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Human Polyclonal KLC1 Primary Antibody for 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 (show APP Antibodies), KLC1:JIP1 (show MAPK8IP1 Antibodies), and APP:JIP1) contain conformations with favorable binding free energies indicating that KLC1 and JIP1 (show MAPK8IP1 Antibodies) may take part in APP (show APP Antibodies) transport in Alzheimer's disease patients.
BNIP-2 (show BNIP2 Antibodies) is a kinesin-1 adapter involved in vesicular transportation in the cytoplasm and that association with cargos depends on interaction of the CRAL-TRIO (show TRIO Antibodies) 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 (show DNM1L Antibodies) 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 (show DNAH8 Antibodies) 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 (show LZTS1 Antibodies)), SCOCO (short coiled-coil protein (show SCOC Antibodies)) and kinesins (kinesin heavy chain (show KIF5A Antibodies)) 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.
In old mice, lack of KLC1 results in retinal pigment epithelium pathogenesis that was strikingly comparable to aspects of age-related macular degeneration.
Alcalpha (show CLSTN1 Antibodies) 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 (show GRID2 Antibodies) region of KLC1
Data show that amyloid precursor protein (APP (show APP Antibodies)) levels are well-correlated with the amount of the light chain of kinesin-1 (KLC1).
KLC1-ALK (show ALK Antibodies) 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 (show CLSTN1 Antibodies).
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 (show DCTN1 Antibodies) by kinesin-1.
Impairment of anterograde transport by knockdown of KIF5B (show KIF5B Antibodies) or KLC1 delayed stress-granule dissolution.
analysis of a novel protein-protein interaction between KLC1 and JLP that involves leucine zipper-like domains
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