Anti-CLTB / Clathrin light chain B

Adding 0.2 ml of distilled water will yield a concentration of 500 ug/ml. CLTB antibody detects Clathrin light chain B, a component of clathrin-coated vesicles essential for endocytosis and intracellular trafficking. The UniProt recommended name is Clathrin light chain B (CLTB). This cytoplasmic protein associates with clathrin heavy chains to form triskelion structures that assemble into coated pits and vesicles mediating membrane transport.Functionally, CLTB antibody identifies a 248-amino-acid protein that stabilizes clathrin triskelia and regulates their disassembly during vesicle recycling. CLTB modulates the curvature and dynamics of the clathrin coat, influencing receptor-mediated endocytosis, synaptic vesicle turnover, and Golgi trafficking. It acts in concert with accessory proteins such as Hsc70 and auxilin during clathrin uncoating.The CLTB gene is located on chromosome 5q35.3 and is ubiquitously expressed, with high levels in neuronal and endocrine tissues. CLTB's co-expression with Clathrin light chain A (CLTA) allows tissue-specific modulation of vesicular transport efficiency and kinetics. It contributes to receptor internalization and synaptic function.Pathologically, altered CLTB expression has been linked to neurodegenerative and metabolic disorders. Variants affecting clathrin assembly disrupt synaptic vesicle trafficking, leading to impaired neurotransmission. Research using CLTB antibody supports studies in endocytosis, membrane dynamics, and intracellular transport mechanisms.CLTB antibody is validated for western blotting, immunohistochemistry, and immunofluorescence to detect clathrin complex proteins. NSJ Bioreagents provides CLTB antibody reagents optimized for cell biology, neuroscience, and membrane trafficking studies.Structurally, Clathrin light chain B binds to the proximal leg of clathrin heavy chains through its N-terminal domain and regulates triskelion assembly via its flexible C-terminal tail. This antibody enables analysis of CLTB's structural and regulatory roles in clathrin-mediated vesicle formation.