Myoglobin Recombinant Protein | MB recombinant protein

Myoglobin, Recombinant, Human

Cat. Num. AAA637837

• Gene Names: MB; PVALB
• Applications: ELISA
• Purity: > 95%
• Synonyms: Myoglobin; Recombinant; Human; MB recombinant protein

• Purity/Purification: > 95%
• Form/Format: Supplied as a liquid in 20mM Tris HCL, pH 8.0, 50% glycerol
• Concentration: 0.25mg/ml (varies by lot)

• Applicable Applications for MB recombinant protein: ELISA (EL/EIA)
• Application Notes: Suitable for use in ELISA., , Recommended Dilution:, Optimal dilutions to be determined by the researcher.
• Source: Recombinant human Myoglobin is expressed in E.coli with an amino-terminal hexahistidine tag.
• Preparation and Storage: May be stored at 4 degree C for short-term only. For long-term storage and to avoid repeated freezing and thawing, add sterile glycerol (40-50%), aliquot and store at -20 degree C. Aliquots are stable for at least 12 months at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Related Product Information for MB recombinant protein

Myoglobin is a cytoplasmic, single chain polypeptide of 153 amino acids. It contains a single heme group. Myoglobin is found in skeletal and carciac muscle. It is not in smooth muscle. it functions as an oxygen transporting pigment. Upon damage to the muscle cell due to infarction of a coronary artery, neurological trauma, infection of tumor processes, myoglobin escapes to the environment and can be found in plasma using sensitive assays. 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.

Product Categories/Family for MB recombinant protein

Molecular Biology; MB-Serum Proteins

NCBI and Uniprot Product Information

• NCBI GI #: 44955888
• NCBI GeneID: 4151
• NCBI Accession #: NP_976312.1
• NCBI GenBank Nucleotide #: NM_203378.1
• UniProt Accession #: P02144; Q52H51; Q5THY7
• Molecular Weight: 21.7kD
• NCBI Official Full Name: myoglobin
• NCBI Official Synonym Full Names: myoglobin
• NCBI Official Symbol: MB
• NCBI Official Synonym Symbols: PVALB
• NCBI Protein Information: myoglobin
• UniProt Protein Name: Myoglobin
• Protein Family: Myoglobin
• UniProt Gene Name: MB
• UniProt Entry Name: MYG_HUMAN

NCBI Description

This gene encodes a member of the globin superfamily and is expressed in skeletal and cardiac muscles. The encoded protein is a haemoprotein contributing to intracellular oxygen storage and transcellular facilitated diffusion of oxygen. At least three alternatively spliced transcript variants encoding the same protein have been reported. [provided by RefSeq, Jul 2008]

Uniprot Description

MB: Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. Belongs to the globin family.

Protein type: Carrier

Chromosomal Location of Human Ortholog: 22q13.1

Molecular Function: iron ion binding; heme binding; oxygen binding; oxygen transporter activity

Biological Process: slow-twitch skeletal muscle fiber contraction; response to hydrogen peroxide; oxygen transport; heart development; brown fat cell differentiation; response to hypoxia; response to hormone stimulus; enucleate erythrocyte differentiation