Recombinant Human JMY protein is a Human Fragment protein, in the 163 to 341 aa range, expressed in Escherichia coli, with >80% purity and suitable for SDS-PAGE.
>80% SDS-PAGE
Escherichia coli
His-DHFR tag N-Terminus
SDS-PAGE
No
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Acts both as a nuclear p53/TP53-cofactor and a cytoplasmic regulator of actin dynamics depending on conditions (PubMed:30420355). In nucleus, acts as a cofactor that increases p53/TP53 response via its interaction with p300/EP300. Increases p53/TP53-dependent transcription and apoptosis, suggesting an important role in p53/TP53 stress response such as DNA damage. In cytoplasm, acts as a nucleation-promoting factor for both branched and unbranched actin filaments (PubMed:30420355). Activates the Arp2/3 complex to induce branched actin filament networks. Also catalyzes actin polymerization in the absence of Arp2/3, creating unbranched filaments (PubMed:30420355). Contributes to cell motility by controlling actin dynamics. May promote the rapid formation of a branched actin network by first nucleating new mother filaments and then activating Arp2/3 to branch off these filaments. Upon nutrient stress, directly recruited by MAP1LC3B to the phagophore membrane surfaces to promote actin assembly during autophagy (PubMed:30420355). The p53/TP53-cofactor and actin activator activities are regulated via its subcellular location (By similarity).
Junction-mediating and -regulatory protein, JMY
Recombinant Human JMY protein is a Human Fragment protein, in the 163 to 341 aa range, expressed in Escherichia coli, with >80% purity and suitable for SDS-PAGE.
>80% SDS-PAGE
Escherichia coli
His-DHFR tag N-Terminus
SDS-PAGE
No
No
Human
Reconstitute in water
Constituents: 0.58% Sodium chloride, 0.32% Tris HCl
Fragment
21.7 kDa
163 to 341
Recombinant
His-DHFR tag N-Terminus
Lyophilized
Purified via His tag
Acts both as a nuclear p53/TP53-cofactor and a cytoplasmic regulator of actin dynamics depending on conditions (PubMed:30420355). In nucleus, acts as a cofactor that increases p53/TP53 response via its interaction with p300/EP300. Increases p53/TP53-dependent transcription and apoptosis, suggesting an important role in p53/TP53 stress response such as DNA damage. In cytoplasm, acts as a nucleation-promoting factor for both branched and unbranched actin filaments (PubMed:30420355). Activates the Arp2/3 complex to induce branched actin filament networks. Also catalyzes actin polymerization in the absence of Arp2/3, creating unbranched filaments (PubMed:30420355). Contributes to cell motility by controlling actin dynamics. May promote the rapid formation of a branched actin network by first nucleating new mother filaments and then activating Arp2/3 to branch off these filaments. Upon nutrient stress, directly recruited by MAP1LC3B to the phagophore membrane surfaces to promote actin assembly during autophagy (PubMed:30420355). The p53/TP53-cofactor and actin activator activities are regulated via its subcellular location (By similarity).
Belongs to the JMY family.
Ubiquitinated by MDM2, leading to its subsequent degradation by the proteasome. In case of DNA damage, the interaction with MDM2 is altered, preventing degradation and allowing interaction with p300/EP300 and its function in p53/TP53 stress response (By similarity).
Nucleus, Cytoskeleton
Blue Ice
-20°C
-20°C
This supplementary information is collated from multiple sources and compiled automatically.
JMY also known as Junction-mediating and -regulatory protein is a protein involved in actin nucleation. It interacts with actin to facilitate the formation of new actin filaments. JMY has a molecular mass of around 168 kDa and is highly expressed in various tissues including the brain heart and skeletal muscle. This expression pattern suggests its widespread role in cellular processes across different organ systems.
JMY influences cell movement and stability by controlling actin polymerization. It contributes to the actin-related protein (Arp2/3) complex which is important for branching actin filament networks. JMY controls cell migration and morphology through its actin-nucleating activity affecting how cells respond to their environment and communicate with one another. Its function in actin dynamics makes it a significant player in maintaining cellular architecture and facilitating processes like endocytosis and phagocytosis.
JMY participates in the regulation of the actin cytoskeleton and p53 pathways. In the actin cytoskeleton pathway JMY interacts with other proteins like WAVE and Arp2/3 to control actin assembly impacting cell shape and motility. In the p53 pathway JMY modulates transcriptional responses to DNA damage linking its actin-regulating functions with cellular stress responses. JMY establishes important connections between signaling pathways and structural cellular components therefore influencing a range of cellular behaviors.
JMY has been implicated in cancer progression and neurodegenerative diseases. Its dysregulation can lead to altered cell migration and invasion which are characteristics of cancer metastasis. For example loss of JMY activity might relate to the ability of cancer cells to metastasize especially in breast cancer. In neurodegenerative diseases aberrant actin dynamics potentially involving JMY contribute to neuronal dysfunction and loss. Research continues to explore JMY's interaction with other proteins in disease contexts including p53 pointing to its dual regulatory role in both structural integrity and gene transcription.
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