Polyclonal Antibody to Myoglobin (MYO), derived from recombinant MYO (Met1~Gly154), is reactive with Sheep.
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Myoglobin is a single-chain globular protein of 153 amino acids, containing a heme prosthetic group in the center around which the remaining apoprotein folds. It has eight alpha helices and a hydrophobic core. It has a molecular weight of 16700 daltons, and is the primary oxygen-carrying pigment of muscle tissues. Unlike the blood-borne hemoglobin, to which it is structurally related, this protein does not exhibit cooperative binding of oxygen, since positive cooperativity is a property of multimeric/oligomeric proteins only. Instead, the binding of oxygen by myoglobin is unaffected by the oxygen pressure in the surrounding tissue. Myoglobin is often cited as having an 'instant binding tenacity' to oxygen given its hyperbolic oxygen dissociation curve.
Caution: For research use only. Not for use in clinical diagnostic procedures. Please properly store each component based on the instruction.
Type: Primary
Antigen: MYO
Clonality: Polyclonal
Clone:
Conjugation: Unconjugated
Epitope:
Host: Rabbit
Isotype: IgG
Reactivity: Sheep