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B-type di-heme cytochrome with a major alpha-absorption peak at 561 nm and a minor peak at 555 nm. Additionally we are shipping CYB561 Kits (25) and CYB561 Antibodies (19) and many more products for this protein.
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We demonstrate here that the optical spectra, EPR (show EREG Proteins) spectra and redox potentials of recombinant TCytb are similar to those of the well characterized bovine chromaffin granule Cyt (show CYGB Proteins)-b561.
dihydrolipoic acid (DHLA)-dependent reduction of these two Cyt (show CYGB Proteins)-b561 proteins
expression of Cytochrome b561, is androgen regulated in the context of CaP cells and its increased expression in castration recurrent prostate cancer reflects increased androgen receptor (show AR Proteins) signaling in tumor cells
Data show that four members of the b561 family of predicted ferric reductases: mouse cytochrome b561, human duodenal cytochrome b, and mouse stromal cell-derived receptor 2, have ferric reductase activity.
Cyb561 from chromaffin cell membranes has high and low potential hemes as demonstrated by electron paramagnetic resonance and circular dichroism.
The pH-induced alteration and the destruction of heme in cytochrome b561 under oxidative conditions may play a significant role in the amplification of oxidative stress in catecholaminergic neurons.
Purified cytochrome b561 reconstituted into an artificial phospholipid bilayer is capable of transferring electron equivalents across the membrane to support monooxygenase activity of soluble extravesicular dopamine beta-hydroxylase (show DBH Proteins).
Raman data indicate that the two heme b centers of CYB561 adopt a six-coordinated low-spin state, in both reduced and oxidized forms.
importance of the two well-conserved Cys (show DNAJC5 Proteins) residues near the intravesicular heme center
a detailed characterization of cyt (show CYGB Proteins) b561 using electron paramagnetic resonance (EPR (show EREG Proteins)) and optical spectroscopy on the wild-type and mutant forms of the cytochrome expressed in insect cells
These results indicate that His92 can be considered part of the b(H) heme center, and His110 part of the b(L) heme center, in adrenal cyt (show CYGB Proteins) b(561).
We studied hereditary control of HR with the twin pair design, at rest and during environmental (cold) stress. Single nucleotide polymorphism disruption of a microribonucleic acid (microRNA) recognition motif in the human CYB561 3'-UTR was identified .
structural features in the cyt (show CYGB Proteins) b(561) family are well conserved at both the sequence and the protein level
CYB561 is a senescene-associated gene in normal human oral keratinocytes.
B-type di-heme cytochrome with a major alpha-absorption peak at 561 nm and a minor peak at 555 nm.
, cytochrome b561
, cytochrome B561
, cytochrome b561 family, member A1
, ferric-chelate reductase 2