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:
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
results strongly suggest that HSP22 represses HCC progression, especially HCC cell migration, by the down-regulation of the PI3K/AKT signaling pathway. PMID: 28456666
Data indicated that the HSPB8 expression level was strongly positively correlated with MAPK signaling pathway and CREB pathway and worse prognosis. The methylation level of its DNA was negatively associated with its expression and positively associated with overall survival. These results suggest that HSPB8 could promote the proliferation and inhibit the apoptosis of GC cells by activating ERKCREB signaling. PMID: 29693129
HSPB2 competes with HSPB8 for binding to BAG3. In contrast, HSPB3 negatively regulates HSPB2 association with BAG3. PMID: 28181153
Silencing of HSPB8 markedly decreased the mitotic levels of BAG3 in HeLa cells, supporting its crucial role in BAG3 mitotic functions. The results support a role for the HSPB8-BAG3 chaperone complex in quality control of actin-based structure dynamics that are put under high tension, notably during cell cytokinesis. PMID: 28275944
HSPB8 is involved in regulating the cell cycle and cell migration in MCF-7 cells. PMID: 28060751
suggest that HSPB8 may act as an intracellular factor against hepatitis C virus replication and that DNAJC5B has the same function, with more relevant results for genotype 3 PMID: 29182667
It has been demonstrated that HSPB8-BAG3-HSP70 ensures the functionality of stress granules and restores proteostasis by targeting defective ribosomal products for degradation. PMID: 27570075
HSPB8 counteracts accumulation of aberrantly localized misfolded forms of TDP-43 and its 25 KDa fragment involved in most sporadic cases of Amyotrophic Lateral Sclerosis and of Fronto Lateral Temporal Dementia. PMID: 26961006
expands the understanding of disease mechanisms, tissue involvement, and phenotypic outcome of HSPB8 mutations PMID: 26718575
our findings suggest the existence of a so-far unrecognized quality control mechanism involving BAG3, HSPB8 and p62/SQSTM1 for accurate remodelling of actin-based mitotic structures that guide spindle orientation. PMID: 26496431
This study demonstreated that expression of HSPB8 was restricted to GFAP+ astrocytes in patient with multiple sclerosis. PMID: 26694816
Pangenomic profiling of velcade-sensitive and resistant cells showed that the small heat shock protein HSPB8 was overexpressed in multiple myeloma resistant cells. PMID: 25051369
HSP22 acts as a positive regulator in TGF-alpha-induced migration of ovarian cancer cells, subsequently directing ovarian cancer toward progression. PMID: 25731856
HSP22 plays an important role on gastric tumor aggressiveness and prognosis and may act as a promising target for prognostic prediction. PMID: 24804817
Mutant HSPB8 causes protein aggregates and a reduced mitochondrial membrane potential in dermal fibroblasts from distal hereditary motor neuropathy patients. PMID: 22595202
The expression of HspB8 inhibits the growth of genetically diverse melanoma cells that include caspase-1 activation outside of the realm of the inflammasome, mTORC1-dependent Beclin-1 upregulation and its cleavage by the activated caspase-1. PMID: 22898869
findings show that during heat shock recovery NF-kappaB activates selective removal of misfolded or aggregated proteins by controlling expression of BAG3 and HSPB8 and by modulating the level of the BAG3-HspB8 complex PMID: 22302993
we observed upregulation of HSPB8 and BAG3 selectively in astrocytes located within the degenerated areas of patients with protein aggregation diseases PMID: 21696420
We studied the HSPB1 and HSPB8 mutation occurrence in patients with distal hereditary motor neuropathy and those with the axonal form of Charcot-Marie-Tooth disease type 2 PMID: 22176143
present study demonstrates that HSPB8 is silenced by DNA methylation in hematopoietic malignant and normal cells PMID: 21914495
The results of this syudy suggested that defects in HspB8-mediated autophagy are likely to contribute to dHMNII pathology and their detection in peripheral blood mononuclear cells could be a useful, accessible biomarker for the disease. PMID: 21985219
