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.
B cell antigen receptor Ig beta associated protein 1; BPM 90; BPM L; BPM-L; BPM90; BPML; IBAP 1 ; Imp 9; Importin 9; Novel centrosomal protein RanBPM; RAN binding protein 9; Ran binding protein centrosomal; Ran Binding Protein in the Microtubule organizing center; Ran binding protein M; Ran BP9; Ran-binding protein 9; Ran-binding protein M; RANB9_HUMAN; RanBP 7; RANBP 9; RanBP7; RanBP9; RanBPM
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.
May act as scaffolding protein, and as adapter protein to couple membrane receptors to intracellular signaling pathways (Probable). Acts as a mediator of cell spreading and actin cytoskeleton rearrangement. Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1. May be involved in signaling of ITGB2/LFA-1 and other integrins. Enhances HGF-MET signaling by recruiting Sos and activating the Ras pathway. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but not affect estrogen-induced transactivation. Stabilizes TP73 isoform Alpha, probably by inhibiting its ubiquitination, and increases its proapoptotic activity. Inhibits the kinase activity of DYRK1A and DYRK1B. Inhibits FMR1 binding to RNA.
基因功能參考文獻(xiàn):
review provides a complete guide on RanBPM interactors, the physiological role of RanBPM in cellular functions, and potential applications in disease therapeutics. PMID: 29723489
Ran binding protein 9(RanBPM) is a scaffolding protein with a modulatory function that regulates the activities of IFN-stimulated response elements. IFN-lambda1 affects the cellular distribution of RanBPM and stimulates the interaction between RanBPM and interferon, lambda receptor 1(IFN-lambdaR1). Therefore, RanBPM plays a novel role in the IFN-lambda-regulated signaling pathway. PMID: 28547582
High RANBPM expression is associated with cancer. PMID: 26919101
RanBP9/TSSC3 complex cooperatively suppress metastasis via downregulation of Src-dependent Akt pathway to expedite mitochondrial-associated anoikis. PMID: 28032865
Results show that increased expression of RanBPM associates with postponed disease progression and better prognosis suggesting that RanBPM plays an inhibitory role in regulating proliferation and invasion of lung cancer cells. PMID: 28739732
The 20-mer peptide (residues 228-247) of human DDX-4, an ATP-dependent RNA helicase known to regulate germ cell development, binds to a unique shallow binding surface on RanBPM formed by highly conserved loops on the surface of the beta-sheet with two aspartates on one end, a positive patch on the opposite end, and a tryptophan lining at the bottom of the surface. PMID: 27622290
RanBPM acts as a negative regulator of BLT2 and IL8, thus attenuating the invasiveness of aggressive breast cancer cells PMID: 28027932
RanBP9 absence hampers the molecular mechanisms leading to efficient repair of damaged DNA, resulting in enhanced sensitivity to genotoxic stress. PMID: 26943034
Loss of RanBPM expression may play an important role in gastric cancer tumor development and metastasis. Reduced RanBPM expression is also associated with chemoresistance of gastric cancer cells. PMID: 26977028
RanBP9 is positively expressed in bone tumor tissues and cell strains. PMID: 27049080
RanBPM was found to enhance Zta-dependent transcriptional activity via the inhibition of Zta sumoylation. PMID: 25900136
association analyses between RANBP9 variants and the risk of schizophrenia were conducted, however no significant association was identified. PMID: 25482375
RanBP9 relocates APP intracellular domain to Tip60-enriched nuclear speckles and prevented the formation of nuclear spots formation; results place RanBP9 as an important player in the multiple steps of AbetaPP signaling PMID: 25024339
these analyses reveal that RanBPM subcellular localization results from the combined effects of several elements that either confer direct transport through the nucleocytoplasmic transport machinery PMID: 25659156
RanBP9 transgene overexpression causes early synaptic deficits, impaired learning and accelerates amyloid plaque accumulation. PMID: 24254706
