PKM1/2 (C5E6) Rabbit mAb

PKM1/2 (C5E6) Rabbit mAb

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品牌:Cell Signaling Technology 品牌认证

货号:3106

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抗体英文名 :PKM1/2 (C5E6) Rabbit mAb

抗原 :synthetic peptide corresponding to the sequence of human PKM1

应用范围 :W, IP

适应物种 :H,M,R

库存 :大量

级别 :详见MSDS文件

供应商 :CST

保质期 :详见说明书

是否单克隆 :1

保存条件 :-20°c

规格 :100 ul (10 western blots)/carrier free & custom formulation / quantity

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
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) Isotype
W IP H M R Endogenous 60 Rabbit IgG
Protocols
Specificity / Sensitivity

PKM1/2 (C5E6) Rabbit mAb detects endogenous levels of total PKM1 and PKM2 proteins.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to the sequence of human PKM1.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell types using PKM1/2 (C5E6) Rabbit mAb.

Western Blotting

Western Blotting

Western blot analysis of extract from mouse muscle using PKM1/2 (C5E6) Rabbit mAb.

Background

Pyruvate kinase, a glycolytic enzyme, catalyses the conversion of phosphoenolpyruvate to pyruvate. In mammals, the M1 isoform (PKM1) is expressed in most adult tissues (1). The M2 isoform (PKM2), an alternatively-spliced variant of M1, is expressed during embryonic development (1). Studies found that cancer cells exclusively express PKM2 (1-3). PKM2 is shown to be essential for aerobic glycolysis in tumors (Warburg effect) (1). When the M2 isoform is switched to the M1 isoform, aerobic glycolysis is reduced and oxidative phosphorylation is increased in cancer cells (1). These cells also show decreased tumorigenicity in mouse xenografts (1). Recent studies show that the oncogenic forms of FGFR1 directly phosphorylate Tyr105 of PKM2 and thereby inhibit the formation of active tetrameric PKM2 (4). A PKM2 mutant found in cancer cells, in which Tyr105 is replaced by phenylalanine, leads to reduced cell proliferation in hypoxia and tumor growth in xenografts in nude mice (4). These findings suggest that the phosphorylation at Tyr105 is a critical switch for the metabolism in cancer cells that promotes tumor growth (4).

  1. Christofk, H.R. et al. (2008) Nature 452, 230-3.
  2. Mazurek, S. et al. (2005) Semin Cancer Biol 15, 300-8.
  3. Dombrauckas, J.D. et al. (2005) Biochemistry 44, 9417-29.
  4. Hitosugi, T. et al. (2009) Sci Signal 2, ra73.

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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