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AB42567

Recombinant Human PRL-1 protein (His tag C-Terminus)

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Recombinant Human PRL-1 protein (His tag C-Terminus) is a Human Full Length protein, in the 2 to 173 aa range, expressed in Escherichia coli, with >95%, suitable for Inhib.

View Alternative Names

PRL1, PTPCAAX1, PTP4A1, Protein tyrosine phosphatase type IVA 1, PTP(CAAXI), Protein-tyrosine phosphatase 4a1, Protein-tyrosine phosphatase of regenerating liver 1, PRL-1

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag C-Terminus

Applications

Inhib

applications

Biologically active

No

Accession

Q93096

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 50% Glycerol (glycerin, glycerine), 0.435% Sodium chloride, 0.395% Tris HCl, 0.307% Glutathione, 0.0584% EDTA, 0.05% Sorbitan monolaurate, ethoxylated, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "Inhib": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

0.45 U/ug. One unit will hydrolyze 1 pmol 6, 8-difluoro-4-methyl umbelliferyl phosphate (DiFMUP) per minute at pH 6.3 and 30ºC. Assay buffer: 50 mM Bis-Tris, pH 6.3, 2 mM EDTA, 2 mM DTT, 100 mM DiFMUP.

Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":"19.8 kDa","actualMolecularWeight":null,"aminoAcidEnd":173,"aminoAcidStart":2,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q93096","tags":[{"tag":"His","terminus":"C-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

PRL-1 also known as phosphatase of regenerating liver-1 or DIFMU-P is an enzyme that functions as a phosphatase. It has a molecular mass of approximately 20 kDa. PRL-1 is actively expressed in various tissues including the liver and skeletal muscle where it plays significant roles in cellular processes. Mechanically it exhibits a dual specificity for both tyrosine and serine/threonine residues enabling it to dephosphorylate target proteins which can regulate diverse signaling pathways.
Biological function summary

PRL-1 plays an important role in cell proliferation differentiation and migration. Its activity impacts cellular motility making it important for physiological and pathological processes. While PRL-1 primarily acts as a monomer it can also form complexes with other proteins amplifying its biological effects. Elevation in PRL-1 expression levels correlates with enhanced migratory capacity of tumor cells suggesting a role in cancer progression.

Pathways

Various cellular functions involve PRL-1 which participates in the MAPK and PI3K/Akt pathways. These pathways are critical in regulating cell cycle and survival. PRL-1's relation to proteins like AKT1 and ERK1/2 highlights its contribution to intracellular signaling cascades that drive growth and survival responses in cells. PRL-1's phosphatase activity influences these pathways by modulating the phosphorylation status of various substrate proteins impacting downstream signaling.

Increased expression of PRL-1 relates to cancer particularly colorectal and breast cancers. Its role in promoting cell proliferation and migration makes it a target of interest for cancer research. PRL-1 is connected with proteins such as p53 and E-cadherin within these contexts correlating with the loss of cell-cell adhesion and increased invasive characteristics in tumor cells. Targeting PRL-1 could provide therapeutic benefits in managing cancer-associated pathologies.

Specifications

Form

Liquid

General info

Function

Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. May play a role in the development and maintenance of differentiating epithelial tissues. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family.

Post-translational modifications

Farnesylated. Farnesylation is required for membrane targeting. Unfarnesylated forms are shifted into the nucleus.

Subcellular localisation

Early endosome

Product protocols

Target data

Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. May play a role in the development and maintenance of differentiating epithelial tissues. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis.
See full target information PTP4A1

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