HEBP1 Human

Heme Binding Protein 1 Human Recombinant
Cat. No.
BT14733
Source
Escherichia Coli.
Synonyms
Heme-binding protein 1, p22HBP, HEBP1, HBP, HEBP.
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

HEBP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-189 a.a.) and having a molecular mass of 23.5kDa.
HEBP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Heme Binding Protein 1 (HEBP1) is an intracellular protein that binds to tetrapyrroles. It has a chemoattractant peptide of 21 amino acids at its N-terminus. This peptide is a natural ligand for formyl peptide receptor-like receptor 2 (FPRL2) and can stimulate calcium mobilization and chemotaxis in monocytes and dendritic cells.
Description
Recombinant HEBP1 Human is produced in E. coli. It is a single, non-glycosylated polypeptide chain containing 212 amino acids (amino acids 1-189) with a molecular mass of 23.5 kDa. The protein is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless, and sterile filtered solution.
Formulation
The HEBP1 protein solution has a concentration of 0.5 mg/ml and contains 20 mM Tris-HCl buffer (pH 8.0), 0.15 M NaCl, 30% glycerol, and 1 mM DTT.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For longer storage, it should be frozen at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
The purity is determined to be greater than 90% by SDS-PAGE analysis.
Synonyms
Heme-binding protein 1, p22HBP, HEBP1, HBP, HEBP.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMLGMIKN SLFGSVETWP WQVLSKGDKE EVAYEERACE GGKFATVEVT DKPVDEALRE AMPKVAKYAG GTNDKGIGMG MTVPISFAVF PNEDGSLQKK LKVWFRIPNQ FQSDPPAPSD KSVKIEEREG ITVYSMQFGG YAKEADYVAQ ATRLRAALEG TATYRGDIYF CTGYDPPMKP YGRRNEIWLL KT.

Product Science Overview

Introduction

Heme Binding Protein 1 (HEBP1) is a protein encoded by the HEBP1 gene in humans. It is involved in various biological processes, primarily related to heme binding and metabolism. HEBP1 is a member of the heme-binding protein family, which plays a crucial role in the regulation of heme and porphyrin metabolism .

Structure and Function

HEBP1 binds with high affinity to one molecule of heme or porphyrins. It can also bind metalloporphyrins, free porphyrins, and N-methylprotoporphyrin with similar affinities . The protein’s ability to bind heme and porphyrins suggests its role in the detoxification and transport of these potentially toxic compounds within the cell .

Biological Significance

Heme is an essential molecule that plays vital roles in various biological processes, including oxygen transport, electron transfer, and catalysis of biochemical reactions . HEBP1’s ability to bind heme and porphyrins indicates its importance in maintaining cellular heme homeostasis and preventing the accumulation of free heme, which can be toxic to cells .

Recombinant HEBP1

Recombinant HEBP1 is produced using recombinant DNA technology, which involves inserting the HEBP1 gene into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant protein is used in various research applications to study its structure, function, and interactions with other molecules .

Research Applications

Research on HEBP1 has provided insights into its role in heme metabolism and its potential implications in various diseases. For example, studies have shown that HEBP1 may be involved in the regulation of circadian rhythms, lipid and glucose metabolism, and diseases such as Fanconi Anemia . Additionally, the structural analysis of heme proteins, including HEBP1, has revealed important features of heme binding pockets and their implications for protein design and prediction .

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