Biotin-Linked Polyclonal Antibody to Alpha-Hemoglobin Stabilizing Protein (aHSP), derived from recombinant aHSP (Met1~Ser102), is reactive with Human.
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High pressure induces an irreversible aggregation of the ferrous deoxy α-chains, whereas the AHSP/α-Hb complex shows reversible hexacoordination of the α-Hb without protein aggregation. Upon pressure release, the relaxation kinetics of the transition from the hexacoordinated to pentacoordinated form of α-Hb in the presence of AHSP exhibit a biphasic shape. High pressure did not induce dissociation of α-Hb from its chaperone, as evidenced by the ligand binding kinetics that show a unique rate for the AHSP/α-Hb complex. For both free α-Hb and the AHSP/α-Hb complex, the bimolecular rate constant of CO binding (kCOon) versus pressure exhibits a bell shape, attributed to the transition of the rate-determining step from the chemical barrier to the migration of CO within the protein matrix.
Caution: For research use only. Not for use in clinical diagnostic procedures. Please proper stored each component based on the instruction.
Type: Primary
Antigen: aHSP
Clonality: Polyclonal
Clone:
Conjugation: Biotin
Epitope:
Host: Rabbit
Isotype: IgG
Reactivity: Human