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:
Liquid or 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.
Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II). Binds specifically to double-stranded DNA and at low levels to DNA modified by the antitumor agent cisplatin. May potentiate cisplatin-induced cell death by blocking replication and repair of modified DNA. Also acts as a transcriptional coactivator for p63/TP63.
基因功能參考文獻:
Data revealed that SSRP1 is highly overexpressed in glioma tissues at both the mRNA and protein levels and correlated with tumor grade. Further analysis demonstrated that that SSRP1 regulates the proliferation and metastasis of glioma cells via the MAPK signaling pathway. PMID: 29048646
These data uncover a previously unknown role for SSRP1 in promoting the activation of the Wnt signaling pathway activity during cellular differentiation. PMID: 27146025
we propose that FACT is both a marker and a target of aggressive breast cancer cells, whose inhibition results in their death or conversion a less aggressive subtype PMID: 28423528
High FACT expression is associated with glioblastoma. PMID: 27370399
The association of LEDGF proteins with the FACT complex and give further support to a role of SSRP1 in HIV-1 infection. PMID: 27216501
Results show that SSRP1 upregulation contributed to hepatocellular carcinoma development and the tumor-suppressive miR-497 served as its negative regulator. PMID: 26755331
FACT chaperone stabilizes the soluble CENP-T/-W complex in the cell and promotes dynamics of exchange, enabling CENP-T/-W deposition at centromeres. PMID: 27284163
This discloses a novel property of FACT wherein it has a co-remodeling activity and strongly enhances the remodeling capacity of the chromatin remodelers. Altogether, our data suggest that FACT may acts in concert with RSC to facilitate excision of DNA lesions during the initial step of BER. PMID: 27467129
SSRP1/Ets-1/Pim-3 signalling is tightly associated with the proliferation, apoptosis, autophagy, invasion and clonogenicity of nasopharyngeal carcinoma cells, and blockage of this signalling facilitates chemosensitivity of the cells to docetaxel. PMID: 27525970
Our studies facilitate the understanding of SSRP1 and provide insights into the molecular mechanisms of interaction with DNA and histones of the FACT complex. PMID: 26687053
AID accesses the H2B N-terminal basic region exposed by partial unwrapping of the nucleosomal DNA, thereby triggering the invasion of FACT into the nucleosome PMID: 26966247
FACT is required for TOP1 binding to H3K4me3 at non-B DNA containing chromatin for the site-specific cleavage. PMID: 26842758
FACT, NF-kappaB, and cell-cycle progression are inhibited by quinacrine, which overcomes resistance to erlotinib in non-small cell lung cancer PMID: 25028470
EEF1A1, SSRP1, and XRCC6 are novel interacting partners of the mineralocorticoid receptor PMID: 25000480
A primary role for FACT in RNF20 recruitment chromatin remodeling for initiation of homologous recombination repair. PMID: 24357716
In the absence of FACT complex, SSRP1 and SPT16 mRNAs are unstable and inefficiently translated, making reactivation of FACT function unlikely in normal cells. PMID: 23839038
hFACT-H2A/H2B interactions play a key role in overcoming the nucleosomal barrier by Pol II and promoting nucleosome survival during transcription PMID: 23610384
The HSF1-RPA complex leads to preloading of RNA polymerase II and opens the chromatin structure by recruiting a histone chaperone, FACT PMID: 22940245
specific FACT subunits synchronize interactions with various target sites on individual nucleosomes to generate a high affinity binding event and promote reorganization. PMID: 21969370
DNA-PK and FACT both play roles in DNA repair. Therefore both are putative targets for therapeutic inhibition. PMID: 21679440
The histone chaperone FACT: structural insights and mechanisms for nucleosome reorganization. PMID: 21454601
Studies suggest that that even though FACT has rapid chromatin-binding activity, the binding pattern of FACT on chromatin changes after origin licensing, which may contribute to the establishment of its functional link to the DNA replication machinery. PMID: 21232560
results demonstrate that SSRP1 is crucial for microtubule growth and spindle assembly during mitosis. PMID: 19995907
SSRP1 stimulates p63 activity by associating with this activator at the promoter PMID: 12374749
CK2 regulates the DNA-binding ability of SSRP1 and that this regulation may be responsive to specific cell stresses. PMID: 15659405
These results demonstrate that SSRP1 degradation during apoptosis is a two-step process coupling caspase cleavage and ubiquitin-dependent proteolysis. PMID: 16498457
SSRP1 has Spt16-dependent and -independent roles in regulating gene transcription in human cells. PMID: 17209051
CENP-H-containing complex facilitates deposition of newly synthesized CENP-A into centromeric chromatin in cooperation with FACT and CHD1. PMID: 19625449
SSRP1 may play a role in the DNA damage response mediated by homologous recombination; SSRP1 physically interacts with a key recombination repair protein, Rad54 PMID: 19639603
These results indicate that SSRP1 is a novel cellular protein involved in LANA-dependent DNA replication. PMID: 19710137
occurrence of an unusual TG 3' splice site in intron 1 PMID: 17672918