SULT1A2 Antibody (C-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, E |
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Primary Accession | P50226 |
Other Accession | NP_803564.1, NP_001045.1 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 34310 Da |
Antigen Region | 258-286 aa |
Gene ID | 6799 |
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Other Names | Sulfotransferase 1A2, ST1A2, Aryl sulfotransferase 2, Phenol sulfotransferase 2, Phenol-sulfating phenol sulfotransferase 2, P-PST 2, SULT1A2, STP2 |
Target/Specificity | This SULT1A2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 258-286 amino acids from the C-terminal region of human SULT1A2. |
Dilution | WB~~1:1000 |
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 | SULT1A2 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | SULT1A2 |
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Synonyms | STP2 |
Function | Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. Is also responsible for the sulfonation and activation of minoxidil. Mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk. |
Cellular Location | Cytoplasm. |
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Provided below are standard protocols that you may find useful for product applications.
Background
SULT1A2 catalyzes the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. Is also responsible for the sulfation and activation of minoxidil. Mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk.
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