PEST (PTPN12), GST-tag Recombinant

SKU:BHP18200035
Research Validated
Overview
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Recombinant PEST Human protein, N-terminal GST-tag. Spanning aa 2-300. Produced in E. coli. Suitable for binding assays, inhibitor screening, and drug discovery.
Expression System E. coli
Affinity Tag N-terminal GST-tag
Biosafety Level BSL-1
Expression Region aa 2-300
Specific Activity 76 pmole/min/µg
UniProt ID Q05209
Options selector
Catalog no. Size
30023 50 ug
Available Options

Select the variant that best fits your experiment. Availability and lead time may vary by option.

  • Options — Size: 50 ug
  • Lead time: options listed in “Availability Content”; other statuses may take longer.
  • Storage: >12 months at -80°C
  • Shipping: Shipped at -80°C (dry ice) (dry ice).
  • Upon receipt: store at recommended temperature as soon as possible.
  • Sales terms and conditions: Please review prior to ordering.
Field Specification
Mfr No 30023
Alternative Names PTP-PEST, PTPG1, tcag7.1075, PTPN12
Formulation 40 mM Tris-HCl, pH 8.0, 110 mM NaCl, 2.2 mM KCl, 3 mM DTT, 20% glycerol, and 16 mM glutathione
Molecular Weight 61.4 kDa
Product Type
  • Recombinant Protein
Shipping -80°C (dry ice)
Species Human
Storage >12 months at -80°C
UniProt # Q05209

Scientific Background

Protein tyrosine phosphatase-PEST (PTPN12), a ubiquitously expressed cytoplasmic tyrosine phosphatase, is thought to play an important role in cell adhesion and motility, cell migration, and signal transduction for antigen receptors in B and T lymphocytes. Signal transduction via tyrosine phosphorylation, normally fine-tuned by the concerted action of both protein tyrosine kinases and protein tyrosine phosphatases (PTPs), is a key mechanism in tumorigenesis. Studies suggest potential role for PTP-PEST in regulation of p130(cas) in mitogen- and cell adhesion-induced signaling events.

Product Description

E. coli Expression

Recombinant PEST Human protein is produced using a validated E. coli expression system and supplied in aqueous buffer solution. Suitable for enzyme kinetics, inhibitor screening, binding assays, structural studies, and related biochemical research applications.

Protein Specifications

UniProt ID Q05209
Expression System E. coli
Amino Acids / Region 2-300
Affinity Tag N-terminal GST-tag
Molecular Weight 61.4 kDa
Formulation 40 mM Tris-HCl, pH 8.0, 110 mM NaCl, 2.2 mM KCl, 3 mM DTT, 20% glycerol, and 16 …
Storage >12 months at -80°C
Biosafety Level Not applicable (BSL-1)
✓ Purity Verified

Specific Activity

76 pmole/min/µg

Safety & Handling

Avoid freeze/thaw cycles.

What expression system was used and why does it matter for enzymatic activity?

This protein was produced in E. coli. Expression system selection determines post-translational processing, disulfide bond formation, and co-factor incorporation — all of which affect enzymatic activity. Insect cell (Sf9) systems are preferred for kinases and multi-subunit enzymes that require phosphorylation or chaperone assistance; E. coli is used for structurally simpler proteins.

What amino acid region is included in this construct?

This protein spans amino acids 2-300. Confirm the region includes your domain of interest — the active site, binding pocket, or substrate recognition sequence — before placing your order. Refer to the UniProt database for domain annotation.

What is the purity and how was it verified?

Purity is assessed by SDS-PAGE; see the Certificate of Analysis. A gel image is provided with each lot. BPS Bioscience performs rigorous QC on each lot, including purity assessment and functional activity testing where applicable. Contact technical support if purity ≥99% is required for biophysical measurements.

What applications is this protein suitable for?

Useful for the study of enzyme kinetics and regulation, to dephosphorylate target substrates and for screening inhibitors. Refer to the product datasheet for validated protocols and recommended assay conditions. Contact BioHippo technical support for application-specific guidance.

How should this protein be stored and handled?

>12 months at -80°C Avoid repeated freeze-thaw cycles — prepare single-use working aliquots. Add BSA or glycerol to aliquots if storing diluted enzyme is necessary. Typical stability is at least 6 months at −80°C.

BioHippo offers flexible sourcing for qualified research institutions and partners.

  • Bulk quantities: Large-scale orders for HTS campaigns or structural studies.
  • Custom constructs: Alternative tag positions, truncation variants, or point mutants may be available upon request.
  • Biotinylated variants: Avi-Tag site-specific biotinylation is available for SPR/BLI surface capture applications.
  • Extended QC data: Activity assay data, SEC-HPLC profiles, or additional purity methods available on request.

Contact BioHippo customer support for custom requirements.

  1. J.F. Cote, et al., J Biol Chem. 2002, 277: 2973-86.
  2. K. Horsch et al., Mol Endocrinol. 2001, 12: 2182-96.
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Experience the power of Celltrypse™, c-LEcta's innovative enzyme solution for gentle and efficient cell dissociation. Request your free sample and discover a superior alternative for your cell culture workflows.

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