E. coli biotin ligase
(BirA) is highly specific in covalently attaching biotin to the 15
amino
acid AviTag peptide. This recombinant protein was biotinylated in
vivo
by AviTag-BirA technology, which method is BriA catalyzes amide
linkage
between the biotin and the specific lysine of the AviTag.
The tag type will
be
determined during production process. If you have specified tag
type, please tell us and we will develop the specified tag
preferentially.
產品提供形式:
Lyophilized
powder
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Note: We will
preferentially ship the format that we have in stock, however,
if you have any special requirement for the format, please
remark your requirement when placing the order, we will prepare
according to your demand.
復溶:
We recommend that this vial be briefly centrifuged
prior
to opening to bring the contents to the bottom. Please reconstitute
protein in deionized sterile water to a concentration of 0.1-1.0
mg/mL.We recommend to add 5-50% of glycerol (final concentration)
and
aliquot for long-term storage at -20℃/-80℃. Our default final
concentration of glycerol is 50%. Customers could use it as
reference.
儲存條件:
Store at -20°C/-80°C upon receipt, aliquoting is
necessary for
mutiple use. Avoid repeated freeze-thaw cycles.
保質期:
The shelf life is related to many factors, storage
state,
buffer ingredients, storage temperature and the stability of the
protein
itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C.
The
shelf life of lyophilized form is 12 months at -20°C/-80°C.
貨期:
Delivery time may
differ from different purchasing way or location, please kindly
consult your local distributors for specific delivery time.
Note: All of our
proteins are default shipped with normal blue ice packs, if you
request to ship with dry ice, please communicate with us in
advance
and extra fees will be charged.
注意事項:
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Cytochrome b5 is a membrane-bound hemoprotein functioning as an electron carrier for several membrane-bound oxygenases. It is also involved in several steps of the sterol biosynthesis pathway, particularly in the C-6 double bond introduction during the C-6 desaturation.
基因功能參考文獻:
Cygb has a nitric-oxide dioxygenase function and ascorbate and cytochrome b(5) have roles as reductants PMID: 20511233
Chemical shift-based constraints for solution structure determination of cytochrome b5 PMID: 11941499
The hydrophobic clusters contribute to the greater stability of rat outer mitochondrial membrane Cyb5 and are responsible for higher kinetic barriers of hemin release and hemin reorientation compared to bovine microsomal apocyt b5. PMID: 12269800
outer mitochondrial membrane cytochrome b5 and not microsomal membrane cytochrome b5 functions as an activator for androgenesis in rat Leydig cells. PMID: 12668680
b5 is integrated into the ER membrane via the loosely bound state, which is described, and the 3 amino acids, -Leu-Met-Tyr, are important for conversion of the loosely-bound state to the firmly-integrated state. PMID: 12761189
when rat endoplasmic reticulum cytochrome b5 was coexpressed with wild-type desaturase, both proteins interacted and Delta6-desaturase activity was significantly increased PMID: 14563830
The first mutation (D60R) of cytochrome b(5), stabilized the holoprotein in a probable manifestation of enhanced helical propensity or improved electrostatic interactions PMID: 15379561
simulations provided qualitative microscopic explanations of many of the differences in physical properties between outer mitochondrial membrane CYB5 isoform and microsomal CYB5 and two mutants in terms of localized changes in structure and flexibility PMID: 16807901
The data distinguished the four helical segments and provided insight into the existence of holo- and nonholo-like interactions in the cytochrome's heme binding site. PMID: 18398853
The effect of the His63-iron bond and proximity of heme plane on the population of helical conformation in H4 and H5 of cytochrome b5 was investigated. PMID: 18398854
The hydrophobic domain of cytochrome b5 participates not only in hemeprotein interaction, but also in electron transfer from cytochrome b5 to cytochrome P4503A4. PMID: 19817686