Mouse DHFR Antibody (C-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| IHC-P, WB, E |
---|---|
Primary Accession | P00375 |
Reactivity | Mouse, Rat |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 21606 Da |
Antigen Region | 135-164 aa |
Gene ID | 13361 |
---|---|
Other Names | Dihydrofolate reductase, Dhfr |
Target/Specificity | This Mouse DHFR antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 135-164 amino acids from the C-terminal region of mouse DHFR. |
Dilution | WB~~1:2000 IHC-P~~1:50~100 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | Mouse DHFR Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | Dhfr |
---|---|
Function | Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway (PubMed:25980602). Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (PubMed:25980602). Binds its own mRNA. |
Cellular Location | Mitochondrion. Cytoplasm |
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Provided below are standard protocols that you may find useful for product applications.
Background
Dihydrofolate reductase converts dihydrofolate into tetrahydrofolate, a methyl group shuttle required for the de novo synthesis of purines, thymidylic acid, and certain amino acids. While the functional dihydrofolate reductase gene has been mapped to chromosome 5, multiple intronless processed pseudogenes or dihydrofolate reductase-like genes have been identified on separate chromosomes. Dihydrofolate reductase deficiency has been linked to megaloblastic anemia.
References
Cody,V., Proteins 65 (4), 959-969 (2006)
Stone,D., J. Biol. Chem. 254 (2), 480-488 (1979)
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