CABP7 Human

Calcium Binding Protein 7 Human Recombinant
Cat. No.
BT28811
Source
Escherichia Coli.
Synonyms

Calcium-binding protein 7, CaBP7, Calneuron II, Calneuron-2, CABP7, CALN2.

Appearance
Sterile filtered colorless solution.
Purity
Greater than 80.0% 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

CABP7 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 208 amino acids (1-188 a.a.) and having a molecular mass of 23.7kDa.
CABP7 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction

Calcium-binding protein 7 (CABP7), a protein with two EF-hand domains, plays a crucial role in regulating intracellular trafficking. It binds calcium ions and interacts with PI4KB, an enzyme involved in lipid signaling, ultimately inhibiting its activity. This inhibitory action negatively regulates the transport of molecules from the Golgi apparatus to the plasma membrane. The CaBP family, which includes CABP7, consists of small calcium-binding proteins with EF-hand domains and has emerged as crucial regulators of neuronal function in the mammalian central nervous system.

Description

Recombinantly produced in E. coli, CABP7 is a single, non-glycosylated polypeptide chain consisting of 208 amino acids (specifically, amino acids 1 to 188). This protein has a molecular weight of 23.7 kDa. For purification and detection purposes, it has been engineered with a 20 amino acid His-tag at its N-terminus and purified using proprietary chromatographic techniques.

Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
This solution contains 0.5 mg/ml of CABP7 protein in a phosphate-buffered saline solution (pH 7.4).
Stability

For short-term storage (up to 1 week), CABP7 Human Recombinant remains stable at 4°C. However, for long-term storage, it is recommended to store the protein below -18°C. Repeated freezing and thawing of the protein should be avoided to prevent degradation.

Purity
Analysis by SDS-PAGE has determined that the purity of this product is greater than 80.0%.
Synonyms

Calcium-binding protein 7, CaBP7, Calneuron II, Calneuron-2, CABP7, CALN2.

Source
Escherichia Coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MPFHPVTAAL MYRGIYTVPN LLSEQRPVDI PEDELEEIRE AFKVFDRDGN GFISKQELGT AMRSLGYMPN EVELEVIIQR LDMDGDGQVD FEEFVTLLGP KLSTSGIPEK FHGTDFDTVF WKCDMQKLTV DELKRLLYDT FCEHLSMKDI ENIIMTEEES HLGTAEECPV DVETCSNQQI RQTCVRKS.

Product Science Overview

Structure and Expression

CaBP7 contains two EF-hand domains, which are helix-loop-helix structural motifs capable of binding calcium ions. The protein is expressed in the human brain and is involved in neuronal functions. The recombinant form of CaBP7 is typically produced in Escherichia coli and purified using conventional chromatography techniques .

Biological Functions

CaBP7 is known to negatively regulate Golgi-to-plasma membrane trafficking by interacting with phosphatidylinositol 4-kinase beta (PI4KB) and inhibiting its activity . This regulation is essential for maintaining proper cellular function and signaling. The CaBP family, including CaBP7, has emerged as important regulators of multiple targets essential to normal neuronal function in the mammalian central nervous system .

Applications

Recombinant CaBP7 is used in various research applications, including SDS-PAGE and mass spectrometry (MS). It is often tagged with a His-tag at the N-terminus to facilitate purification and detection . The protein is available in different concentrations and purities, typically greater than 80%, making it suitable for a range of experimental setups .

Storage and Handling

For optimal stability, recombinant CaBP7 should be stored at 4°C for short-term use and at -20°C for long-term storage. It is important to avoid freeze-thaw cycles to maintain the protein’s integrity .

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