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UNC13B is expressed in the kidney cortical epithelial cells and is upregulated by hyperglycemia. Additionally we are shipping Unc-13 Homolog B (C. Elegans) Antibodies (82) and and many more products for this protein.
The 1-5-8-26 CaM (show CALM1 ELISA Kits) binding motif discovered in Munc13-1 (show UNC13A ELISA Kits) cannot be induced in the classical CaM (show CALM1 ELISA Kits) target skMLCK (show MYLK2 ELISA Kits), indicating unique features of the Munc13 CaM (show CALM1 ELISA Kits) binding motif.
Munc13-1 (show UNC13A ELISA Kits) regulates insulin (show INS ELISA Kits) exocytosis
MUNC13-4 (show UNC13D ELISA Kits) mutations play a role in the development of familial haemophagocytic lymphohistiocytosis subtype 3 through a defective cytotoxic pathway
Data suggest that diacylglycerol-activated hmunc13 serves as an effector of Rab34 (show RAB34 ELISA Kits), mediating lysosome-Golgi trafficking.
Data identified a polymorphism in the UNC13B gene associated with nephropathy. UNC13B mediates apopotosis in glomerular cells in the presence of hyperglycemia, an event occurring early in the development of nephropathy.
In the bound state, the hydrophobic anchor residue of the calmodulin (CaM (show CALM1 ELISA Kits))-binding motif in Munc13 contacts two distinct methionine residues in the carboxyl-terminal domain of CaM (show CALM1 ELISA Kits).
mechanistic basis for high glucose-induced protein secretion is through interaction of munc13 and rab34 (show RAB34 ELISA Kits), indicating a potentially critical role for this newly described pathway in the pathogenesis of DN.
Munc13-2 plays a fundamental role in large dense-core vesicle exocytosis, but in contrast to synapses lacking Munc13s, the corresponding chromaffin cells do not exhibit a vesicle docking defect.
Data demonstrate that Munc13-1 (show UNC13A ELISA Kits) and DOC2B (show DOC2B ELISA Kits) have different effects on network activity and that by enhancing asynchronous release, DOC2B (show DOC2B ELISA Kits) exerts its properties to increase spiking activity and elevate synchronization between neurons within network bursts
Munc13-1 (show UNC13A ELISA Kits) isoform is functionaly redundant in cytotoxic T lymphocytes.
betaARs couple to a cAMP/Epac (show RAPGEF3 ELISA Kits)/PLC (show HSPG2 ELISA Kits)/Munc13-1 (show UNC13A ELISA Kits)/Rab3a (show RAB3A ELISA Kits)/RIM1a (show RIMS1 ELISA Kits)-dependent pathway to enhance glutamate (show GRIN1 ELISA Kits) release at cerebrocortical nerve terminals.
Our data establish Munc13-1 (show UNC13A ELISA Kits) as a major presynaptic target of Ca(2 (show CA2 ELISA Kits)+)-Calmodulin signaling and show that the Ca(2 (show CA2 ELISA Kits)+)-Calmodulin-Munc13-1 (show UNC13A ELISA Kits) complex is a pivotal component of the molecular machinery that determines short-term synaptic plasticity characteristics.
The Munc13 gene family encodes molecules located at the synaptic active zone that regulate the reliability of synapses to encode information over a wide range of frequencies in response to action potentials.
This study demonistrated that Munc13 genotype regulates secretory amyloid precursor protein (show APP ELISA Kits) processing via postsynaptic glutamate (show GRIN1 ELISA Kits) receptors
Mammalian homologue of Caenorhabditis elegans unc-13-1 (Munc13-1 (show UNC13A ELISA Kits)) plays a role in the recruitment of newcomer insulin (show INS ELISA Kits) granules in both first and second phases of glucose-stimulated insulin (show INS ELISA Kits) secretion in mouse islets.
Munc13-1 (show UNC13A ELISA Kits)/2 were shown to facilitate dense-core vesicle fusion but, unlike for synaptic vesicles, were not essential for dense-core vesicle release.
The composition of Munc13 isoforms in a neuron differentially controls its short-term synaptic plasticity characteristics.
Chromaffin cell vesicle-priming by brain-specific (show CALY ELISA Kits) ubMunc13 isoform 2 is calcium ion (Ca2 (show CA2 ELISA Kits)+) dependent but independent of calmodulin (show KRIT1 ELISA Kits) binding to ubMunc13 isoform 2.
This gene is expressed in the kidney cortical epithelial cells and is upregulated by hyperglycemia. The encoded protein shares a high level of similarity to the rat homolog, and contains 3 C2 domains and a diacylglycerol-binding C1 domain. Hyperglycemia increases the levels of diacylglycerol, which has been shown to induce apoptosis in cells transfected with this gene and thus contribute to the renal cell complications of hyperglycemia. Studies in other species also indicate a role for this protein in the priming step of synaptic vesicle exocytosis.
unc-13 homolog B (C. elegans)
, protein unc-13 homolog B
, protein unc-13 homolog B-like
, homolog of rat Munc13 (diacylglycerol-binding)
, UNC-13 homolog 1
, unc-13 homolog A
, unc13 homolog 1
, unc-13 B-like protein