Human Diphthamide Biosynthesis Protein 2 (DPH2) Protein
234€ (1 µg)
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Name
Human Diphthamide Biosynthesis Protein 2 (DPH2) Protein
Category
Proteins and Peptides
Provider
Abbexa
Reference
abx680238
Tested Applications
SDS-PAGE
Description
Human Diphthamide Biosynthesis Protein 2 (DPH2) Protein is a recombinant protein produced in Sf9, Baculovirus cells.
Documentos del producto
Instrucciones
Data sheet
Especificaciones del producto
| Category | Proteins and Peptides |
| Immunogen Target | Diphthamide Biosynthesis Protein 2 (DPH2) |
| Host | Insect |
| Origin | Human |
| Conjugation | Unconjugated |
| Expression | Recombinant |
| Purity | > 85% (SDS-PAGE) |
| Size 1 | 1 µg |
| Size 2 | 5 µg |
| Size 3 | 50 µg |
| Form | Liquid |
| Tested Applications | SDS-PAGE |
| Availability | Shipped within 5-10 working days. |
| Dry Ice | No |
| Alias | DPH2L2,DEDSSH2,Diphthamide biosynthesis protein 2,Diphtheria toxin resistance protein 2 |
| Background | Protein DPH2 |
| Status | RUO |
| Note | THIS PRODUCT IS FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC, THERAPEUTIC OR COSMETIC PROCEDURES. NOT FOR HUMAN OR ANIMAL CONSUMPTION. |
Background
DPH2 is an essential enzyme that works in concert with DPH1 to catalyze the first step of diphthamide biosynthesis on eukaryotic elongation factor 2 (eEF2), forming a critical intermediate for subsequent modifications. It interacts directly with DPH1 to mediate the transfer of a 3-amino-3-carboxypropyl group from S-adenosylmethionine (SAM) to the imidazole ring of a specific histidine residue. DPH2 mutations are associated with defects in protein translation fidelity and resistance to diphtheria toxin, as this toxin specifically targets diphthamide. Structural studies of DPH2 reveal conserved binding sites for SAM, emphasizing its central role in catalytic function. In addition to its enzymatic role, DPH2 is required for maintaining normal cellular physiology, particularly in protein synthesis and stress responses. DPH2 expression is tightly regulated and primarily localized in the cytoplasm, where it coordinates with other diphthamide biosynthesis factors. Deficiencies in DPH2 activity result in incomplete diphthamide synthesis, impacting cellular growth and proliferation. Its evolutionary conservation highlights its critical role in cellular and organismal viability.
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