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Phospho-AMPKβ1 (Ser108) Antibo

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  • 询价
  • Cell Signaling Technology已认证
  • USA
  • 2025年12月06日
  • W, IP
  • Rabbit
  • H,M,R,Mk
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    • 详细信息
    • 文献和实验
    • 技术资料
    • 抗体英文名

      Phospho-AMPKβ1 (Ser108) Antibody

    • 抗原

      synthetic phosphopeptide corresponding to residues surrounding Ser108 of human AMPKβ1

    • 应用范围

      W, IP

    • 宿主

      Rabbit

    • 库存

      大量

    • 供应商

      CST

    • 保质期

      详见说明书

    • 适应物种

      H,M,R,Mk

    • 级别

      详见MSDS文件

    • 是否单克隆

      2

    • 保存条件

      -20°c

    • 规格

      40 ul (4 western blots)/100 ul (10 western blots)/carrier free & custom formulation / quantity

    规格:产品价格:¥请询价
    规格:40 ul (4 western blots)产品价格:¥请询价
    规格:100 ul (10 western blots)产品价格:¥请询价
    规格:carrier free & custom formulation / quantity产品价格:¥请询价

    pathway more info application references datasheet PDF MSDS PDF protocols

    Applications Key:  W=Western Blotting  IP=Immunoprecipitation
    Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey
    Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

    Applications Reactivity Sensitivity MW (kDa) Source
    W IP H M R Mk Endogenous 38 Rabbit
    Protocols
    Specificity / Sensitivity

    Phospho-AMPKβ1 (Ser108) Antibody detects endogenous levels of AMPKβ1 only when phosphorylated at serine 108. The antibody may cross-react with phosphorylated AMPKβ2 when phosphorylated at Ser109.

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser108 of human AMPKβ1. Antibodies are purified by protein A and peptide affinity chromatography.

    Western Blotting

    Western Blotting

    Western blot analysis of extracts from C2C12 cells, untreated (lanes 1,3) or oligomycin-treated (lanes 2,4), using Phospho-AMPKβ1 (Ser108) Antibody (upper) or AMPKβ1 Antibody #4182 (lower). Cell lysates were treated with λ phosphatase in lanes 3 and 4 to demonstrate the phospho-specificity of Phospho-AMPKβ1 (Ser108) Antibody.

    IP

    IP

    Immunoprecipitation of phosphorylated AMPKβ1 from untreated or oligomycin-treated C2C12 cells using Phospho-AMPKβ1 (Ser108) Antibody, followed by western blot analysis using the same antibody.

    Background

    AMP-activated protein kinase (AMPK) is highly conserved from yeast to plants and animals and plays a key role in the regulation of energy homeostasis (1). AMPK is a heterotrimeric complex composed of a catalytic α subunit and regulatory β and γ subunits, each of which is encoded by two or three distinct genes (α1, 2; β1, 2; γ1, 2, 3) (2). The kinase is activated by an elevated AMP/ATP ratio due to cellular and environmental stress, such as heat shock, hypoxia, and ischemia (1). The tumor suppressor LKB1, in association with accessory proteins STRAD and MO25, phosphorylates AMPKα at Thr172 in the activation loop, and this phosphorylation is required for AMPK activation (3-5). AMPKα is also phosphorylated at Thr258 and Ser485 (for α1; Ser491 for α2). The upstream kinase and the biological significance of these phosphorylation events have yet to be elucidated (6). The β1 subunit is post-translationally modified by myristoylation and multi-site phosphorylation including Ser24/25, Ser96, Ser101, Ser108, and Ser182 (6,7). Phosphorylation at Ser108 of the β1 subunit seems to be required for the activation of AMPK enzyme, while phosphorylation at Ser24/25 and Ser182 affects AMPK localization (7). 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 (1,2). 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 (1).

    1. Hardie, D.G. (2004) J Cell Sci 117, 5479-87.
    2. Carling, D. (2004) Trends Biochem Sci 29, 18-24.
    3. Hawley, S.A. et al. (1996) J Biol Chem 271, 27879-87.
    4. Lizcano, J.M. et al. (2004) EMBO J 23, 833-43.
    5. Shaw, R.J. et al. (2004) Proc Natl Acad Sci USA 101, 3329-35.
    6. Woods, A. et al. (2003) J Biol Chem 278, 28434-42.
    7. Warden, S.M. et al. (2001) Biochem J 354, 275-83.
    Application References

    Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know !

    Companion Products

    For Research Use Only. Not For Use In Diagnostic Procedures.

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    图标文献和实验
    相关实验
    • Monoclonal Antibody Production Protocol

      for 5 - 10 min. Aspirate the medium, resuspend pellet and wash again with 30ml of IMDM. One immunized spleen has approx. 108 cells. After this wash the cells are ready for the fusion. Myeloma cell preparation: It is essential that the myelomas be free

    • secondary antibody review -- data from 99 publications

      cytometry   used as a control to detect cell responses targeted antigen   7       Alexa Fluor 488         7       Cy3         8 goat IgG   Alexa Fluor 488   1:2000 detect antibody binding in human embryonic kidney 293T cells Invitrogen 9 donkey

    • Production of Human Fab Antibody Fragments from Phage Display Libraries

      with the desired binding properties (1 ) (see review in ref. 2 ). Initially, the system was used for mapping antibody epitopes by expression of large libraries (107 –108 ) of random peptides (3 –5 ). However, the approach has proved readily applicable

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