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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. Zusätzlich bieten wir Ihnen CYB561 Kits (32) und CYB561 Antikörper (20) und viele weitere Produktgruppen zu diesem Protein an.
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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 (zeige CYGB Proteine) 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.
dihydrolipoic acid (DHLA)-dependent reduction of these two Cyt (zeige CYGB Proteine)-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 (zeige AR Proteine) 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 (zeige DBH Proteine).
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 (zeige DNAJC5 Proteine) residues near the intravesicular heme center
a detailed characterization of cyt (zeige CYGB Proteine) b561 using electron paramagnetic resonance (EPR (zeige EREG Proteine)) 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 (zeige CYGB Proteine) b(561).
We demonstrate here that the optical spectra, EPR (zeige EREG Proteine) spectra and redox potentials of recombinant TCytb are similar to those of the well characterized bovine chromaffin granule Cyt (zeige CYGB Proteine)-b561.
B-type di-heme cytochrome with a major alpha-absorption peak at 561 nm and a minor peak at 555 nm.
, cytochrome b561 family, member A1
, ferric-chelate reductase 2
, cytochrome b561
, cytochrome B561