NTS Human, sf9

Neurotensin Human Recombinant, sf9
Cat. No.
BT1625
Source
Sf9, Baculovirus cells.
Synonyms
Neurotensin/neuromedin N, NTS, Neuromedin N, NN, NmN, NT, NmN-125.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 90.0% as determined by analysis 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.
Shipped with Ice Packs
In Stock

Description

NTS Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 134 amino acids (24-148) and having a molecular mass of 15.4kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).
NTS is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Neurotensin (NTS), a precursor to neuromedin N and neurotensin peptides, is a tridecapeptide found throughout the central nervous system. It is believed to function as a neurotransmitter or neuromodulator. NTS plays a role in dopamine-related processes, gut health, and fat metabolism. In certain tissues, larger forms of neuromedin N and neurotensin may be produced, potentially offering enhanced stability and bioactivity.
Description
Recombinant Human NTS, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain with a molecular weight of 15.4kDa (134 amino acids, 24-148). SDS-PAGE analysis may show a molecular size of approximately 13.5-18kDa. The NTS protein is fused to a 6 amino acid His-Tag at the C-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
A clear, sterile-filtered solution.
Formulation
The NTS protein solution (1mg/ml) is supplied in Phosphate Buffered Saline (pH 7.4) with 10% glycerol.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity exceeds 90.0% as determined by SDS-PAGE analysis.
Synonyms
Neurotensin/neuromedin N, NTS, Neuromedin N, NN, NmN, NT, NmN-125.
Source
Sf9, Baculovirus cells.
Amino Acid Sequence
ADPSDSEEEM KALEADFLTN MHTSKISKAH VPSWKMTLLN VCSLVNNLNS PAEETGEVHE EELVARRKLP TALDGFSLEA MLTIYQLHKI CHSRAFQHWE LIQEDILDTG NDKNGKEEVI KRKIPYILHH HHHH.

Product Science Overview

Physiological Functions

Neurotensin has a variety of physiological roles:

  • In the CNS: It is involved in the regulation of dopamine pathways, which has implications for conditions such as schizophrenia and Parkinson’s disease . Neurotensin also exhibits opioid-independent analgesic properties .
  • In the gastrointestinal tract: It increases intestinal motility, stimulates pancreatic and biliary secretions, and promotes the growth of tissues such as the gut, pancreas, adrenal gland, and liver .
Receptors

Neurotensin exerts its effects through three main receptors:

  1. Neurotensin receptor 1 (NTSR1): A seven-transmembrane G-protein coupled receptor that has a high affinity for neurotensin .
  2. Neurotensin receptor 2 (NTSR2): Another seven-transmembrane G-protein coupled receptor .
  3. Neurotensin receptor 3 (NTSR3): Also known as sortilin 1, this is a single transmembrane domain sorting receptor .
Role in Cancer

Neurotensin and its receptors have been implicated in the proliferation, migration, and DNA synthesis of tumor cells . The NT/NTSR1 complex, in particular, activates phospholipase C (PLC), leading to the production of inositol triphosphate (IP3) and diacylglycerol (DAG) from membrane phospholipids . This signaling pathway is crucial for various cellular processes, including those involved in cancer progression .

Recombinant Neurotensin (Human, sf9)

Recombinant neurotensin is produced using various expression systems, including the sf9 insect cell line. This recombinant form is often tagged with a His-tag for purification purposes and is used in research to study the peptide’s functions and interactions . The recombinant protein is typically expressed in E. coli and purified to a high degree of purity .

Applications

Recombinant neurotensin is used in various research applications, including:

  • Functional studies: To understand its role in neurotransmission and neuromodulation.
  • Cancer research: To study its involvement in tumor growth and metastasis.
  • Drug development: As a potential target for therapeutic interventions in conditions like schizophrenia, Parkinson’s disease, and cancer .

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