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

364€ (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
abx230734
tested applications
ELISA, WB
Description
ATPBD4 Antibody is a Rabbit Polyclonal against ATPBD4.
Documents del producto
Instrucciones
Data sheet
Product specifications
Category | Primary Antibodies |
Immunogen Target | ATP-Binding Domain-Containing Protein 4 (ATPBD4) |
Host | Rabbit |
Reactivity | Human, Mouse |
Recommended Dilution | Optimal dilutions/concentrations should be determined by the end user. |
Clonality | Polyclonal |
Conjugation | Unconjugated |
Isotype | IgG |
Purity | ≥ 95% (SDS-PAGE) |
Purification | Purified by immunogen affinity chromatography. |
Size 1 | 100 µg |
Form | Liquid |
Tested Applications | ELISA, WB |
Buffer | PBS, pH 7.3, with 0.02% sodium azide and 50% glycerol. |
Availability | Shipped within 5-12 working days. |
Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
Dry Ice | No |
UniProt ID | Q7L8W6 |
Gene ID | 89978 |
Alias | ATPBD4,ATP-binding domain-containing protein 4,Diphthamide synthase,Diphthine-ammonia ligase |
Background | Antibody anti-DPH6 |
Status | RUO |
Note | Concentration: 2 mg/ml - Validity: 12 months. |
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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