PTPµ (PTPRM), GST-tag Recombinant

SKU:BHP18200044
Research Validated
Overview
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Recombinant PTPµ Human protein, N-terminal GST-tag. Spanning aa 896-1175. 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 896-1175
Specific Activity 60 U/µg
UniProt ID P28827
Options selector
Catalog no. Size
30053 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 30053
Formulation 25 mM Tris-HCl, pH 8.0, 75 mM NaCl, 0.05% Tween-20, 50% glycerol, 2 mM EDTA, 1 mM DTT, 10 mM glutathione
Molecular Weight 56.2 kDa
Product Type
  • Recombinant Protein
Shipping -80°C (dry ice)
Species Human
Storage >12 months at -80°C
UniProt # P28827

Scientific Background

PTPRM is a member of the protein tyrosine phosphatase family and can participate in a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. PTPRM has been shown to mediate cell-cell aggregation through the interaction with another molecule of PTPRM on an adjacent cell. PTPRM can interact with scaffolding protein RACK1/GNB2L1 and this interaction may be necessary for downstream signaling in response to cell-cell adhesion. PTPRM has been shown to be expressed in human pulmonary vascular endothelia where it directly binds to VE-cadherin and regulates both the tyrosine phosphorylation state of VE-cadherin and barrier integrity.

Product Description

E. coli Expression

Recombinant PTPµ 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 P28827
Expression System E. coli
Amino Acids / Region 896-1175
Affinity Tag N-terminal GST-tag
Molecular Weight 56.2 kDa
Formulation 25 mM Tris-HCl, pH 8.0, 75 mM NaCl, 0.05% Tween-20, 50% glycerol, 2 mM EDTA, 1 m…
Storage >12 months at -80°C
Biosafety Level Not applicable (BSL-1)
✓ Purity Verified

Specific Activity

60 U/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 896-1175. 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. S. Brady-Kalnay, et al., J. Cell Biol 1995, 130: 977.
  2. T. Mourton, et al., J. Biol. Chem. 2002, 276:14896.
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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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