U-Blot® AMPylation MultiPTM Mouse Monoclonal Antibody mix

U-Blot® AMPylation MultiPTM Mouse Monoclonal Antibody mix
U-Blot® AMPylation MultiPTM Mouse Monoclonal Antibody mix
$550.00
Size:100μl
SKU: WT9510M-100

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

01

Documents

Datasheet, COA, SDS, and protocol files can be requested from technical support.

02

Storage & Handling

Storage
Store at -20°C. Avoid repeated freeze-thaw cycles
06

Contact Support

Emailinfo@mail.ucallm.com

Phone+(1)-866-986-9598

WeChat / IMUcallm-Tech

HoursMonday-Friday 09:00-18:00 CST

Request Technical Support
Keywords:AMPylation