COPS5 is a novel RanBP9-binding protein that increases APP processing and Abeta generation by stabilizing RanBP9 protein levels PMID: 23926111
RanBPM acts as a negative regulator of BLT2 signaling to attenuate BLT2-mediated cell motility PMID: 23928309
RanBPM influences TRAF6 ubiquitination and the TRAF6-triggered NF-kappaB signaling pathway through RanBPM's interaction with TRAF6. These data suggest that RanBPM participates in gene transcription by binding to TRAF6. PMID: 21805090
Data indicate that RanBP9 simultaneously inhibits cell-adhesive processes and enhances Abeta generation by accelerating APP, LRP, and beta1-integrin endocytosis. PMID: 22223749
results indicate that RanBPM, potentially through interaction with citron kinase, plays a role in the progression of neocortical precursors through M-phase at the ventricular surface. PMID: 19790105
RanBPM co-localizes with p42IP4 and, together with p42(IP4), the SPRY domain of RanBPM could act as a modulator of synaptic plasticity. PMID: 18298663
data support the idea that RanBP9 and RanBP10 may function as signaling integrators and dictate the efficient regulation of D(1) receptor signaling by PKCdelta and PKCgamma PMID: 20395553
RanBPM may modulate TrkB-mediated downstream signaling and biological functions. PMID: 20403074
These results reveal a novel proapoptotic function for RanBPM in DNA damage-induced apoptosis through the regulation of factors involved in the mitochondrial apoptotic pathway. PMID: 19996306
RanBP9-N60, a processed form of RanBP9 virtually identical to the RanBP9-Delta1/N60 mutant, was strongly increased in Alzheimer disease brains compared with controls. PMID: 19729516
RanBPM is the enzymic substrate for USP11 and is deubiquitinated specifically PMID: 12084015
RANBPM has a role in the HGF-MET and Ras signal transduction pathways PMID: 12147692
overexpressed wildtype HIPK2 and a kinase defective mutant of HIPK2 directly interact with RanBPM in the nucleus of mammalian cells. PMID: 12220523
interacts with steroid receptors to selectively modify their activity PMID: 12361945
demonstrates that CDK11(p46) directly interacts with RanBPM in vitro and in human cells PMID: 14511641
RanBPM may constitute a molecular scaffold that contributes to coupling LFA-1 and other integrins with intracellular signaling pathways PMID: 14722085
Expression of RanBPM inhibited the ubiquitination of p73alpha, and thereby prolonged its half-life. PMID: 15558019
Results identify and characterise a novel interaction between RanBPM and the related receptor tyrosine kinases, Axl and Sky. PMID: 15964779
Coexpression of RANBP9 with constitutively active Raf kinase synergistically inhibited myogenic regulatory factor MyoD-directed muscle reporter gene transcription PMID: 16364241
CD39 associations with RanBPM have the potential to regulate NTPDase catalytic activity. This intermolecular interaction may have important implications for the regulation of extracellular nucleotide-mediated signalling. PMID: 16478441
RanBPM is a potent novel coactivator for thyroid hormone receptors PMID: 16595702
RanBPM, ARMC8alpha, ARMC8beta, Muskelin, p48EMLP, and p44CTLH form complexes in cells PMID: 17467196
Studies in this review indicate that RanBPM acts as a scaffolding protein and is important in regulating cellular function in both the immune system and the nervous system. PMID: 18040864
Results describe the enhancement of the transactivation activity of Epstein-Barr virus Rta protein by RanBPM. PMID: 18455188
These novel findings identify a role for muskelin-RanBP9 complex in pathways that integrate cell morphology regulation and nucleocytoplasmic communication. PMID: 18710924
These results suggest that RanBPM could be a key regulator of Ca(v)3.1 channel-mediated signaling pathways. PMID: 18801335
Overexpression of RanBP9 resulted in the enhancement of APP interactions with LRP and BACE1 and increased lipid raft association of APP. PMID: 19251705
Ubiquitously expressed, with highest levels in testes, placenta, heart, and muscle, and lowest levels in lung. Within the brain, expressed predominantly by neurons in the gray matter of cortex, the granular layer of cerebellum and the Purkinje cells.