Recombinant Human Tyrosine-Protein Phosphatase Non-Receptor Type 5 (PTPN5) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-04465P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) PTPN5.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) PTPN5.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) PTPN5.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) PTPN5.

Recombinant Human Tyrosine-Protein Phosphatase Non-Receptor Type 5 (PTPN5) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-04465P
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Product Overview

Description Recombinant Human Tyrosine-Protein Phosphatase Non-Receptor Type 5 (PTPN5) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P54829
Target Symbol PTPN5
Synonyms FLJ14427; Neural specific protein tyrosine phosphatase; Neural-specific protein-tyrosine phosphatase; Protein tyrosine phosphatase non receptor type 5 (striatum enriched); Protein tyrosine phosphatase non receptor type 5; Protein tyrosine phosphatase striatum enriched; PTN5; PTN5_HUMAN; PTP STEP; PTPN 5; Ptpn5; PTPSTEP; STEP; Striatum-enriched protein-tyrosine phosphatase; Tyrosine protein phosphatase non receptor type 5; Tyrosine-protein phosphatase non-receptor type 5
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence LQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDPDDPLSSYINANYIRGYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNEKCTEYWPEEQVAYDGVEITVQKVIHTEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVMSLY
Expression Range 300-555aa
Protein Length Partial
Mol. Weight 45.5kDa
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function May regulate the activity of several effector molecules involved in synaptic plasticity and neuronal cell survival, including MAPKs, Src family kinases and NMDA receptors.
Subcellular Location Endoplasmic reticulum membrane; Multi-pass membrane protein.
Protein Families Protein-tyrosine phosphatase family, Non-receptor class subfamily
Database References

HGNC: 9657

OMIM: 176879

KEGG: hsa:84867

STRING: 9606.ENSP00000351342

UniGene: PMID: 28389375

  • a dual role for PSD-95 in stabilizing synaptic NMDARs by binding directly to GluN2B but also by promoting synaptic exclusion and degradation of the negative regulator STEP61. PMID: 27457929
  • STEP is involved in the mechanism of depressive disorders and it is a promising molecular target for atypical antidepressant drugs of new generation. (Review) PMID: 28699511
  • Data suggest that PP5/PTPN5 is overexpressed in liver samples from patients with hepatocellular carcinoma (HCC); overexpression of PP5/PTPN5 appears to correlate with tumor burden/stage. Inhibition of PP5/PTPN5 suppresses proliferation and promotes apoptosis of HCC cells; inhibition of PP5/PTPN5 involves activation of AMPK. PMID: 28528695
  • A rare missense variant in the PTPN5 gene (rs56234898; minor allele frequency 1.5%) was significantly associated with decreased severity of Post-Burn Hypertrophic Scarring(P = 1.3x10-6). PMID: 26872063
  • STEP levels are unchanged in pre-frontal cortex and associative striatum in post-mortem human brain samples from subjects with schizophrenia, bipolar disorder and major depressive disorder PMID: 25786133
  • Article focuses on the most recent findings on STEP, discuss how STEP expression and activity are maintained during normal cognitive function, and how disruptions in STEP activity contribute to a number of illnesses. [Review] PMID: 25218562
  • Decreased STEP protein activation in corpus striatum contributes to early enhanced apoptotic signaling in YAC model transgenic mice. PMID: 24588402
  • This experiments demonstrated that deletion of STEP can enhance experience-induced neuroplasticity and memory formation PMID: 22885232
  • The results imply a model in which PTPN5 may play a role in normal cognitive functioning and contribute to aspects of the neuropathology of schizophrenia. PMID: 22555153
  • This study identified a novel role for PTPN5 in mediating the development of stress-related cognitive and morphological changes. PMID: 22649233
  • STEP(61kDa) is required for Abeta transgene-mediated internalization of GluA1/GluA2 glutamate receptors in a transgenic mousemodel. PMID: 21883219
  • STEP contributes to aspects of the pathophysiology in Alzheimer's disease; loss of GluN1/GluN2B subunits from neuronal membranes and Abeta-mediated NMDAR internalization are discussed PMID: 20699650
  • findings show that STEP(61) levels are progressively increased in the prefrontal cortex of Alzheimer disease brains PMID: 20427654
  • determined high-resolution structures of all of the human family members of Mitogen-Activated Protein Kinase-specific protein tyrosine phosphatases PMID: 16441242
  • in colorectal tumors, microsatellite repeats mutation rates are higher than the mean mutation frequency PMID: 19000305
  • FAQs

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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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