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Human Polyclonal KLC1 Primary Antibody für FACS, IHC (p) - ABIN652577
Chernajovsky, Brown, Clark: Human kinesin light (beta) chain gene: DNA sequence and functional characterization of its promoter and first exon. in DNA and cell biology 1997
Show all 2 Pubmed References
structural plasticity of the N-terminal capping helix might represent a structural determinant for TPR domain structural versatility in cargo binding
All binary complexes (KLC1:APP (zeige APP Antikörper), KLC1:JIP1 (zeige MAPK8IP1 Antikörper), and APP:JIP1) contain conformations with favorable binding free energies indicating that KLC1 and JIP1 (zeige MAPK8IP1 Antikörper) may take part in APP (zeige APP Antikörper) transport in Alzheimer's disease patients.
BNIP-2 (zeige BNIP2 Antikörper) is a kinesin-1 adapter involved in vesicular transportation in the cytoplasm and that association with cargos depends on interaction of the CRAL-TRIO (zeige TRIO Antikörper) domain with membrane phosphatidylserine.
The G allele and GG genotype of KLC1 rs8702 were significantly over-represented among cataract patients, as compared to healthy controls, and were associated with an odds ratio for cataract development.
Dnm1L (zeige DNM1L Antikörper) interacts with KLC1 through the tetratricopeptide repeat domains.
Microtubule-bound kinesin-1 and kinesin-3 motor domains were visualized at multiple steps in their ATPase (zeige DNAH8 Antikörper) cycles--including their nucleotide-free states--at approximately 7 A resolution using cryo-electron microscopy.
Studies indicate that FEZ1 (fasciculation and elongation protein zeta 1 (zeige LZTS1 Antikörper)), SCOCO (short coiled-coil protein (zeige SCOC Antikörper)) and kinesins (kinesin heavy chain (zeige KIF5A Antikörper)) are involved in biological transport process.
The expression levels of KLC1 variant E in brain and lymphocytes were significantly higher in Alzheimer's disease patients.
study provides evidence that the combined effect of three variants within the KLC1 gene may predispose to age-related cataract.
For the binding of cargos shared by KLC1, we propose a different site located within the groove but not involving N343.
Phosphorylation of KLC1 at Thr466 increased in aged brains, and JIP1 (zeige MAPK8IP1 Antikörper) binding to kinesin-1 decreased, suggesting that APP (zeige APP Antikörper) transport is impaired by aging. Authors conclude that phosphorylation of KLC1 at Thr466 regulates the velocity of transport of APP (zeige APP Antikörper) by kinesin-1 by modulating its interaction with JIP1b.
In old mice, lack of KLC1 results in retinal pigment epithelium pathogenesis that was strikingly comparable to aspects of age-related macular degeneration.
Alcalpha (zeige CLSTN1 Antikörper) is efficiently processed in part to minimize the inappropriate peripheral retention of kinesin-1
A small peptide sequence is sufficient for initiating kinesin-1 activation through part of TPR (zeige GRID2 Antikörper) region of KLC1
Data show that amyloid precursor protein (APP (zeige APP Antikörper)) levels are well-correlated with the amount of the light chain of kinesin-1 (KLC1).
KLC1-ALK (zeige ALK Antikörper) is the first novel oncogenic fusion identified using only formalin-fixed paraffin-embedded tissue tissues
Phosphorylation of KLC1 at serine 460 modulates binding and trafficking of calsyntenin-1 (zeige CLSTN1 Antikörper).
changes in the phosphorylation state of KLC1 at Ser517/520 are unlikely to affect motor function.
An essential role of mNUDC for anterograde transport of dynein and dynactin (zeige DCTN1 Antikörper) by kinesin-1.
Impairment of anterograde transport by knockdown of KIF5B (zeige KIF5B Antikörper) or KLC1 delayed stress-granule dissolution.
Conventional kinesin is a tetrameric molecule composed of two heavy chains and two light chains, and transports various cargos along microtubules toward their plus ends. The heavy chains provide the motor activity, while the light chains bind to various cargos. This gene encodes a member of the kinesin light chain family. It associates with kinesin heavy chain through an N-terminal domain, and six tetratricopeptide repeat (TPR) motifs are thought to be involved in binding of cargos such as vesicles, mitochondria, and the Golgi complex. Thus, kinesin light chains function as adapter molecules and not motors per se. Although previously named 'kinesin 2', this gene is not a member of the kinesin-2 / kinesin heavy chain subfamily of kinesin motor proteins. Extensive alternative splicing produces isoforms with different C-termini that are proposed to bind to different cargos\; however, the full-length nature and/or biological validity of most of these variants have not been determined.
, kinesin light chain 1
, kinesin light chain 2
, kinesin light chain 4
, kinesin 2 60/70kDa
, kinesin ii
, KLC 1
, medulloblastoma antigen MU-MB-2.50