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anti-Human Transportin 1 Anticorps:
anti-Mouse (Murine) Transportin 1 Anticorps:
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Mouse (Murine) Monoclonal Transportin 1 Primary Antibody pour ICC, FACS - ABIN108620
Siomi, Eder, Kataoka, Wan, Liu, Dreyfuss: Transportin-mediated nuclear import of heterogeneous nuclear RNP proteins. dans The Journal of cell biology 1997
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Mouse (Murine) Monoclonal Transportin 1 Primary Antibody pour ICC, FACS - ABIN108619
Yu, Boyce, Wands, Bond, Bertozzi, Kohler: Metabolic labeling enables selective photocrosslinking of O-GlcNAc-modified proteins to their binding partners. dans Proceedings of the National Academy of Sciences of the United States of America 2012
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Cow (Bovine) Monoclonal Transportin 1 Primary Antibody pour CyTOF, FACS - ABIN269569
Kawamura, Tomozoe, Akagi, Kamei, Ochiai, Yamada: Identification of the nucleocytoplasmic shuttling sequence of heterogeneous nuclear ribonucleoprotein D-like protein JKTBP and its interaction with mRNA. dans The Journal of biological chemistry 2002
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TNPO1-mediated nuclear import may constitute a novel input pathway of how cellular redox state signals to the clock, since redox stress increases binding of TNPO1 to PER1 (Montrer PER1 Anticorps) and decreases its nuclear localization. TNPO1 is one of the novel players essential for normal circadian periods and potentially for redox regulation of the clock.
A molecular docking and dynamics study concluded that R521C and R521H mutations in FUS (Montrer FUS Anticorps) result in weak binding with Karyopherin-beta2 leading to amyotrophic lateral sclerosis.
Data suggest that micoRNA-128 targets the 3prime-untranslated region of nuclear import factor transportin 1 (TNPO1) mRNA.
the TNPO1-Rab8 (Montrer RAB8A Anticorps)-ciliary targeting signals complex mediates selective entry into and retention of cargos within cilia.
Together, these results indicate that transportin-1 mediates YB-1 (Montrer YBX1 Anticorps) nuclear translocation.
findings suggest that a new player, i.e., O-GlcNAcylation, regulates hnRNP A1 translocation and interaction with Trn1, possibly affecting its function
Importins, Impbeta, Kapbeta2, Imp4 (Montrer SPPL2B Anticorps), Imp5 (Montrer IPO5 Anticorps), Imp7 (Montrer IPO7 Anticorps), Imp9 (Montrer IPO9 Anticorps), and Impalpha, show the H3 tail binding more tightly than the H4 tail. The H3 tail binds Kapbeta2 and Imp5 (Montrer IPO5 Anticorps) with KD values of 77 and 57 nm, respectively, and binds the other five Importins more weakly.
Results show that Karyopherin-b2 binds to the N-terminal tail of histone H3 (Montrer HIST3H3 Anticorps) with high affinity even though H3 lacks a recognizable proline-tyrosine nuclear localization signal (PY-NLS (Montrer ALDH1A2 Anticorps)).
FGF2 (Montrer FGF2 Anticorps) nuclear translocation is regulated by Karyopherin-beta2 and Ran GTPase (Montrer RAN Anticorps) in human glioblastoma cells
Kapbeta2 interacts with ULK2 (Montrer ULK2 Anticorps) through ULK2 (Montrer ULK2 Anticorps)'s putative PY-NLS (Montrer ALDH1A2 Anticorps) motif, and facilitates transport from the cytoplasm to the nucleus, depending on its Ser1027 residue phosphorylation by PKA, thereby reducing autophagic activity.
Co-immunoprecipitation and affinity-binding studies revealed that Rab23 (Montrer RAB23 Anticorps) exists in a complex with Kif17 (Montrer KIF17 Anticorps) and importin b2 implying that Kif17 (Montrer KIF17 Anticorps) needs to bind to regulatory proteins like Rab23 (Montrer RAB23 Anticorps) for its ciliary transport
Association with Tnpo1 is necessary for Oxtr (Montrer OXTR Anticorps) nuclear localization. This is required for Oxt (Montrer OXT Anticorps)-induced osteoblast differentiation. osteoblast differentiation.
DJ-1 (Montrer PARK7 Anticorps) import is mediated by an oxidative stress-dependent interaction with karyopherin beta2.
Identification of a karyopherin beta1/beta2 proline-tyrosine nuclear localization signal in huntingtin (Montrer HTT Anticorps) protein.
Tnpo1 is involved in a variety of functions in the adult brain, including neurogenesis, cerebrospinal fluid production and sensing, and circadian rhythms.
Experiments in Xenopus assembly extracts with M9M, a superaffinity nuclear localization sequence that displaces cargoes bound by transportin, or TLB, a mutant transportin that can bind cargo and RanGTP simultaneously, support direct inhibition.
Results indicate that TRN1 positively regulates miRNA activity by promoting the association of miRNAs with AGO1 (Montrer EIF2C1 Anticorps), and they reveal opposing roles of two importin beta (Montrer KPNB1 Anticorps) family proteins in miRNA loading.
Results show that tranportin 1 (AtTRN1) recognizes a broad spectrum of proteins having diverse functions, which will potentially be the cargoes of AtTRN1.
This gene encodes the beta subunit of the karyopherin receptor complex which interacts with nuclear localization signals to target nuclear proteins to the nucleus. The karyopherin receptor complex is a heterodimer of an alpha subunit which recognizes the nuclear localization signal and a beta subunit which docks the complex at nucleoporins. Alternate splicing of this gene results in two transcript variants encoding different proteins.
M9 region interaction protein
, importin 2
, importin beta 2
, importin beta-2
, karyopherin (importin) beta 2
, karyopherin beta-2
, transportin 1