CTPS2 Antibody (N-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| FC, WB, E |
---|---|
Primary Accession | Q9NRF8 |
Other Accession | Q5U2N0, P70303, Q1RMS2 |
Reactivity | Human |
Predicted | Bovine, Mouse, Rat |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 65678 Da |
Antigen Region | 77-105 aa |
Gene ID | 56474 |
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Other Names | CTP synthase 2, CTP synthetase 2, UTP--ammonia ligase 2, CTPS2 |
Target/Specificity | This CTPS2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 77-105 amino acids from the N-terminal region of human CTPS2. |
Dilution | WB~~1:1000 FC~~1:10~50 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
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 | CTPS2 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | CTPS2 |
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Function | Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Constitutes the rate-limiting enzyme in the synthesis of cytosine nucleotides. |
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Provided below are standard protocols that you may find useful for product applications.
Background
CTPS2 catalyzes the formation of CTP from UTP with the concomitant eamination of glutamine to glutamate. This protein is the rate-limiting enzyme in the synthesis of cytosine nucleotides, which play an important role in various metabolic processes and provide the precursors necessary for the synthesis of RNA and DNA. Cancer cells that exhibit increased cell proliferation also exhibit an increased activity of this encoded protein. Thus, this protein is an attractive target for selective chemotherapy.
References
Olsen,J.V., et.al., Cell 127 (3), 635-648 (2006)
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