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anti-Human BICD2 Antibodies:
anti-Mouse (Murine) BICD2 Antibodies:
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Human Polyclonal BICD2 Primary Antibody for WB - ABIN541735
Hoogenraad, Akhmanova, Howell, Dortland, De Zeeuw, Willemsen, Visser, Grosveld, Galjart: Mammalian Golgi-associated Bicaudal-D2 functions in the dynein-dynactin pathway by interacting with these complexes. in The EMBO journal 2001
Show all 3 Pubmed References
Human Polyclonal BICD2 Primary Antibody for WB - ABIN541736
Holland, Milne, Garka, Johnson, Willis, Sims, Rauch, Bird, Virca: Purification, cloning, and characterization of Nek8, a novel NIMA-related kinase, and its candidate substrate Bicd2. in The Journal of biological chemistry 2002
Show all 3 Pubmed References
Human Polyclonal BICD2 Primary Antibody for IHC, IHC (p) - ABIN4284611
Terenzio, Golding, Russell, Wicher, Rosewell, Spencer-Dene, Ish-Horowicz, Schiavo: Bicaudal-D1 regulates the intracellular sorting and signalling of neurotrophin receptors. in The EMBO journal 2014
Human Polyclonal BICD2 Primary Antibody for ICC, IF - ABIN4284610
Lee, Jung, Oh, Choi, Chae, Kim, Lim, Kim, Lee, Seong, Han: BICD1 mediates HIF1α nuclear translocation in mesenchymal stem cells during hypoxia adaptation. in Cell death and differentiation 2018
Results provide evidence that BICD2 is a capsid-associated dynein adaptor utilized by HIV-1 for transport to the nucleus.
BICD2 mutations appear rather unlikely to cause a phenotype of hereditary motor and sensory neuropathy and are a very rare cause of the hereditary spastic paraplegia phenotype
A family with three members affected by spinal muscular dystrophy 2, caused by the first in-frame deletion of BICD2 is described.
our findings contribute to the better understanding of spinal muscular atrophy-2 pathology by providing evidence for a common pathomechanism of BICD2 mutations that increase microtubule stability in motor neurons leading to increased axonal branching and to impaired neuromuscular junction development.
BICD2 facilitates infection by promoting the trafficking of viral cores to the nucleus, thereby promoting nuclear entry of the viral genome and infection
BICD2 missense mutations were identified in patients with severe muscular atrophy with arthrogryposis and asymptomatic individuals with subclinical features.
Data suggest that BICD1 and BICD2 are highly expressed in the nervous system during development and are important in neuronal homeostasis. [REVIEW]
results reveal that dominant mutations in BICD2 hyperactivate DDB motility and suggest that an imbalance of minus versus plus end-directed microtubule motility in neurons may underlie spinal muscular atrophy.
These findings give further insight into the clinical and pathoanatomical consequences of BICD2 mutations.
several analyses of vesicular transport demonstrated that Rab6A and BICD2 play crucial roles in Golgi tubule fusion with the endoplasmic reticulum (ER) in brefeldin A (BFA)-treated cells
the features of BICD2 spinal muscular atrophy, lower extremity predominant are consistent with a pathological process that preferentially affects lumbar lower motor neurons
This study identified BICD3 significantly associated loci with a biologically plausible role in schizophrenia.
Mutations in BICD2 cause congenital autosomal-dominant spinal muscular atrophy and massive Golgi fragmentation in affected cells.
BICD2 mutations cause non-5q linked spinal muscular atrophy in humans
Disease causing mutations resulting in amino acid substitutions in two binding regions of BICD2 increase its binding affinity for the cytoplasmic dynein-dynactin complex.
Data suggest that ASUN promotes perinuclear enrichment of dynein at G2/M that facilitates BICD2- and CENP-F-mediated anchoring of dynein to nuclear pore complexes.
isolation, cloning, and characterization of human Nek8, a new mammalian NIMA-related kinase, and its candidate substrate Bicd2
Data suggest that binding of Lis1 to DDB complex does not strongly disrupt processive motility along microtubules; motile DDB complex binds up to two Lis1 dimers; mutational analysis suggested that Lis1 binds directly to the dynein motor domains during DDB complex movement. (Lis1 = lissencephaly 1 protein; DDB complex = dynein-dynactin-BicD2 complex; BicD2 = bicaudal D homolog 2 protein)
Data indicate that Bicaudal-D2 (BICD2)-deficient mice develop disrupted laminar organization of cerebral cortex and the cerebellum, pointing to impaired radial neuronal migration.
LIS1 is required for dynein-mediated transport induced by membrane tethering of BICD2-N and LIS1 contributes to dynein accumulation at microtubule plus ends and BICD2-positive cellular structures.
BICD2-N transgene increased lifespan in 'low copy' SOD1-G93A ALS transgenic mice.
This gene is one of two human homologs of Drosophila bicaudal-D and a member of the Bicoid family. It has been implicated in dynein-mediated, minus end-directed motility along microtubules. It has also been reported to be a phosphorylation target of NIMA related kinase 8. Two alternative splice variants have been described.
, coiled-coil protein BICD2
, cytoskeleton-like bicaudal D protein homolog 2
, homolog of Drosophila bicaudal D
, protein bicaudal D homolog 2
, bicaudal D homolog 2
, bicaudal D protein
, bicaudal D homolog 2 (Drosophila)
, protein bicaudal D homolog 2-like