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.
Datasheet :
Please contact us to get it.
產品評價
靶點詳情
功能:
Essential multidomain scaffolding protein required for normal development. Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells. Regulates the excitability of cardiac myocytes by modulating the functional expression of Kv4 channels. Functional regulator of Kv1.5 channel. May play a role in adherens junction assembly, signal transduction, cell proliferation, synaptogenesis and lymphocyte activation. During long-term depression in hippocampal neurons, it recruits ADAM10 to the plasma membrane.
基因功能參考文獻:
Results indicate that the GluA1 subunit accessory protein SAP97 may represent a novel target for pharmacotherapeutic intervention in the treatment of cocaine craving PMID: 26149358
dendrite branching promoting action of full length SAP97 depends on ligand(s) that bind to the PDZ3 domain. PMID: 25701814
The data establish a prominent role for PDZ2 and I3 domains of SAP97 in organizing the ss1-adrenergic receptosome involved in connecting the ss1-AR to trafficking and signaling networks. PMID: 23696820
Acute BDNF treatment upregulates the interactions between AMPA receptor subunits (GluR1 and GluR2) with their scaffold proteins SAP97 and GRIP1, respectively. PMID: 23460828
studies show that SAP97 interactions with CRFR1 attenuate CRFR1 endocytosis and that SAP97 is involved in coupling G protein-coupled receptors to the activation of the ERK1/2 signaling pathway. PMID: 23576434
Scribble/Lgl/Dlg polarity protein complex is a regulator of blood-testis barrier dynamics and spermatid polarity during spermatogenesis PMID: 23038739
Cx32 is differentially phosphorylated and exists in a complex with SAP97 and CaM. PMID: 22718765
Overexpression of SAP97 was associated with overexpression of PSD-95 and recruitment of nNOS to the synapse and was accompanied by marked morphological changes, with spines enwrapping and engulfing presynaptic terminals. PMID: 20865734
SAP97 isoforms can regulate the ability of synapses to undergo plasticity by controlling the surface distribution of AMPA and NMDA receptors. PMID: 21768261
investigation of structure of SAP97 isoforms: Data suggest conformation of SAP97 is determined by nature of N-terminus, which may, in turn, influence specific role of a particular splice variant. (signal sequence involved in mitochondrial targeting) PMID: 22242544
SAP97 and dystrophin macromolecular complexes determine two pools of cardiac sodium channels Nav1.5 in cardiomyocytes. PMID: 21164104
Upregulation of SAP97 coincides with the redistribution of aquaporin (AQP)4 and inwardly-rectifying potassium channel (Kir) 4.1 in blue light-injured rat retina. PMID: 20625331
In cardiac myocytes SAP97 regulates surface expression of channels underlying I(K1) PMID: 20530486
Following acute injection of phencyclidine SAP-97 transcripts are upregulated in the adult neocortex. PMID: 19836928
findings show that, in Schwann cells, Dlg1 interacts with PTEN to inhibit axonal stimulation of myelination; this mechanism limits myelin sheath thickness & prevents overmyelination in sciatic nerves PMID: 20448149
CaMKIIalpha targets a specific SAP97 splice variant to disengage AKAP79/150 from regulating GluR1 AMPARs PMID: 19858198
As monitored by circular dichroism and differential scanning calorimetry, SAP97 (T(m)=64 degrees C) is significantly more thermal stable than SAP90/PSD-95 (T(m)=52 degrees C) and follows a bimodal phase transition. PMID: 19632332
Binding to GluR-A AMPA receptor subunit is determined by a novel sequence motif PMID: 12070168
findings suggest that synapse associated protein 97/NR2A NMDA receptor interaction is regulated by calcium calmodulin dependent protein kinase II-dependent phosphorylation PMID: 12933808
a complex composed of SAP97, CASK, Veli, and Mint1 associates with Kir2 channels via the C-terminal PDZ-binding motif. SAP97, Veli-1, or Veli-3 binds directly to the Kir2.2 C terminus and recruits CASK PMID: 14960569
in T cells, Discs large (Dlg1) is recruited upon activation to cortical actin and forms complexes with early participants in T cell activation PMID: 15263016
data highlight the potential role of abnormalities in the subcellular distribution of Synapse-associated proteins PSD-95 and SAP97 in the pathophysiology of a neurological disease PMID: 15703272
a direct interaction between SAP97 and PSD-95 may play a functional role in the trafficking and clustering of AMPA receptors. PMID: 16332687
These results suggest that SAP97 may play a central role in the coordinated growth of synapses during development and plasticity by recruiting a complex of postsynaptic proteins that enhances presynaptic terminal growth. PMID: 16495462
Profound modifications of NR2B subunit association with synapse-associated protein-97 occurs in 6-OHDA, L-DOPA -treated dyskinesia. PMID: 16540568
Interaction between synthetic GluR-A C-terminal peptides and the PDZ2 domain of SAP97. Last 4 residues of GluR-A peptides bind to PDZ2 in a fashion typical of class I PDZ interactions. PMID: 16634638
These results demonstrate that the different N termini of the predominant endogenous forms of PSD-95 (alpha-isoform) and SAP97 (beta-isoform) govern their role in regulating synaptic function. PMID: 16815335
SAP97 was expressed postsynaptically at the climbing fibers synapse at early ages during Purkinje cell dendritic growth; its expression changed from neurons to Bergmann glia once these glial cells had completed their enwrapping process. PMID: 17335044
calcium/calmodulin-dependent protein kinase II (CaMKII)-dependent SAP97 phosphorylation regulates the subcellular localization of Kv4.2. PMID: 17635915
We speculate that restricted dynamics & preferential Kir2.1 binding to PDZ2 are features that enable SAP97 to function as a scaffold protein, allowing other proteins to bind to other 2 PDZ domains in sufficient proximity to yield productive channelosomes. PMID: 18004877
The distribution of SAP97 confirms that this protein is actually an integral component of the PSD, and suggests that it may have a role in inserting or stabilizing its main binding partner, Glu-R1, at the edge of the PSD. PMID: 18392731
SAP97 is a major partner for surface expression and CaMKII-dependent regulation of cardiac Kv4.2 and kv4.3 channels. PMID: 19213956
N-terminal splicing of SAP97 controls synaptic strength by regulating distribution of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors. PMID: 19357261
Our data demonstrate that the retention and trafficking of NMDARs in this endoplasmic reticulum subcompartment requires both CASK and SAP97. PMID: 19620977
SAP97 regulates Kir2.3 channels by multiple mechanisms. PMID: 19633205
Widely expressed. Strongly expressed in epithelial cells, in the small intestine it is only detected in the vili. Expressed in brain, heart (at protein level), muscle, lung and liver. In the brain it was detected in olfactory bulbs, cerebral cortex, hippo