Mouse Monoclonal Sulfotyrosine antibody. Suitable for WB, IP, cELISA and reacts with Modified Amino Acid samples. Cited in 3 publications.
pH: 7.5
Preservative: 0.05% Sodium azide
Constituents: 1.35% Glycine, 1.21% Tris, 0.88% Sodium chloride
WB | IP | cELISA | |
---|---|---|---|
Modified Amino Acid | Tested | Expected | Expected |
Species | Dilution info | Notes |
---|---|---|
Species Modified Amino Acid | Dilution info 1/1000 | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Modified Amino Acid | Dilution info Use at an assay dependent concentration. | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Modified Amino Acid | Dilution info Use at an assay dependent concentration. | Notes - |
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Mouse Monoclonal Sulfotyrosine antibody. Suitable for WB, IP, cELISA and reacts with Modified Amino Acid samples. Cited in 3 publications.
pH: 7.5
Preservative: 0.05% Sodium azide
Constituents: 1.35% Glycine, 1.21% Tris, 0.88% Sodium chloride
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Sulfotyrosine is a post-translational modification of the amino acid tyrosine where a sulfate group gets added to the phenolic hydroxyl moiety. This process is known as tyrosine sulfation and plays a critical role in protein-protein interactions. Tyrosine sulfation occurs primarily in the Golgi apparatus and is mediated by tyrosylprotein sulfotransferases. It doesn't refer to a single protein but rather the chemical modification found on various proteins. The distinct molecular mass for the modification itself is about 80 Da taking into account the addition of the sulfate group. This modification mostly appears in secretory and membrane proteins across a wide range of tissues and organisms.
The sulfotyrosine modification significantly enhances the binding properties of proteins involved in diverse biological processes. It affects proteins such as adhesion molecules G protein-coupled receptors and coagulation factors often being essential for their proper function. Many proteins containing sulfotyrosine participate in forming multi-protein complexes that mediate cell signaling and communication.
Sulfotyrosine modifications integrate notably into signal transduction and immune response pathways. Proteins like P-selectin glycoprotein ligand-1 (PSGL-1) and chemokine receptors such as CCR5 require sulfotyrosine for optimal receptor-ligand interactions which impacts leukocyte trafficking and chemotaxis. These modifications often serve as docking sites for other proteins coordinating complex pathways important for cellular responses.
Sulfotyrosine modifications have implications in inflammatory diseases and cancer. The modification plays a role in mediating the interactions involving proteins like PSGL-1 in immune response pathways which are critical in inflammatory diseases such as rheumatoid arthritis. Additionally abnormal tyrosine sulfation on chemokine receptors like CCR5 has associations with the metastatic properties of cancer influencing both tumor development and immune evasion mechanisms. Their correlation emphasizes the importance of understanding sulfotyrosine's functional roles in disease pathogenesis.
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All lanes: Western blot - Anti-Sulfotyrosine antibody [Sulfo-1C-A2] (ab136481) at 1/1000 dilution
Lane 1: Purified bovine fibrinogen treated with 1.5 mg/ml abalone sulfatase at 37°C overnight.
Lane 2: Purified bovine fibrinogen
All lanes: Goat anti-mouse secondary antibody conjugated to HRP at 1/2000 dilution
Developed using the ECL technique.
Lanes 1 - 3: control IgG
Lanes 4 - 6: Western blot - Anti-Sulfotyrosine antibody [Sulfo-1C-A2] (ab136481) at 1/1000 dilution
Lanes 1 and 4: 3T3/NIH cell lysate
Lanes 2 and 5: HEK 293 cell lysate
Lanes 3 and 6: Bovine cardiac tissue lysate
All lanes: Goat anti-mouse secondary antibody conjugated to HRP at 1/2000 dilution
Developed using the ECL technique.
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