PTEN Human, His

Phosphatase and Tensin homolog Human Recombinant, His Tag
Cat. No.
BT3780
Source
Escherichia Coli.
Synonyms
Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN, EC 3.1.3.67, EC 3.1.3.16, EC 3.1.3.48, Phosphatase and tensin homolog, Mutated in multiple advanced cancers 1, PTEN, MMAC1, TEP1, BZS, MHAM, PTEN1, 10q23del, MGC11227.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

PTEN Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 423 amino acids (1- 403 a.a.) and having a molecular mass of 49.3kDa.
The PTEN is purified by proprietary chromatographic techniques.

Product Specs

Introduction
PTEN, a tumor suppressor, plays a crucial role in suppressing tumor development and is found in various organisms, from humans to worms. It possesses a tensin-like domain and a catalytic domain resembling dual-specificity protein tyrosine phosphatases. PTEN functions as a phosphatase, acting on both proteins and 3-phosphorylated phosphoinositides, thereby regulating signal transduction pathways involving lipid second messengers. Unlike most protein tyrosine phosphatases, PTEN exhibits a preference for dephosphorylating phosphoinositide substrates. By regulating intracellular levels of phosphatidylinositol-3,4,5-trisphosphate, PTEN acts as a tumor suppressor by negatively regulating the AKT/PKB signaling pathway, influencing cell survival signaling.
Description
Recombinant Human PTEN, with an N-terminal 20-amino acid His tag, is produced in E. coli. This non-glycosylated polypeptide chain consists of 423 amino acids (1-403 a.a.) and has a molecular weight of 49.3 kDa. The protein is purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
The PTEN solution is formulated in 20mM Tris-HCl buffer (pH 8.0) containing 1mM EDTA, 2mM DTT, 100mM NaCl, and 20% glycerol.
Stability
For short-term storage (up to 4 weeks), store the entire vial at 4°C. For extended storage, freeze the product at -20°C. To ensure long-term stability, it is advisable to add a carrier protein (0.1% HSA or BSA) before freezing. Avoid repeated freeze-thaw cycles.
Purity
The purity is determined to be greater than 85.0% via SDS-PAGE analysis.
Synonyms
Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN, EC 3.1.3.67, EC 3.1.3.16, EC 3.1.3.48, Phosphatase and tensin homolog, Mutated in multiple advanced cancers 1, PTEN, MMAC1, TEP1, BZS, MHAM, PTEN1, 10q23del, MGC11227.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTAIIKEIVS RNKRRYQEDG FDLDLTYIYP NIIAMGFPAE RLEGVYRNNI DDVVRFLDSK HKNHYKIYNL CAERHYDTAK FNCRVAQYPF EDHNPPQLEL IKPFCEDLDQ WLSEDDNHVA AIHCKAGKGR TGVMICAYLL HRGKFLKAQE ALDFYGEVRT RDKKGVTIPS QRRYVYYYSY LLKNHLDYRP VALLFHKMMF ETIPMFSGGT CNPQFVVCQL KVKIYSSNSG PTRREDKFMY FEFPQPLPVC GDIKVEFFHK QNKMLKKDKM FHFWVNTFFI PGPEETSEKV ENGSLCDQEI DSICSIERAD NDKEYLVLTL TKNDLDKANK DKANRYFSPN FKVKLYFTKT VEEPSNPEAS SSTSVTPDVS DNEPDHYRYS DTTDSDPENE PFDEDQHTQI TKV.

Product Science Overview

Structure and Function

PTEN contains a tensin-like domain and a catalytic domain similar to that of dual-specificity protein tyrosine phosphatases . Unlike most protein tyrosine phosphatases, PTEN preferentially dephosphorylates phosphoinositide substrates . This activity is crucial for negatively regulating the intracellular levels of phosphatidylinositol-3,4,5-trisphosphate (PIP3), thereby inhibiting the AKT/PKB signaling pathway . The inhibition of this pathway is essential for controlling cell proliferation and survival, making PTEN a vital tumor suppressor .

Human Recombinant PTEN with His Tag

Recombinant PTEN is often produced in various expression systems to study its function and for potential therapeutic applications . The human recombinant PTEN with a His Tag is a form of PTEN that has been genetically engineered to include a polyhistidine tag at the N-terminus . This His Tag facilitates the purification of the protein using affinity chromatography techniques, making it easier to isolate and study .

Clinical Significance

Mutations in the PTEN gene are associated with a wide range of cancers, including glioblastoma, lung cancer, breast cancer, and prostate cancer . The loss of PTEN function leads to uncontrolled cell growth and proliferation due to the unchecked activation of the AKT/PKB signaling pathway . Therefore, PTEN is a critical target for cancer research and therapeutic development .

Research and Applications

Recombinant PTEN with a His Tag is widely used in research to understand its role in various cellular processes and its implications in cancer . By studying the recombinant protein, researchers can gain insights into the mechanisms of PTEN function and develop potential therapeutic strategies to restore its activity in cancer cells .

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