Comparison

Anti-Phospho-AMPK beta 1 (Ser182) Rabbit pAb

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.

Amount: 100 ul
Available: In stock
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