Abcam, ab317953, APC Anti-Myosin light chain kinase/MLCK antibody [EP1458Y]

Size: 100µL
Rabbit Recombinant Monoclonal Myosin light chain kinase/MLCK antibody - conjugated to APC.
Key facts
Host species:Rabbit,
Clonality:Monoclonal,
Clone number:EP1458Y,
Isotype:IgG,
Conjugation:APC,
Excitation/Emission:Ex: 650nm, Em: 660nm,
Carrier free:No,
Applications:Target Binding Affinity, Antibody LabellingSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:The exact immunogen used to generate this antibody is proprietary information.

Product details:
Patented technology
Our RabMAb
technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to
RabMAb® patents
What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:
- High batch-to-batch consistency and reproducibility
- Improved sensitivity and specificity
- Long-term security of supply
- Animal-free batch production
For more information, read more on
recombinant antibodies
How are conjugated primary antibodies validated?
This conjugated primary antibody is released using a quantitative quality control method that evaluates binding affinity post-conjugation and efficiency of antibody labeling.
For suitable applications and species reactivity, please refer to the unconjugated version of this clone.

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 7.4Preservative: 0.02% Sodium azideConstituents: PBS, 1% BSA, Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions-+4°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle, Store in the dark

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Myosin light chain kinase also known as MLCK is an enzyme that phosphorylates myosin light chain proteins facilitating muscle contraction. This kinase primarily interacts with myosin a molecular motor protein responsible for converting chemical energy into mechanical force. The myosin light chains are a part of this complex and are important for regulating myosin's ATPase activity. The molecular weight of MLCK is approximately 130 kDa. It is expressed in various tissues including smooth muscle skeletal muscle and endothelial cells reflecting its central role in these muscle types.
Biological function summary
Myosin light chain kinase plays a critical role in the regulation of muscle contraction and cellular motility. By phosphorylating the myosin light chain MLCK allows the interaction of actin and myosin which is essential for muscle contraction and movement. In smooth muscle MLCK activity is important for regulating vascular tone and blood pressure. As part of a complex with calmodulin MLCK activation depends on calcium levels linking its activity with intracellular signaling pathways influenced by calcium ions.
Pathways
Myosin light chain kinase is an integral part of the calcium-calmodulin pathway where it acts in response to increased intracellular calcium levels signaled through various cellular activities. This kinase is also involved in the RhoA-Rho kinase pathway which regulates smooth muscle contraction and cytoskeletal dynamics. Related proteins in these pathways include calmodulin whose binding activates MLCK and RhoA a small GTPase associated with the assembly of actin-myosin filaments.
Myosin light chain kinase has links to cardiovascular diseases such as hypertension due to its role in smooth muscle contraction and blood vessel function. Asthma is another condition related to MLCK as the kinase influences airway smooth muscle tone which can affect breathing. Dysregulation of MLCK activity can manifest in altered muscle contractility in these diseases making it a potential target for therapeutic intervention. Research continues to explore the kinase's interactions with calmodulin and other proteins within these disease pathways.