Certificate of Analysis and Data Sheet

Source:
E.Coli

Catalog No.
PRO-374

Background:

Myoglobin is a cytoplasmic hemoprotein, expressed solely in cardiac myocytes and oxidative skeletal muscle fibers, that reversibly binds O(2) by its heme residue, a porphyrin ring:iron ion complex. Since the initial discovery of its structure over 40 years ago, wide-ranging work by many investigators has added importantly to our understanding of its function and regulation. Functionally, myoglobin is well accepted as an O(2)-storage protein in muscle, capable of releasing O(2) during periods of hypoxia or anoxia. Myoglobin is also thought to buffer intracellular O(2) concentration when muscle activity increases and to facilitate intracellular O(2) diffusion by providing a parallel path that augments simple diffusion of dissolved O(2). The use of gene targeting and other molecular biological techniques has revealed important new insights into the developmental and environmental regulation of myoglobin and provided additional functions for this hemoprotein such as scavenging nitric oxide and reactive O(2) species.

Description :

Recombinant Human Myoglobin heme free produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 11.67kDa. Recombinant Human Myo heme free contains N-terminal T7 tag and purified by proprietary chromatographic techniques.

Physical Appearance:

Sterile Filtered solution.

Formulation:

The sterile solution (1mg/ml) contains phosphate-buffered saline (pH 7.4) and 0.05% NaN3.

Stability:

Recombinant Myo heme free although stable at 15⁰C for 2 weeks, should be stored at 4⁰C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please avoid freeze-thaw cycles.

Purity:

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Anion-exchange FPLC.
(c) Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel.

Dimers and aggregates:

Less than 1% as determined by silver-stained SDS-PAGE gel analysis.

Endotoxin:

Less than 0.1 ng/ug (IEU/ug) of Recombinant Myoglobin.

Usage:

This material is offered by ProSpec-TechnoGene for research, laboratory or further evaluation purposes.

Latest Publications:

1. Picosecond structural dynamics of myoglobin following photodissociation of carbon monoxide as revealed by ultraviolet time-resolved resonance Raman spectroscopy.
Biochemistry 2005 Nov 15;44(45):14709-14
2. Do neuroglobin and myoglobin protect Toxoplasma gondii from nitrosative stress?
IUBMB Life 2005 Oct;57(10):689-91
3. SNP A79G in the second exon of the myoglobin gene in elite long distance runners.
Br J Sports Med 2005 Oct;39(10):781-2
4. The position 68(E11) side chain in myoglobin regulates ligand capture, bond formation with heme iron, and internal movement into t he xenon cavities.
J Biol Chem 2005 Nov 18;280(46):38740-55
5. Negative myoglobin staining in hemiplegic muscle of acute stroke patients predicts functional recovery.
Am J Phys Med Rehabil 2005 Sep;84(9):692-8; quiz 699-700, 718
6. Ligand migration pathway and protein dynamics in myoglobin: a time-resolved crystallographic study on L29W MbCO.
Proc Natl Acad Sci U S A 2005 Aug 16;102(33):11704-9