CALN1 Human

Calnueron-1 Human Recombinant
Cat. No.
BT29002
Source
Escherichia Coli.
Synonyms
Calcium-binding protein 8, CaBP8, Calneuron I, Calneuron-1, CALN1, CABP8.
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.
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Description

CALN1 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 212 amino acids (1-192 a.a.) and having a molecular mass of 24kDa. The CALN1 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
CALN1, a protein with a close resemblance to calcium-binding proteins in the calmodulin family, possesses two EF-hand domains and potential calcium-binding sites. Notably, CALN1 exhibits regulatory effects on Golgi-to-plasma membrane trafficking through its interaction with PI4KB, inhibiting its activity. Functionally, CALN1 plays a role in neuronal physiology and holds potential implications in memory and learning processes.
Description
CALN1 Human Recombinant, incorporating a 20 amino acid His tag at the N-terminus and produced in E.Coli, is characterized as a single, non-glycosylated polypeptide chain. This chain comprises 212 amino acids (1-192 a.a.) and exhibits a molecular mass of 24kDa. The purification process of CALN1 involves the utilization of proprietary chromatographic techniques.
Physical Appearance
A clear and sterile solution.
Formulation
The CALN1 solution, provided at a concentration of 0.5 mg/ml, consists of 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT, 50mM NaCl, and 0.1mM PMSF.
Stability
For optimal storage, maintain the CALN1 solution at 4°C if the entire vial will be used within 2-4 weeks. For prolonged storage, it is recommended to store the solution in a frozen state at -20°C. To ensure long-term stability, consider adding a carrier protein (0.1% HSA or BSA). It is advisable to minimize the number of freeze-thaw cycles.
Purity
The purity of CALN1 is determined to be greater than 90.0% based on SDS-PAGE analysis.
Synonyms
Calcium-binding protein 8, CaBP8, Calneuron I, Calneuron-1, CALN1, CABP8.
Source
Escherichia Coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MPFHHVTAGL LYKGNYLNRS LSAGSDSEQL ANISVEELDE IREAFRVLDR DGNGFISKQE LGMAMRSLGY MPSEVELAII MQRLDMDGDG QVDFDEFMTI LGPKLVSSEG RDGFLGNTID SIFWQFDMQR ITLEELKHIL YHAFRDHLTM KDIENIIINE EESLNETSGN CQTEFEGVHS QKQNRQTCVR KS.

Product Science Overview

Structure and Expression

Calnueron-1 is a human fragment protein expressed in Escherichia coli and is typically purified to a high degree of over 90% purity . The recombinant form of this protein is often tagged with a His tag at the N-terminus to facilitate purification and detection . The protein sequence includes several key regions that are essential for its function, including calcium-binding domains that enable it to interact with other proteins and cellular structures .

Function and Role in Neurons

Calnueron-1 is primarily involved in the regulation of calcium signaling within neurons. It negatively regulates Golgi-to-plasma membrane trafficking by interacting with phosphatidylinositol 4-kinase beta (PI4KB) and inhibiting its activity . This regulation is crucial for maintaining proper cellular function and signaling pathways in neurons.

The protein is believed to play a significant role in memory and learning processes, making it an important target for research in neurobiology and cognitive sciences . Its ability to bind calcium ions and modulate various signaling pathways highlights its importance in neuronal physiology.

Applications in Research

Recombinant Calnueron-1 is widely used in research to study its function and role in cellular processes. It is suitable for various applications, including SDS-PAGE and mass spectrometry (MS), which are techniques used to analyze protein structure and function . Researchers utilize this protein to investigate its interactions with other proteins and its impact on cellular signaling pathways.

Potential Implications

Understanding the function and regulation of Calnueron-1 has significant implications for the study of neurological diseases and disorders. Given its role in memory and learning, alterations in Calnueron-1 expression or function could potentially be linked to conditions such as Alzheimer’s disease and other cognitive impairments . Further research into this protein could provide valuable insights into the mechanisms underlying these conditions and contribute to the development of therapeutic strategies.

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