HMOX1 Human

Heme Oxygenase 1 Human Recombinant
Cat. No.
BT20015
Source
Escherichia Coli.
Synonyms
HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek'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

HO-1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids (1-266) and having a molecular mass of 31.4 kDa. HO-1 is fused to an 8 amino acid His Tag at C-Terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Heme Oxygenase-1 (HMOX1) plays a crucial role in heme degradation, catalyzing the breakdown of heme into biliverdin, iron, and carbon monoxide. It exhibits high activity in the spleen, contributing to the breakdown of red blood cells. HMOX1 is involved in various physiological processes, including cardiovascular regulation, response to stress, and modulation of inflammatory responses. Its upregulation has been observed in conditions such as ulcerative colitis and atherosclerosis. HMOX1 demonstrates anti-inflammatory effects by reducing the secretion of pro-inflammatory cytokines like MCP-1, IL-6, TNF-alpha, and IL-10 in macrophages.
Description
This product consists of a recombinant human HMOX1 protein produced in E. coli. It is a single, non-glycosylated polypeptide chain comprising 274 amino acids (residues 1-266) with a molecular weight of 31.4 kDa. The protein includes an 8-amino acid His tag fused at the C-terminus to facilitate purification via chromatographic techniques.
Physical Appearance
A clear and colorless solution that has been sterilized by filtration.
Formulation
The HMOX1 protein is supplied at a concentration of 1 mg/ml in a solution buffered with 20mM Tris-HCl at pH 8. The formulation also contains 50mM NaCl, 0.1mM PMSF (a protease inhibitor), and 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to store the protein at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is advisable for long-term storage. Repeated freezing and thawing of the product should be avoided.
Purity
The purity of the HMOX1 protein is greater than 95%, as determined by SDS-PAGE analysis.
Synonyms
HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1.
Source
Escherichia Coli.
Amino Acid Sequence
MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALEQDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQLYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHHHHHH.

Product Science Overview

Introduction

Heme Oxygenase 1 (HO-1), also known as HMOX1, is a crucial enzyme in the human body that plays a significant role in heme catabolism. This enzyme is responsible for the degradation of heme into biliverdin, carbon monoxide, and ferrous iron . The recombinant form of HO-1 is produced using advanced biotechnological methods, allowing for its use in various research and therapeutic applications.

Structure and Function

HO-1 is a 31 kDa protein encoded by the HMOX1 gene. It is primarily found in the endoplasmic reticulum of cells and is induced by oxidative stress . The enzyme’s activity involves the cleavage of the heme molecule, which is a pro-oxidant, into biliverdin, a potent antioxidant. Biliverdin is subsequently converted to bilirubin by biliverdin reductase .

Biological Significance

HO-1 has several critical functions in the body:

  1. Antioxidant Defense: By degrading heme, HO-1 helps to reduce oxidative stress and protect cells from damage.
  2. Anti-inflammatory Effects: The by-products of heme degradation, such as carbon monoxide, have anti-inflammatory properties.
  3. Regulation of Iron Homeostasis: The release of ferrous iron during heme degradation is essential for maintaining iron balance in the body .
Clinical Implications

HO-1 has been implicated in various physiological and pathological processes:

  • Cardiovascular Health: HO-1 plays a role in regulating cardiovascular function and responding to stressors .
  • Hematopoiesis: It influences the self-renewal and differentiation of hematopoietic stem cells, which are crucial for blood cell production .
  • Immune Response: HO-1 modulates both innate and adaptive immune responses, making it a potential target for immunotherapy .
Recombinant HO-1

Recombinant HO-1 is produced using E. coli expression systems. The recombinant protein is typically tagged with a His-tag for purification purposes and is available in carrier-free formulations to avoid interference in experimental applications . This form of HO-1 is used extensively in research to study its functions and potential therapeutic applications.

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