubule plus-end-associated protein CLIP-170 binds tightly to formins to accelerate actin filament elongation.
We find that LRRK1-mediated phosphorylation of CLIP-170 causes the accumulation of p150(Glued) (also known as DCTN1) a subunit of dynactin, at microtubule plus ends, thereby facilitating the migration of EGFR-containing endosomes.
herpesvirus particles are absolutely dependent on CLIP-170-mediated capture to initiate transport in primary human cells.
We show that AMPH-1/BIN1 binds to nesprin and actin, as well as to the microtubule-binding protein CLIP170 in both species. We propose that BIN1 has a direct and evolutionarily conserved role in nuclear positioning, altered in myopathies.
Restin inhibits epithelial-mesenchymal transition and tumor metastasis by controlling the expression of the tumor metastasis suppressor mir-200a/b via association with p73.
CLIP-170 tethers kinetochores to microtubule ends against the dynein-mediated poleward force to slide kinetochores along microtubules
A defect in the CLIP1 gene (CLIP-170) can cause autosomal recessive intellectual disability.
Data suggest that CLIP-170 acts as a novel recruiter and spatial regulator of PLK1 at kinetochores during early mitosis, promoting K-fiber stability and chromosome alignment for error-free chromosome segregation.
siRNA-mediated knockdown of the cytoplasmic linker protein compromised the assembly and branching of capillary-like blood vessels and neovascularization in vivo. It was critical for the motility abilities of HUVECs through its actions on cell polarity.
HDAC6 interacts with cytoplasmic linker protein 170 (CLIP-170) and that these two proteins function together to stimulate the migration of pancreatic cancer cells.
CLIP-170 phosphorylation by Plk1 regulates proper chromosome alignment
Depletion of CLIP-170 significantly impaired vascular endothelial tube formation and sprouting in vitro and inhibited breast tumor growth in mice by decreasing tumor vascularization.
We further demonstrate that this binding was prevented when the C-terminal tyrosine of EB1 was absent in the peptidic probes.
results suggest that EB1 and ClipCG12 act cooperatively to regulate microtubule dynamics (CLIP-170)
End-binding proteins interact with the CAP-Gly domains of CLIP-170 and p150(glued).
These results demonstrate that CLIP-170 mediates paclitaxel sensitivity in breast cancer via a microtubule-dependent mechanism.
Herein, the authors have identified polo-like kinase 1 (Plk1) and casein kinase 2 (CK2) as two kinases of CLIP-170 and mapped S195 and S1318 as their respective phosphorylation sites.
Drosophila CLIP-190 (and potentially also mouse CLIP-170) does not possess a significant role in the axon growth-promoting microtubule machinery.
Cytoplasmic linker protein 170 was ubiquitously expressed in mouse kidney, liver, lung, normal non-atherosclerotic aorta, and atherosclerotic aorta and was partly localized in the vascular endothelium.
Phosphorylation regulates CLIP-170 conformational changes resulting in its autoinhibition.
Restin expressed in vivo suppresses the growth of tumors in nude mice
CLIP170 is a key regulator of microtubule stabilization that is required for enhanced cell spreading and phagocytosis in activated macrophages.
Two +TIPs, CLIP-170 and end-binding protein 3 (EB3), turn over rapidly on MT ends. Diffusion of CLIP-170 and EB3 appears to be rate limiting for their binding to MT plus ends.
The protein encoded by this gene links endocytic vesicles to microtubules. This gene is highly expressed in Reed-Sternberg cells of Hodgkin disease. Several transcript variants encoding different isoforms have been found for this gene.
CAP-GLY domain containing linker protein 1
, CAP-Gly domain-containing linker protein 1
, CAP-Gly domain-containing linker protein 1-like
, cytoplasmic linker protein 1
, cytoplasmic linker protein 170 alpha-2
, cytoplasmic linker protein CLIP-170
, restin (Reed-Steinberg cell-expressed intermediate filament-associated protein)
, Clip 170
, Reed-Steinberg cell-espressed intermediate filament-associated protein
, cytoplasmic linker protein 50
, restin (Reed-Steinberg cell-espressed intermediate filament-associated protein)
, cytoplasmic linker protein 170