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Anti-PKM2 Picoband Antibody
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- BACKGROUND
Application 
| WB, IHC-P |
|---|---|
| Primary Accession | P14618 |
| Host | Rabbit |
| Reactivity | Human |
| Clonality | Polyclonal |
| Format | Lyophilized |
| Description | Rabbit IgG polyclonal antibody for Pyruvate kinase PKM(PKM) detection. Tested with WB, IHC-P in Human. |
| Reconstitution | Add 0.2ml of distilled water will yield a concentration of 500ug/ml. |
| Gene ID | 5315 |
|---|---|
| Other Names | Pyruvate kinase PKM, 2.7.1.40, Cytosolic thyroid hormone-binding protein, CTHBP, Opa-interacting protein 3, OIP-3, Pyruvate kinase 2/3, Pyruvate kinase muscle isozyme, Thyroid hormone-binding protein 1, THBP1, Tumor M2-PK, p58, PKM, OIP3, PK2, PK3, PKM2 |
| Calculated MW | 57937 MW KDa |
| Application Details | Immunohistochemistry(Paraffin-embedded Section), 0.5-1 µg/ml, Human, By Heat Western blot, 0.1-0.5 µg/ml, Human |
| Subcellular Localization | Cytoplasm. Nucleus. Translocates to the nucleus in response to different apoptotic stimuli. Nuclear translocation is sufficient to induce cell death that is caspase independent, isoform-specific and independent of its enzymatic activity. |
| Tissue Specificity | Specifically expressed in proliferating cells, such as embryonic stem cells, embryonic carcinoma cells, as well as cancer cells. . |
| Protein Name | Pyruvate kinase PKM |
| Contents | Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3. |
| Immunogen | A synthetic peptide corresponding to a sequence at the N-terminus of human PKM2(475-500aa KDPVQEAWAEDVDLRVNFAMNVGKAR), different from the related mouse sequence by five amino acids, and from the related rat sequence by four amino acids. |
| Purification | Immunogen affinity purified. |
| Cross Reactivity | No cross reactivity with other proteins. |
| Storage | At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing. |
| Sequence Similarities | Belongs to the pyruvate kinase family. |
| Name | PKM |
|---|---|
| Synonyms | OIP3 {ECO:0000303|PubMed:9466265}, PK2, |
| Function | Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP (PubMed:20847263, PubMed:15996096, PubMed:1854723). The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production (PubMed:20847263, PubMed:15996096, PubMed:1854723). The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival (PubMed:20847263, PubMed:15996096, PubMed:1854723). |
| Cellular Location | [Isoform M2]: Cytoplasm. Nucleus Note=Translocates to the nucleus in response to various signals, such as EGF receptor activation or apoptotic stimuli (PubMed:17308100, PubMed:22056988, PubMed:24120661). Nuclear translocation is promoted by acetylation by EP300 (PubMed:24120661). Deacetylation by SIRT6 promotes its nuclear export in a process dependent of XPO4, thereby suppressing its ability to activate transcription and promote tumorigenesis (PubMed:26787900). |
| Tissue Location | [Isoform M2]: Specifically expressed in proliferating cells, such as embryonic stem cells, embryonic carcinoma cells, as well as cancer cells. |
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Provided below are standard protocols that you may find useful for product applications.
Background
PKM (Pyruvate Kinase, Muscle), also known as PK3 or PKM2, is an enzyme that in humans is encoded by the PKM gene. The activity of pyruvate kinase subtype M2 is increased by fructose 1, 6-bisphosphate (Fru-1, 6-P2). By in situ hybridization, Popescu and Cheng (1990) mapped the THBP1 gene to 15q24-q25. Ashizawa et al. (1991) manipulated the intracellular Fru-1, 6-P2 concentration in several mammalian cell lines, including human, by varying the glucose concentration in the media. Using a novel proteomic screen for phosphotyrosine-binding proteins, Christofk et al. (2008) observed that PKM2 binds directly and selectively to tyrosine-phosphorylated peptides.
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