ATP-Binding Domain-Containing Protein 4 (ATPBD4) Antibody

Este producto es parte de DPH - diphthamide biosynthesis
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357.5€ (100 µg)

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935106861
info@markelab.com
name
ATP-Binding Domain-Containing Protein 4 (ATPBD4) Antibody
category
Primary Antibodies
provider
Abbexa
reference
abx145559
tested applications
ELISA, WB, IHC

Description

ATPBD4 Antibody is a Rabbit Polyclonal against ATPBD4.

Documents del producto

Instrucciones
Data sheet
Descargar

Product specifications

Category
Primary Antibodies
Immunogen Target
ATP-Binding Domain-Containing Protein 4 (ATPBD4)
Host
Rabbit
Reactivity
Human
Recommended Dilution
ELISA: 1/20000 - 1/80000, WB: 1/500 - 1/2000, IHC: 1/100 - 1/200. Optimal dilutions/concentrations should be determined by the end user.
Clonality
Polyclonal
Conjugation
Unconjugated
Isotype
IgG
Purification
Purified by antigen affinity column chromatography.
Size 1
100 µg
Size 2
1 mg
Form
Lyophilized
Tested Applications
ELISA, WB, IHC
Buffer
Prior to lyophilization: 1% BSA and 0.02% NaN3.
Availability
Shipped within 7-15 working days.
Storage
Store at -20 °C. Avoid repeated freeze/thaw cycles.
Dry Ice
No
NCBI Accession
BC066652
Alias
ATPBD4,ATP-binding domain-containing protein 4,Diphthamide synthase,Diphthine-ammonia ligase
Background
Antibody anti-DPH6
Status
RUO
Note
Concentration: Lyophilized form: Not applicable.  After reconstitution: 1 mg/ml. - 

Descripción

DPH6 is an ATP-dependent enzyme responsible for converting the diphthine intermediate to diphthamide through the addition of an amidino group. It acts in the final step of diphthamide biosynthesis, ensuring that the modified histidine residue on eEF2 achieves its fully functional state. DPH6 relies on the coordinated action of other diphthamide biosynthesis proteins to access substrates and carry out its catalytic activity. Genetic studies indicate that mutations or disruptions in DPH6 can result in resistance to bacterial toxins such as diphtheria toxin and impaired ribosomal translocation, highlighting its critical cellular role. DPH6 contains conserved ATP-binding motifs essential for its enzymatic function, and its expression is tightly regulated in metabolically active tissues. The absence of functional DPH6 disrupts protein synthesis, leading to cellular and organismal defects, particularly in systems dependent on high translational efficiency. DPH6 also interacts with DPH7, facilitating the amidination reaction and ensuring proper coordination of the biosynthesis pathway.

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