HSPB8 may play an important role in the protection of cells under lethal heat shock treatment, and the K141N mutation can impair the protective effect. PMID: 21983727
phosphorylation of HspB8 by ERK1 might be important for regulation of interaction of HspB8 with different target proteins PMID: 21526341
Overexpression of HSPB1, as well as HSPB6, HSPB7 and HSPB8 independently protect against tachycardia remodeling by attenuation of the RhoA GTPase pathway at different levels. PMID: 21731611
The complexes formed by Bag3 and HspB8 might have variable stoichiometry and can participate in different processes including clearing of the cell from improperly folded proteins. PMID: 21767525
Drosophila HSP67Bc is the functional ortholog of human HSPB8 and Dm-HSP67Bc induces autophagy via the eIF2alpha pathway. PMID: 20858900
HspB8 increases misfolded SOD1 clearance via autophagy. PMID: 20570967
Data show that the interaction between HspB6 and Bag3 requires the same regions that are involved in the HspB8-Bag3 association. PMID: 19845507
The results confirm predictions that Hsp22 belongs to the family of intrinsically disordered proteins with certain parts of its molecule retaining folded structure and undergoing reversible thermal unfolding. PMID: 19783089
In two pedigrees with distal hereditary motor neuropathy type II linked to chromosome 12q24.3, we identified the same mutation (K141N) in small heat-shock 22-kDa protein 8 (encoded by HSPB8; also called HSP22). PMID: 15122253
Hsp22 is highly homologous to small heat shock proteins and effectively prevents aggregation of denatured protein both in vitro and in vivo. It is supposed that chaperone-like activity is of great importance for Hsp22 functioning PMID: 15541337
Reduced chaperone activity of mutated HspB8 is associated with neuromuscular disorders PMID: 15879436
The rate of HSP22 gene mutation in Chinese patients with Charcot-Marie-Tooth disease is as low as 0.87%(1/115). PMID: 16086267
Our results suggest that a variety of oligomers composed of different proportions of different sHSPs may form in cell types expressing multiple sHSPs. PMID: 16225851
HspB8 might play important role in regulating Abeta aggregation and, therefore, development of classic senile plaques in Alzheimer's disease and cerebral amyloid angiopathy in hereditary cerebral hemorrhage with amyloidosis of Dutch type. PMID: 16485107
Small heat shock protein B8 (HSP22) is a novel TLR4 agonist abundantly expressed in synovial tissue from patients with rheumatoid arthritis. PMID: 16709864
found aberrantly increased interactions of neuropathy-associated mutant HSP22 forms with themselves, with wild-type HSP22, and with the other sHSPs, alphaB-crystallin, and HSP27. PMID: 16935933
Aberrant DNA methylation silences the novel heat shock protein H11 in melanoma PMID: 17033167
HspB8 overload causes melanoma growth arrest and apoptosis through TAK1 activation PMID: 17173073
Displays chaperone activity, autokinase activity, and trigger or block apoptosis activity. Decrease may contribute to development of some neurologic diseases and others. (Review) PMID: 17304582
HSP22 seems to play an important role in the nervous system. PMID: 17722063
Effect of mutations in the beta5-beta7 loop on the structure and properties of human small heat shock protein HSP22 PMID: 17922839
These results suggested that the HspB8-Bag3 complex might stimulate the degradation of Htt43Q by macroautophagy. PMID: 18006506
HSPB8 is a candidate CDK-independent cyclin D1 target that can mediate its effects PMID: 18006821
HspB8 and Bag3: a new chaperone complex targeting misfolded proteins to macroautophagy. PMID: 18094623
Hsp22 induction represents a new aspect of the estrogenic response with potential significance for the biology of estrogen receptor-positive breast cancer cells. PMID: 18229450
Mutations in serine residues of HSP22 which are phosphorylated by cAMP-dependent protein kinase were accompanied by decrease of chaperone-like activity. PMID: 18298377
Activation of the bone morphogenetic protein receptors Alk3 and Bmpr2 by H11kinase/Hsp22 promotes cardiac cell growth and survival. PMID: 19246680
H11 kinase is a novel mediator of myocardial hypertrophy in vivo PMID: 12456486