Item no. |
PTM-6785 |
Manufacturer |
PTM Biolabs
|
Amount |
100 ul |
Format |
Lyophilized powder |
Applications |
WB |
Specific against |
Human (Homo sapiens) |
Host |
Rabbit |
Isotype |
IgG |
Conjugate/Tag |
Unconjugated |
Alias |
AMPK subunit beta-1, AMPKb, AMPK, PRKAB1 |
Shipping condition |
Room temperature |
Available |
|
Manufacturer - Type |
Primary Antibodies |
Manufacturer - Category |
Uncategorized |
Manufacturer - Targets |
AMPK beta 1 |
Shipping Temperature |
Ambient temperature |
Storage Conditions |
Store at -20°C. Avoid freeze/thaw cycles. |
Manufacturer - Research Area |
Signal Transduction, Neuroscience, Metabolism, Cancer, Cardiovascular Biology |
Product description |
AMPKβ1 is the β1 regulating subunit of AMP-activated protein kinase. It is post-translationally modified by myristoylation and multi-site phosphorylation including Ser24/25, Ser96, Ser101, Ser108, and Ser182. Phosphorylation at Ser108 of the β1 subunit seems to be required for AMPK activation, while phosphorylation at Ser24/25 and Ser182 affects AMPK localization. Several mutations in AMPKγ subunits have been identified, most of which are located in the putative AMP/ATP binding sites (CBS or Bateman domains). Mutations at these sites lead to reduction of AMPK activity and cause glycogen accumulation in heart or skeletal muscle. Accumulating evidence indicates that AMPK not only regulates the metabolism of fatty acids and glycogen, but also modulates protein synthesis and cell growth through EF2 and TSC2/mTOR pathways, as well as blood flow via eNOS/nNOS. |
Purification Method |
Protein A purified |
Constituents |
PBS, Glycerol, BSA |
PTM |
Phospho |
Modification Site |
Ser182 |
Clonality |
Polyclonal |
Stability |
Stable for 12 months from date of receipt/reconstitution. |
Background |
AMPKβ1 is the β1 regulating subunit of AMP-activated protein kinase. It is post-translationally modified by myristoylation and multi-site phosphorylation including Ser24/25, Ser96, Ser101, Ser108, and Ser182. Phosphorylation at Ser108 of the β1 subunit seems to be required for AMPK activation, while phosphorylation at Ser24/25 and Ser182 affects AMPK localization. Several mutations in AMPKγ subunits have been identified, most of which are located in the putative AMP/ATP binding sites (CBS or Bateman domains). Mutations at these sites lead to reduction of AMPK activity and cause glycogen accumulation in heart or skeletal muscle. Accumulating evidence indicates that AMPK not only regulates the metabolism of fatty acids and glycogen, but also modulates protein synthesis and cell growth through EF2 and TSC2/mTOR pathways, as well as blood flow via eNOS/nNOS. |
Cellular Localization |
Cell nucleus and cytosol |
Note: The presented information and documents (Manual, Product Datasheet, Safety Datasheet and Certificate of Analysis) correspond to our latest update and should serve for orientational purpose only. We do not guarantee the topicality. We would kindly ask you to make a request for specific requirements, if necessary.
All products are intended for research use only (RUO). Not for human, veterinary or therapeutic use.