
Thermo Fisher Scientific PTPRA Polyclonal Antibody
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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 F245-Y295. if (typeof window.$mangular === undefined
|| !window.$mangular) { window.$mangular = {}; } $mangular.antigenJson = \[{
targetFamily:
PTPRA,
uniProtId:
P18433-5,
ncbiNodeId:
9606,
antigenRange:
245-295,
antigenLength:
802,
antigenImageFileName:
PA5-102538_PTPRA_P18433-5_Rabbit.svg,
antigenImageFileNamePDP:
PA5-102538_PTPRA_P18433-5_Rabbit_PDP.jpeg,
sortOrder:
1}\]
; $mangular.isB2BCMGT = false
; $mangular.isEpitopesModalImageMultiSizeEnabled = true
;
View immunogen .st0{fill:#FFFFFF;} .st1{fill:#1E8AE7;}
Conjugate
Unconjugated Unconjugated Unconjugated
Form
Liquid
Concentration
1 mg/mL
Purification
Affinity 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_2851940
Product Specific Information
Antibody detects endogenous levels of total PTP alpha.
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.
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