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(chǎn)品提供形式:
Lyophilized powder
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(fù)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(chǔ)存條件:
Store at -20°C/-80°C upon receipt, aliquoting is
necessary for
mutiple use. Avoid repeated freeze-thaw cycles.
保質(zhì)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(xiàng):
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC1 and UBC7 E2 ligases, and transfers it to substrates promoting their degradation. Mediates the degradation of endoplasmic reticulum proteins (ERQC), also called ER-associated degradation (ERAD). Component of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). In ERAD-L, facilitates retrotranslocation of misfolded proteins from the ER lumen through the ER membrane in conjunction with DER1. Both proteins have lateral gates facing each other which form a channel through the ER membrane and which distort the membrane region between the lateral gates, making it much thinner than a normal phospholipid bilayer. Substrates insert into the membrane as a hairpin loop with one strand interacting with DER1 and the other with HRD1. ERAD-L substrates are ubiquitinated through HRD1 in conjunction with the E2 ubiquitin-conjugating enzymes UBC1 and UBC7-CUE1. Ubiquitinated substrates are then removed to the cytosol via the action of the CDC48-NPL4-UFD1 ATPase complex and targeted to the proteasome. ERAD-M substrates are processed by the same HRD1-HRD3 core complex, but only a subset of the other components is required for ERAD-M.
基因功能參考文獻(xiàn):
Hrd1 is required for ER to cytosol retrotranslocation of ricin A chain, independently of its ubiquitin ligase activity PMID: 20519439
Hrd1p dislocates ricin A chain to the cytosol from the ER lumen, in a manner independent of its E3 ubiquitin ligase activity. PMID: 20519439
Authors reconstituted retrotranslocation with purified S. cerevisiae proteins, using proteoliposomes containing the multi-spanning ubiquitin ligase Hrd1. Retrotranslocation of the luminal domain of a membrane-spanning substrate is triggered by autoubiquitination of Hrd1. PMID: 27321670
Cytosolic entry of Shiga-like toxin a chain from the yeast endoplasmic reticulum requires catalytically active Hrd1p. PMID: 22829918
Hrd1 therefore likely plays a general role in targeting proteins that persistently associate with and potentially obstruct the translocon. PMID: 22689655
Study shows that Hrd1p is the central membrane component in ERAD-L; its overexpression bypasses the need for the other components of the Hrd1p complex. PMID: 21074049
Data suggest that the Saccharomyces cerevisiae Hrd1 complex manages three distinct substrate classes. PMID: 20212318
Usa1p is required for optimal function and regulation of the Hrd1p endoplasmic reticulum-associated degradation ubiquitin ligase. PMID: 19940128
analysis of RING-E2 fidelity for Hrd1p, a membrane-anchored ubiquitin ligase PMID: 17035235
Systematic analysis of model substrates revealed that glycans mark structural determinants that are sensitive to the overall folding state of the molecule. PMID: 19458187