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AB268897

Recombinant human PTP1B protein (Active)

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Recombinant human PTP1B protein (Active) is a Human Full Length protein, in the 1 to 435 aa range, expressed in Baculovirus infected Sf9 cells, with >70%, suitable for SDS-PAGE, FuncS.

View Alternative Names

PTP1B, PTPN1, Tyrosine-protein phosphatase non-receptor type 1, Protein-tyrosine phosphatase 1B, PTP-1B

2 Images
Functional Studies - Recombinant human PTP1B protein (Active) (AB268897)
  • FuncS

Supplier Data

Functional Studies - Recombinant human PTP1B protein (Active) (AB268897)

The specific activity of ab268897 was ~2,640 nmol/min/mg in a phosphatase assay using pNPP as substrate.

SDS-PAGE - Recombinant human PTP1B protein (Active) (AB268897)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant human PTP1B protein (Active) (AB268897)

SDS-PAGE analysis of ab268897.

Key facts

Purity

>70% SDS-PAGE

Expression system

Baculovirus infected Sf9 cells

Tags

GST tag N-Terminus

Applications

FuncS, SDS-PAGE

applications

Biologically active

Yes

Biological activity

The specific activity of ab268897 was ~2,640 nmol/min/mg in a phosphatase assay using pNPP as substrate.

Accession

P18031

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 25% Glycerol (glycerin, glycerine), 1.74% Sodium chloride, 0.42% MOPS, 0.31% Glutathione, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.002% PMSF

storage-buffer

Reactivity data

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

Sequence info

[{"sequence":"MEMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWKELSHEDLEPPPEHIPPPPRPPKRILEPHNGKCREFFPNHQWVKEETQEDKDCPIKEEKGSPLNAAPYGIESMSQDTEVRSRVVGGSLRGAQAASPAKGEPSLPEKDEDHALSYWKPFLVNMCVATVLTAGAYLCYRFLFNSNT","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":435,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Baculovirus infected Sf9 cells","accessionNumber":"P18031","tags":[{"tag":"GST","terminus":"N-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
True

Supplementary information

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

Protein tyrosine phosphatase 1B (PTP1B) is an enzyme involved in the dephosphorylation of tyrosine residues in proteins. Known also as PTPN1 this protein has a molecular weight of approximately 50 kDa. PTP1B is widely expressed in tissues but is highly present in the liver muscle and adipose tissue. It plays a critical role in regulating signal transduction pathways by removing phosphate groups from phosphotyrosine residues on target proteins. This action generally serves as a 'turn-off' switch for various signaling pathways.
Biological function summary

PTP1B plays important roles in glucose and lipid metabolism. It is not generally considered a part of a complex functioning instead as a singular enzyme. Its main action involves the negative regulation of the insulin signaling pathway by dephosphorylating the insulin receptor as well as its associated substrates. This regulation helps maintain normal levels of insulin sensitivity influencing cellular glucose uptake and metabolism.

Pathways

PTP1B has important functions in the insulin and leptin signaling pathways. It has a regulatory influence in these pathways affecting key metabolic processes. In the insulin signaling pathway PTP1B closely interacts with the insulin receptor as well as with insulin receptor substrates (IRS). Its dephosphorylating activity can lead to decreased insulin sensitivity. In the leptin pathway PTP1B modulates leptin signaling by dephosphorylating the Janus kinase 2 (JAK2) another protein involved in the control of energy balance and metabolism.

Excessive activity of PTP1B links with disorders such as type 2 diabetes and obesity. Overactivity of PTP1B can lead to insulin resistance contributing to the pathogenesis of type 2 diabetes. In obesity PTP1B may interfere with the normal activity of leptin a hormone critical for regulating energy balance. Its interaction with the insulin receptor and JAK2 makes PTP1B a target for therapeutic interventions aimed at improving insulin sensitivity and energy homeostasis.

Specifications

Form

Liquid

Additional notes

Affinity purified.

General info

Function

Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class 1 subfamily.

Post-translational modifications

Oxidized on Cys-215; the Cys-SOH formed in response to redox signaling reacts with the alpha-amido of the following residue to form a sulfenamide cross-link, triggering a conformational change that inhibits substrate binding and activity. The active site can be restored by reduction.. Ser-50 is the major site of phosphorylation as compared to Ser-242 and Ser-243. Activated by phosphorylation at Ser-50.. S-nitrosylation of Cys-215 inactivates the enzyme activity.. Sulfhydration at Cys-215 following endoplasmic reticulum stress inactivates the enzyme activity, promoting EIF2AK3/PERK activity.

Product protocols

Target data

Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET.
See full target information PTPN1

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