Protein-Tyrosine Phosphatase H1 (PTPH1) Antibody

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Description
Phosphorylation of receptors by protein kinases is a process that can be reversed by a group of enzymes called protein phosphatases. Coordinated control of kinases and phosphatases provides the cell with the capacity to rapidly switch between phosphorylated and dephosphorylated protein states in dynamic response to environmental stimuli. Activation of critical enzymes by kinase phosphorylation alone is not enough to provide adequate regulation ?it is the combination with phosphatase dephosphorylation that effectively creates on/off switches to control cellular events. Errors in control, either through kinases or their counterpart phosphatases, can lead to unchecked cell growth attributable to human cancers and developmental disorders. Potential mechanisms to control dephosphorylation include changes in the expression of protein phosphatases, their subcellular localization, phosphorylation of phosphatase catalytic and regulatory subunits and regulation by endogenous phosphatase inhibitors. Most protein phosphatases are not stringently specific for their substrates. Consequently, changes in phosphatase activity may have a broad impact on dephosphorylation and turnover of phosphoproteins that are substrates for different kinases. This may be an important point of control to connect cellular circuitry of interrelated signaling pathways, and to synchronize physiological responses.
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Product specifications
| Category | Primary Antibodies |
| Immunogen Target | Target: Protein-Tyrosine Phosphatase H1 (PTPH1) Immunogen: KLH-conjugated synthetic peptide between 366-397 amino acids from the Central region of human PTPH1. |
| Host | Rabbit |
| Reactivity | Human, Mouse |
| Recommended Dilution | WB: 1/1000, IHC-P: 1/10 - 1/50. Not tested in IHC-F. Optimal dilutions/concentrations should be determined by the end user. |
| Clonality | Polyclonal |
| Conjugation | Unconjugated |
| Isotype | IgG |
| Observed MW | Calculated MW: 104 kDa |
| Purification | Purified through a protein G column, eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS. |
| Size 1 | 80 µl |
| Size 2 | 400 µl |
| Form | Liquid |
| Tested Applications | ELISA, WB, IHC |
| Buffer | PBS containing 0.09% sodium azide. |
| Availability | Shipped within 5-10 working days. |
| Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | P26045 |
| Background | Antibody anti-PTPH1 |
| Status | RUO |
| Note | THIS PRODUCT IS FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC, THERAPEUTIC OR COSMETIC PROCEDURES. NOT FOR HUMAN OR ANIMAL CONSUMPTION. |
Descripción
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Protein-Tyrosine Phosphatase H1 (PTPH1) Antibody
Phosphorylation of receptors by protein kinases is a process that can be reversed by a group of enzymes called protein phosphatases. Coordinated control of kinases and phosphatases provides the cell with the capacity to rapidly switch between phosphorylated and dephosphorylated protein states in dynamic response to environmental stimuli. Activation of critical enzymes by kinase phosphorylation alone is not enough to provide adequate regulation ?it is the combination with phosphatase dephosphorylation that effectively creates on/off switches to control cellular events. Errors in control, either through kinases or their counterpart phosphatases, can lead to unchecked cell growth attributable to human cancers and developmental disorders. Potential mechanisms to control dephosphorylation include changes in the expression of protein phosphatases, their subcellular localization, phosphorylation of phosphatase catalytic and regulatory subunits and regulation by endogenous phosphatase inhibitors. Most protein phosphatases are not stringently specific for their substrates. Consequently, changes in phosphatase activity may have a broad impact on dephosphorylation and turnover of phosphoproteins that are substrates for different kinases. This may be an important point of control to connect cellular circuitry of interrelated signaling pathways, and to synchronize physiological responses.
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