Western Blotting (WB), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p))
Purification
This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis
Immunogen
This PTPH1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 366-397 amino acids from the Central region of human PTPH1.
PTPN3
Reactivity: Human
ELISA
Host: Rabbit
Polyclonal
Biotin
Application Notes
For WB starting dilution is: 1:1000
For IHC-P starting dilution is: 1:10~50
Restrictions
For Research Use only
Format
Liquid
Concentration
2 mg/mL
Buffer
Supplied in PBS with 0.09 % (W/V) sodium azide.
Preservative
Sodium azide
Precaution of Use
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage
4 °C,-20 °C
Storage Comment
Store at 4°C for three months and -20°C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
Target
PTPN3
(Protein tyrosine Phosphatase, Non-Receptor Type 3 (PTPN3))
PTP-H1 antibody, PTPH1 antibody, 9530011I20Rik antibody, PTPCL antibody, protein tyrosine phosphatase, non-receptor type 3 antibody, PTPN3 antibody, Ptpn3 antibody
Background
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.