NXPH1 Human

Neurexophilin 1 Human Recombinant
Cat. No.
BT2106
Source
Escherichia Coli.
Synonyms
Nbla00697, NPH1, Neurexophilin-1, NXPH1.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

NXPH1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 273 amino acids (22-271) and having a molecular mass of 31kDa. NXPH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Neurexophilin 1 (NXPH1) belongs to the neurexophilin family and is involved in cell adhesion within the nervous system. This protein forms a strong complex with alpha neurexins, facilitating interactions between dendrites and axons.
Description
This recombinant NXPH1 protein is produced in E. coli and consists of 273 amino acids (22-271) with a molecular weight of 31kDa. It includes a 23 amino acid His-tag at the N-terminus for purification purposes.
Physical Appearance
Clear solution that has been sterilized by filtration.
Formulation
The NXPH1 protein is provided at a concentration of 0.5mg/ml in a buffer containing 20mM Tris-HCl (pH 8.0), 0.4M UREA, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For longer periods, store frozen at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freezing and thawing.
Purity
Purity is greater than 90% as assessed by SDS-PAGE.
Synonyms
Nbla00697, NPH1, Neurexophilin-1, NXPH1.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSANLTNGG KSELLKSGSS KSTLKHIWTE SSKDLSISRL LSQTFRGKEN DTDLDLRYDT PEPYSEQDLW DWLRNSTDLQ EPRPRAKRRP IVKTGKFKKM FGWGDFHSNI KTVKLNLLIT GKIVDHGNGT FSVYFRHNST GQGNVSVSLV PPTKIVEFDL AQQTVIDAKD SKSFNCRIEY EKVDKATKNT LCNYDPSKTC YQEQTQSHVS WLCSKPFKVI CIYISFYSTD YKLVQKVCPD YNYHSDTPYF PSG.

Product Science Overview

Structure and Characteristics

Neurexophilin 1 is characterized by its unique structure, which includes:

  • N-terminal signal peptide: This segment directs the protein to the secretory pathway.
  • Variable N-terminal domain: This domain varies among different neurexophilins.
  • Highly conserved central domain: This domain is N-glycosylated, meaning it has sugar molecules attached to it.
  • Short linker region: This region connects the central domain to the C-terminal domain.
  • Cysteine-rich C-terminal domain: This domain is essential for the protein’s stability and function .
Function and Interaction

Neurexophilin 1 forms a tight complex with alpha-neurexins (α-neurexins), which are proteins that promote adhesion between dendrites and axons. This interaction is crucial for synaptic function and the formation of neural circuits . Neurexophilin 1 is physiologically processed in neuronal cells, where it undergoes N-glycosylation and proteolytic cleavage to form a mature protein .

Expression and Processing

Neurexophilin 1 is expressed in various tissues, including the brain, where it plays a role in synaptic signaling. The protein is rapidly N-glycosylated after synthesis and then slowly processed to a smaller mature form through endoproteolytic cleavage. This processing occurs specifically in neuron-like cells, indicating a cell-specific mechanism .

Recombinant Neurexophilin 1

Recombinant Neurexophilin 1 is produced using genetic engineering techniques, where the NXPH1 gene is inserted into a host cell, such as bacteria or mammalian cells, to produce the protein. This recombinant protein is used in research to study its structure, function, and interactions with other proteins, such as neurexins .

Research and Applications

Research on Neurexophilin 1 has provided insights into its role in the nervous system and its potential implications in neurological disorders. Studies have shown that Neurexophilin 1 can suppress the proliferation of hematopoietic cells, indicating its potential role in regulating cell growth and differentiation . Additionally, understanding the interaction between Neurexophilin 1 and neurexins can help in developing therapeutic strategies for synaptic dysfunction and related diseases .

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
© Copyright 2024 Thebiotek. All Rights Reserved.