Description
Key facts
Cell type:HeLa,
Species or organism:Human,
Tissue:Cervix,
Knockout validation:Sanger Sequencing,
Mutation description:Knockout achieved by using CRISPR/Cas9, 25 bp deletion in exon2.,
Disease:Adenocarcinoma
Product details:
Knockout cell lysate achieved by CRISPR/Cas9.
REACH authorisation
Abcam has not and does not intend to apply for the REACH Authorisation of customers' uses of products that contain European Authorisation list (Annex XIV) substances.
It is the responsibility of our customers to check the necessity of application of REACH Authorisation, and any other relevant authorisations, for their intended uses.
Lysate preparation:
Our lysates are made using RIPA buffer to which we add a protease inhibitor cocktail and phosphatase inhibitor cocktail (ratio: 300:100:10).
This means that the protein of interest is denatured.
If you require a native form of the protein please use the live cell version. Please refer to our lysis protocol for further details on how our lysates are prepared.
User storage instructions:
Lyophilizate may be stored at 4°C. After reconstitution, store at -20°C for short-term storage or -80°C for long-term storage.
This product is subject to limited use licenses from The Broad Institute and ERS Genomics Limited, and is developed with patented technology. For full details of the limited use licenses and relevant patents please refer to our
limited use license
patent pages
Properties and Storage Information:
Gene name-KCNJ11, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, Shipped at conditions-Ambient - Can Ship with Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Kir6.2 also known by alternate names KCNJ11 and 2BIR is part of the ATP-sensitive potassium channel (K-ATP channel) complex specifically the pore-forming subunit. This protein has a molecular mass of approximately 43 kDa. Expression of Kir6.2 occurs in various tissues most notably in pancreatic beta cells cardiac muscle and neuronal tissues. These channels play an important role in cell membrane potential regulation and excitability modulating insulin release and muscle contraction by responding to intracellular levels of ATP and ADP.
Biological function summary
Kir6.2 functions by coupling cellular metabolic states to electrical activity via its role in the K-ATP channel complex. This complex integrates Kir6.2 with the sulfonylurea receptor SUR1 or SUR2 forming an important connection between cellular metabolism and membrane excitability. Kir6.2 helps manage glucose-induced insulin secretion in pancreatic beta cells contributing to the temporal burst of insulin after meals. Its function in neurons and muscle fibers includes balancing cellular energy levels and physiological processes such as neurotransmitter release and muscle contraction.
Pathways
Kir6.2 plays a significant role in insulin secretion and cardiac muscle contraction pathways. It interacts closely with various proteins including SUR1 in the insulin release pathway and SUR2 in cardiovascular regulation. The activity of Kir6.2 links it with processes such as glucose-stimulated insulin secretion where its modulation significantly impacts the entry of calcium ions through voltage-dependent calcium channels further altering the exocytosis of insulin granules. The reactivity to intracellular ATP levels means Kir6.2 acts as a metabolic sensor influencing these pathways accordingly.
Kir6.2 is linked to conditions such as neonatal diabetes mellitus and congenital hyperinsulinism. Mutations in the gene encoding Kir6.2 can disrupt normal K-ATP channel functioning leading to these diseases. In neonatal diabetes Kir6.2 alterations impair insulin secretion due to disrupted ATP binding or channel closure while in congenital hyperinsulinism dysfunction of Kir6.2 in hyperactive channels results in excessive insulin production. This exposes strong connections with proteins like insulin within these conditions highlighting its important influence on glucose metabolism and energy homeostasis.
