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        ASK 1 (phospho Ser966) rabbit pAb
        ES1264
        規(guī)格: 價格:
        50μL ¥1280.00
        100μL ¥1980.00

        Overview

        Product name: ASK 1 (phospho Ser966) rabbit pAb
        Reactivity: Human;Mouse;Rat
        Alternative Names: MAP3K5; ASK1; MAPKKK5; MEKK5; Mitogen-activated protein kinase kinase kinase 5; Apoptosis signal-regulating kinase 1; ASK-1; MAPK/ERK kinase kinase 5; MEK kinase 5; MEKK 5
        Source: Rabbit
        Dilutions: Western Blot: 1/500 - 1/2000. Immunohistochemistry: 1/100 - 1/300. ELISA: 1/20000. Not yet tested in other applications.
        Immunogen: The antiserum was produced against synthesized peptide derived from human ASK1 around the phosphorylation site of Ser966. AA range:932-981
        Storage: -20°C/1 year
        Clonality: Polyclonal
        Isotype: IgG
        Concentration: 1 mg/ml
        Observed Band: 155kD
        GeneID: 4217
        Human Swiss-Prot No: Q99683
        Cellular localization: Cytoplasm . Endoplasmic reticulum. Interaction with 14-3-3 proteins alters the distribution of MAP3K5/ASK1 and restricts it to the perinuclear endoplasmic reticulum region.
        Background: Mitogen-activated protein kinase (MAPK) signaling cascades include MAPK or extracellular signal-regulated kinase (ERK), MAPK kinase (MKK or MEK), and MAPK kinase kinase (MAPKKK or MEKK). MAPKK kinase/MEKK phosphorylates and activates its downstream protein kinase, MAPK kinase/MEK, which in turn activates MAPK. The kinases of these signaling cascades are highly conserved, and homologs exist in yeast, Drosophila, and mammalian cells. MAPKKK5 contains 1,374 amino acids with all 11 kinase subdomains. Northern blot analysis shows that MAPKKK5 transcript is abundantly expressed in human heart and pancreas. The MAPKKK5 protein phosphorylates and activates MKK4 (aliases SERK1, MAPKK4) in vitro, and activates c-Jun N-terminal kinase (JNK)/stress-activated protein kinase (SAPK) during transient expression in COS and 293 cells; MAPKKK5 does not activate MAPK/ERK. [provided by Re
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