抗Human Transportin 1 抗体:
抗Mouse (Murine) Transportin 1 抗体:
抗Rat (Rattus) Transportin 1 抗体:
Mouse (Murine) Monoclonal Transportin 1 Primary Antibody for ICC, FACS - ABIN108619
Siomi, Eder, Kataoka, Wan, Liu, Dreyfuss: Transportin-mediated nuclear import of heterogeneous nuclear RNP proteins. in The Journal of cell biology 1997
Show all 7 Pubmed References
Mouse (Murine) Monoclonal Transportin 1 Primary Antibody for ICC, FACS - ABIN108620
Yu, Boyce, Wands, Bond, Bertozzi, Kohler: Metabolic labeling enables selective photocrosslinking of O-GlcNAc-modified proteins to their binding partners. in Proceedings of the National Academy of Sciences of the United States of America 2012
Show all 7 Pubmed References
Cow (Bovine) Monoclonal Transportin 1 Primary Antibody for 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. in The Journal of biological chemistry 2002
Show all 5 Pubmed References
Human Polyclonal Transportin 1 Primary Antibody for IHC (p), WB - ABIN541593
Cheng, Zhang, Kim, Zhao, Zhao, Su: Mip1, an MEKK2-interacting protein, controls MEKK2 dimerization and activation. in Molecular and cellular biology 2005
Show all 3 Pubmed References
Human Polyclonal Transportin 1 Primary Antibody for IHC (p), WB - ABIN541594
Schroder, Cloonan, Bushell, Sculley: Alternative polyadenylation and splicing of mRNAs transcribed from the human Sin1 gene. in Gene 2004
Show all 3 Pubmed References
Transportin 1, a member of the importin-beta family proteins, binds to a PY-NLS(2) sequence motif close to the amino terminus of matrix protein (M1) exposed during acid priming of the viral core.
high-affinity binding of karyopherin-beta2 to the FUS C-terminal proline-tyrosine nuclear localization signal tethers the proteins together, allowing multiple, distributed weak intermolecular contacts to disrupt FUS self-association, blocking liquid-liquid phase separation
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 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 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-ciliary targeting signals complex mediates selective entry into and retention of cargos within cilia.
Together, these results indicate that transportin-1 mediates YB-1 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, Imp5, Imp7, Imp9, and Impalpha, show the H3 tail binding more tightly than the H4 tail. The H3 tail binds Kapbeta2 and Imp5 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 with high affinity even though H3 lacks a recognizable proline-tyrosine nuclear localization signal (PY-NLS).
FGF2 nuclear translocation is regulated by Karyopherin-beta2 and Ran GTPase in human glioblastoma cells
Kapbeta2 interacts with ULK2 through ULK2's putative PY-NLS motif, and facilitates transport from the cytoplasm to the nucleus, depending on its Ser1027 residue phosphorylation by PKA, thereby reducing autophagic activity.
Studies indicate potential roles of Tranportin-1 and Transportin-2 beyond protein nuclear import.
ADAR1 carries a unique nuclear localization signal (NLS) that overlaps one of its double-stranded RNA-binding domains (dsRBDs). This dsRBD-NLS is recognized by nuclear import receptor transportin 1 (also called karyopherin-beta2) in an RNA-sensitive manner.
Data suggest the C-terminal nuclear localization domain (QYP) is critical for RAM (RNMT-activating mini protein) to enter the cell nucleus where RAM activates RNMT resulting in mRNA cap methylation; TNPO1/TNPO2 mediate RAM nuclear entry.
C-terminal FUS mutations prevent TNPO 1 binding to the NLS, inhibiting nuclear import and promoting cytoplasmic aggregation. The presence of TNPO 1 in wild-type FUS aggregates in frontotemporal lobar degeneration-FUS distinguishes it from ALS.
Crystal structure of human Karyopherin beta2 bound to the PY-NLS of Saccharomyces cerevisiae Nab2
The crystal structure of the FUS-NLS/Trn1 complex shows extensive contacts between the two proteins and a unique alpha-helical structure in the FUS-NLS.
Disulfide formation with transportin-1 is required for nuclear localization and the activation of FOXO4 induced by reactive oxygen species.
In case of L7, importin beta2 or importin beta3 are preferentially used by clusters with a high import efficiency.
Co-immunoprecipitation and affinity-binding studies revealed that Rab23 exists in a complex with Kif17 and importin b2 implying that Kif17 needs to bind to regulatory proteins like Rab23 for its ciliary transport
Association with Tnpo1 is necessary for Oxtr nuclear localization. This is required for Oxt-induced osteoblast differentiation. osteoblast differentiation.
DJ-1 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 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, and they reveal opposing roles of two importin beta 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