U-Blot® AMPylation MultiPTM Mouse Monoclonal Antibody mix

Catalog No.: WT9510M
Specification: 100μL/300μL
Stock: In stock
Product details, specifications, documents, and related products are available from the catalog record. Learn more
Product information
Background:AMPylation, also known as adenylylation, is a reversible post-translational modification of proteins. In this process, a class of enzymes called "AMPylases" covalently attaches an AMP (adenosine monophosphate) group from ATP to serine, threonine, or tyrosine residues on target proteins. This dynamic process is precisely regulated by "writers" (AMPylases) and "erasers" (de-AMPylases), thereby fine-tuning the function of the modified proteins. AMPylation was first discovered in 1967 in the regulation of bacterial glutamine synthetase, and its biological significance is profound. It is not only exploited by pathogenic bacteria to hijack host cell signaling to promote infection, but also plays critical physiological roles in humans—for example, the ER-localized enzyme FICD regulates the activity of the chaperone BiP in response to unfolded protein stress. Recent studies have further revealed that AMPylation plays important roles in various physiopathological processes, including metabolic regulation, neurodevelopment, diabetes, and cancer metastasis.
Product Overview
- Catalog No.
- WT9510M
- SKU
- WT9510M-100
- Category
- AMPylation
- Product Type
- Other
- Size
- 100μL/300μL
- Stock Status
- In stock
- Available Stock
- 20
- Minimum Order Quantity
- 1
Storage & Compliance
- Storage
- Store at -20°C. Avoid repeated freeze-thaw cycles
- Research Use Only
- Yes
Additional Specifications
- Antibody Type
- Multi PTM
- Target
- AMPylation
- Reactivity
- Species Independent
- Application
- WB
- MW(Calculated)
- --
- MW(Observed)
- --
- Host Species
- Mouse
- Isotype
- IgG2b,k
- Conjugate
- Unconjugated
- Modification
- AMPylation
- Modification Site
- --
- Recommended dilution ratio
- WB 1:400
- Composition
- PBS, 40% Glycerol, 0.05% BSA, 0.02% sodium azide
- Purification process
- --
- storageCondition
- Store at -20°C. Avoid repeated freeze-thaw cycles
- Stability
- Stable for 12 months from date of receipt / reconstitution.
- Concentration
- 2 mg/ml
- Clonal
- Recombinant mAb
- Clone Number
- --
- Immunogen
- --
- Gene Name
- --
- Protein Name
- --
- Alternative name
- --
- Organism-1
- --
- Gene ID
- --
- SwissProt-1
- --
- --
- Background:
- Background
- AMPylation, also known as adenylylation, is a reversible post-translational modification of proteins. In this process, a class of enzymes called "AMPylases" covalently attaches an AMP (adenosine monophosphate) group from ATP to serine, threonine, or tyrosine residues on target proteins. This dynamic process is precisely regulated by "writers" (AMPylases) and "erasers" (de-AMPylases), thereby fine-tuning the function of the modified proteins. AMPylation was first discovered in 1967 in the regulation of bacterial glutamine synthetase, and its biological significance is profound. It is not only exploited by pathogenic bacteria to hijack host cell signaling to promote infection, but also plays critical physiological roles in humans—for example, the ER-localized enzyme FICD regulates the activity of the chaperone BiP in response to unfolded protein stress. Recent studies have further revealed that AMPylation plays important roles in various physiopathological processes, including metabolic regulation, neurodevelopment, diabetes, and cancer metastasis.
- Cellular Localization
- --
- --
- Background:AMPylation, also known as adenylylation, is a reversible post-translational modification of proteins. In this process, a class of enzymes called "AMPylases" covalently attaches an AMP (adenosine monophosphate) group from ATP to serine, threonine, or tyrosine residues on target proteins. This dynamic process is precisely regulated by "writers" (AMPylases) and "erasers" (de-AMPylases), thereby fine-tuning the function of the modified proteins. AMPylation was first discovered in 1967 in the regulation of bacterial glutamine synthetase, and its biological significance is profound. It is not only exploited by pathogenic bacteria to hijack host cell signaling to promote infection, but also plays critical physiological roles in humans—for example, the ER-localized enzyme FICD regulates the activity of the chaperone BiP in response to unfolded protein stress. Recent studies have further revealed that AMPylation plays important roles in various physiopathological processes, including metabolic regulation, neurodevelopment, diabetes, and cancer metastasis.
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Tech Support
ucallm
Documents
Datasheet, COA, SDS, and protocol files can be requested from technical support.
Storage & Handling
- Storage
- Store at -20°C. Avoid repeated freeze-thaw cycles
Contact Support
Emailinfo@mail.ucallm.com
Phone+(1)-866-986-9598
WeChat / IMUcallm-Tech
HoursMonday-Friday 09:00-18:00 CST
