Rabbit Polyclonal TR1 antibody. Suitable for IHC-P and reacts with Human samples. Cited in 3 publications. Immunogen corresponding to Synthetic Peptide within Human TAS1R1.
pH: 7.4
Preservative: 0.099% Sodium azide
Constituents: PBS
IHC-P | |
---|---|
Human | Tested |
Mouse | Predicted |
Rat | Predicted |
Dog | Predicted |
Hamster | Predicted |
Horse | Predicted |
Monkey | Predicted |
Pig | Predicted |
Rabbit | Predicted |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 6 µg/mL | Notes Perform heat-mediated antigen retrieval before commencing with IHC staining protocol. |
Species | Dilution info | Notes |
---|---|---|
Species Mouse, Rat, Rabbit, Horse, Hamster, Dog, Pig, Monkey | Dilution info - | Notes - |
Putative taste receptor. TAS1R1/TAS1R3 responds to the umami taste stimulus (the taste of monosodium glutamate). Sequence differences within and between species can significantly influence the selectivity and specificity of taste responses.
GPR70, T1R1, TR1, GM148, TAS1R1, Taste receptor type 1 member 1, G-protein coupled receptor 70
Rabbit Polyclonal TR1 antibody. Suitable for IHC-P and reacts with Human samples. Cited in 3 publications. Immunogen corresponding to Synthetic Peptide within Human TAS1R1.
pH: 7.4
Preservative: 0.099% Sodium azide
Constituents: PBS
BLAST analysis of the peptide immunogen showed no homology with other human proteins, except TAS1R2 (69%).
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Thioredoxin reductase 1 (TR1) also known as TXNRD1 is an enzyme that is part of a family of pyridine nucleotide disulfide oxidoreductases. It catalyzes the reduction of thioredoxin using NADPH as an electron donor to maintain cellular redox balance. TR1 is a homodimeric protein with each subunit weighing approximately 55 kDa. It is found expressed in many tissues with higher levels noted in the liver kidney and testis reflecting its diverse cellular roles.
TR1 influences cellular redox homeostasis and plays a significant role in regulating oxidative stress. It operates as a standalone enzyme not as part of a larger protein complex. By reducing disulfide bonds in proteins it helps to protect cells from oxidative damage and maintains the reduced state of cellular thiols. TR1 also contributes to the regulation of cell proliferation and apoptosis reflecting its multifaceted roles in both normal cellular processes and responses to cellular stress.
TR1 takes part in both the oxidative stress response and the regulation of cellular metabolism. It is key within the thioredoxin system pathway working closely with thioredoxin (Trx) to detoxify reactive oxygen species. Additionally TR1 interacts with proteins such as Trx in the regulation of signaling pathways related to apoptosis. Together these interactions facilitate cellular responses to environmental changes.
TR1 displays significant roles in cancer and neurodegenerative diseases. It is frequently overexpressed in various cancer types which can contribute to tumor growth and resistance to therapies. The enzyme also shows connections to neurodegenerative disorders where imbalance in redox regulation and oxidative stress are common pathological features. In both contexts TR1 interacts closely with proteins like thioredoxin further emphasizing its critical place in disease pathogenesis.
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This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
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Formalin-fixed paraffin-embedded human colon carcinoma tissue stained for TR1 with ab230788 at 6 μg/ml in immunohistochemical analysis.
Formalin-fixed paraffin-embedded human non-small cell lung carcinoma tissue stained for TR1 with ab230788 at 6 μg/ml in immunohistochemical analysis.
Formalin-fixed paraffin-embedded human testis tissue stained for TR1 with ab230788 at 6 μg/ml in immunohistochemical analysis.
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