PNOC Human

Prepronociceptin Human Recombinant
Cat. No.
BT7990
Source
Escherichia Coli.
Synonyms
Prepronociceptin, Nocistatin, OFQ, Pre-Pro-N/OFQ, Pronociceptin, Orphanin FQ, Nociceptin, PpN/OFQ, N/OFQ, PPNOC.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% 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.
Shipped with Ice Packs
In Stock

Description

PNOC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 180 amino acids (20-176) and having a molecular mass of 20.6kDa. 
PNOC is fused to a 23 amino acid His-tag at N-terminus.

Product Specs

Introduction
Prepronociceptin (PNOC) is a ligand for the opioid receptor-like receptor (OPRL1). It acts as a neurotransmitter in the brain, influencing pain perception and movement. PNOC may also play a role in the differentiation and development of neurons.
Description
Recombinant human PNOC, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 180 amino acids (residues 20-176). It has a molecular weight of 20.6 kDa. The PNOC protein is fused to a 23 amino acid His-tag at its N-terminus.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
PNOC protein solution at a concentration of 1 mg/ml in a buffer composed of 20 mM Tris-HCl (pH 8.0), 0.4 M urea, and 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), keep at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein like 0.1% HSA or BSA is recommended for long-term storage. Avoid repeated freezing and thawing.
Purity
Purity exceeds 90% as determined by SDS-PAGE analysis.
Synonyms
Prepronociceptin, Nocistatin, OFQ, Pre-Pro-N/OFQ, Pronociceptin, Orphanin FQ, Nociceptin, PpN/OFQ, N/OFQ, PPNOC.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSCQRDCL TCQEKLHPAL DSFDLEVCIL ECEEKVFPSP LWTPCTKVMA RSSWQLSPAA PEHVAAALYQ PRASEMQHLR RMPRVRSLFQ EQEEPEPGME EAGEMEQKQL QKRFGGFTGA RKSARKLANQ KRFSEFMRQY LVLSMQSSQR RRTLHQNGNV.

Product Science Overview

Preparation and Synthetic Routes

Recombinant human PNOC protein, fused to a His-tag at the N-terminus, is expressed in Escherichia coli (E. coli). The recombinant protein is typically purified using affinity chromatography techniques to achieve high purity levels .

Industrial Production Methods

The industrial production of recombinant human PNOC involves the following steps:

  1. Gene Cloning: The gene encoding PNOC is cloned into an expression vector that includes a His-tag for purification purposes.
  2. Transformation: The expression vector is introduced into E. coli cells through a process called transformation.
  3. Expression: The transformed E. coli cells are cultured under conditions that induce the expression of the recombinant PNOC protein.
  4. Purification: The recombinant protein is purified using affinity chromatography, which exploits the His-tag to isolate the protein from other cellular components.
  5. Characterization: The purified protein is characterized using techniques such as SDS-PAGE to confirm its purity and molecular weight .
Applications and Research

Prepronociceptin and its derived peptides are of significant interest in research due to their roles in pain modulation, neuronal differentiation, and development. They are also studied for their potential therapeutic applications in conditions such as postpartum depression and drug dependence .

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