1-832-868-1888
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Catalog Number: |
12822 |
| other_names: | PKM, p58, PK3, PKM2, Pyruvate Kinase, Pyruvate kinase 2/3, Pyruvate kinase, m1, Pyruvate kinase, muscle, TCB, Tumor M2-PK, OIP-3, OIP3, Opa-interacting protein 3, CTHBP, PK, muscle type, PK2, Pyruvate kinase isozymes M1/M2, Pyruvate kinase muscle iso ... |
Amount: |
100μg/100μl |
| calculated_mw: | 58 kDa |
| host_species: | Rabbit |
Price: |
$319 |
Swiss-Prot No: |
P14618 |
Form of Antibody: |
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. |
Storage/Stability: |
|
Immunogen: |
Synthesized peptide derived from human PKM2 around the phosphorylation site of Ser37. |
Purification: |
Affinity purification using immunogen. |
Specificity/Sensitivity: |
PKM2(phospho-Ser37) Antibody detects endogenous levels of PKM2 only when phosphorylated at Ser37 |
Applications: |
|
Background: |
Pyruvate kinase M2 (PKM2) is upregulated in multiple cancer types and contributes to the Warburg effect. Relative research demonstrated that EGFR-activated ERK2 binds directly to PKM2 Ile 429/Leu 431 through the ERK2 docking groove and phosphorylates PKM2 at Ser 37. Phosphorylated PKM2 Ser 37 recruits PIN1 for cis–trans isomerization of PKM2, which promotes PKM2 binding to importin α5 and translocating to the nucleus. In addition, levels of PKM2 Ser 37phosphorylation correlate with EGFR and ERK1/2 activity in human glioblastoma specimens [1] |
References: |
[1] Yang W, Zheng Y, Xia Y, Ji H, Chen X, Guo F, Lyssiotis CA, Aldape K, Cantley LC, Lu Z. ERK1/2-dependent phosphorylation and nuclear translocation of PKM2 promotes the Warburg effect. Nat Cell Biol. 2012 Dec;14(12):1295-304. doi: 10.1038/ncb2629. |
appl_detail: |
Western blotting: 1:1000-3000 |
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