Recombinant Proteins

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Product List

Myo Human w/o H

Myoglobin (Heme free) Human Recombinant

Myoglobin heme free Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 11.67 kDa. The Myoglobin heme free contains N-terminal T7 tag and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14842
Source
Escherichia Coli.
Appearance
Sterile Filtered solution.

Myoglobin

Myoglobin Human

Human Myoglobin produced in Human Cardiac Tissues having a molecular mass of 17.5kDa.
Myoglobin is released from recently injured myocardial cells within a few hours of Infarction. Peak levels are reached more quickly than CK-MB or Troponin complex.
Shipped with Ice Packs
Cat. No.
BT14907
Source
Human Cardiac Tissues.
Appearance
Sterile Filtered red solution.

Myoglobin His Human

Myoglobin His Human Recombinant

MB produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids (1-154a.a.) and having a molecular mass of 19.3kDa.
MB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14955
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

Myoglobin Human

Myoglobin Human Recombinant

Myoglobin Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 17.67 kDa. The Myoglobin is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15015
Source
Escherichia Coli.
Appearance
Sterile Filtered brownish solution.

Introduction

Definition and Classification

Myoglobin (Mb) is an iron- and oxygen-binding protein found predominantly in the cardiac and skeletal muscle tissue of vertebrates . It belongs to the globin superfamily of proteins and is structurally similar to hemoglobin, the oxygen-carrying protein in red blood cells . Myoglobin consists of a single polypeptide chain with 153 amino acids and a heme group that binds oxygen .

Biological Properties

Key Biological Properties: Myoglobin has a high affinity for oxygen, which allows it to store and transport oxygen within muscle cells . It is a monomeric protein, meaning it consists of a single polypeptide chain .

Expression Patterns and Tissue Distribution: Myoglobin is primarily expressed in cardiac and skeletal muscle tissues . It is found in high concentrations in Type I (slow-twitch) muscle fibers, which are involved in endurance activities, and to a lesser extent in Type II (fast-twitch) muscle fibers . Myoglobin is also present in smooth muscle cells, although in lower concentrations .

Biological Functions

Primary Biological Functions: The main function of myoglobin is to store and facilitate the transport of oxygen within muscle cells . This is crucial during periods of intense muscle activity when the demand for oxygen is high .

Role in Immune Responses and Pathogen Recognition: While myoglobin’s primary role is related to oxygen transport, it also plays a role in modulating nitric oxide homeostasis within muscle cells, which can influence immune responses .

Modes of Action

Mechanisms with Other Molecules and Cells: Myoglobin binds oxygen on its heme group, which allows it to acquire oxygen from hemoglobin in the blood and transfer it to muscle tissues . This binding is facilitated by the high affinity of myoglobin for oxygen compared to hemoglobin .

Binding Partners and Downstream Signaling Cascades: Myoglobin interacts with various molecules, including nitric oxide and reactive oxygen species, which can influence cellular signaling pathways and muscle function .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: Myoglobin expression is regulated by several transcription factors, including MEF2, NFAT, and Sp1, which are activated by locomotor activity, intracellular calcium fluxes, and low oxygen tension . Post-translational modifications, such as phosphorylation, also play a role in regulating myoglobin activity .

Applications

Biomedical Research: Myoglobin is used as a model protein in structural biology due to its well-characterized structure . It has been instrumental in understanding protein folding and function.

Diagnostic Tools: Elevated levels of myoglobin in the blood can be used as a biomarker for muscle injury, including myocardial infarction (heart attack) .

Therapeutic Strategies: Research is ongoing to explore the potential of myoglobin as a therapeutic target for treating various cardiac and skeletal muscle disorders .

Role in the Life Cycle

Role Throughout the Life Cycle: Myoglobin plays a critical role in muscle function throughout the life cycle. During development, it supports the growth and differentiation of muscle cells . In adulthood, it helps maintain muscle oxygenation during physical activity . In aging and disease, changes in myoglobin expression and function can impact muscle health and contribute to conditions such as heart failure and muscle atrophy .

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