Thermo Fisher Scientific Phospho-PTPRA (Tyr271) Polyclonal Antibody

Applications

Tested Dilution

Publications

Western Blot (WB)

1:500-1:2,000

-

Immunohistochemistry (Paraffin) (IHC (P))

1:50-1:200

-

Immunocytochemistry (ICC/IF)

1:100-1:500

-

Product Specifications

Species Reactivity

Human, Mouse, Rat

Host/Isotype

Rabbit / IgG

Class

Polyclonal

Type

Antibody

Immunogen

A synthesized peptide derived from human PTPRA(Accession P18433), corresponding to amino acid residues around phosphorylated Tyr271. if (typeof window.$mangular === undefined || !window.$mangular) { window.$mangular = {}; } $mangular.antigenJson = \[{targetFamily:PTPRA,uniProtId:P18433-5,ncbiNodeId:9606,antigenRange:271,antigenLength:802,antigenImageFileName:PA5-105519_PTPRA_P18433-5_Rabbit.svg,antigenImageFileNamePDP:PA5-105519_PTPRA_P18433-5_Rabbit_PDP.jpeg,sortOrder:1}\]; $mangular.isB2BCMGT = false; $mangular.isEpitopesModalImageMultiSizeEnabled = true;

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Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

1 mg/mL

Purification

sequential chromatography

Storage buffer

PBS, pH 7.4, with 50% glycerol

Contains

0.02% sodium azide

Storage conditions

-20°C

Shipping conditions

Wet ice

RRID

AB_2816947

Product Specific Information

Antibody detects endogenous levels of PTP alpha only when phosphorylated at Tyr271.

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.