Thermo Fisher Scientific Phospho-PTPRA (Ser180) Polyclonal Antibody

Applications

Tested Dilution

Publications

Western Blot (WB)

1:500-1:2,000

-

Immunohistochemistry (Paraffin) (IHC (P))

1:100-1:500

-

Immunohistochemistry (Frozen) (IHC (F))

1:100-1:500

-

Immunocytochemistry (ICC/IF)

1:50-1:200

-

ELISA (ELISA)

1:500-1:1,000

-

Product Specifications

Species Reactivity

Human, Mouse, Rat

Host/Isotype

Rabbit / IgG

Class

Polyclonal

Type

Antibody

Immunogen

KLH conjugated synthetic phosphopeptide derived from human PTPRA around the phosphorylation site of Ser180. if (typeof window.$mangular === undefined || !window.$mangular) { window.$mangular = {}; } $mangular.antigenJson = \[{targetFamily:PTPRA,uniProtId:P18433-5,ncbiNodeId:9606,antigenRange:180,antigenLength:802,antigenImageFileName:BS-5175R_PTPRA_P18433-5_Rabbit.svg,antigenImageFileNamePDP:BS-5175R_PTPRA_P18433-5_Rabbit_PDP.jpeg,sortOrder:1}\]; $mangular.isB2BCMGT = false; $mangular.isEpitopesModalImageMultiSizeEnabled = true;

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Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

1 mg/mL

Purification

Protein A

Storage buffer

0.01M TBS, pH 7.4, with 50% glycerol, 1% BSA

Contains

0.02% ProClin 300

Storage conditions

-20°C

Shipping conditions

Ambient (domestic); Wet ice (international)

Target Information

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.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.