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.
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中文名稱:
Recombinant Human Voltage-dependent L-type calcium channel subunit alpha-1D(CACNA1D) ,partial
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
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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(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.
Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1D gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, and by benzothiazepines.
基因功能參考文獻(xiàn):
Although both otoferlin and synaptotagmin bind membrane fusion SNARE proteins, only otoferlin interacts with the L-type calcium channel Cav1.3. PMID: 28696301
Study have showned a significant effect of the autism-associated mutation A760G on the gating of CaV1.3 such that channel activation is significantly left-shifted, Ca(2+)-dependent inactivation is decreased, and deactivation is slowed, resulting in excess Ca2+ entry. However, these effects are mitigated by an increase in voltage-dependent inactivation. Also, A760G mutation differentially affects CaV1.3 splice variants. PMID: 27255217
Data suggest that p.G403D mutation in CACNA1D causes persistent hyperinsulinaemic hypoglycaemia with heart defects (presenting as aortic valve insufficiency) and severe neuromuscular disease (presenting as hypotonia); this study involves DNA mutational analysis in one patient plus 2 unrelated patients. [CASE REPORT] PMID: 28318089
These results provide the evidence of a direct regulatory role of Snapin on Cav1.3 channels in atrial myocytes. PMID: 27915047
Study used structure modeling and MD simulations to predict omega-currents in CaV1.1 and CaV1.3 channel VSDs when one of the first three S4 gating charges harbors a disease-causing mutation. Using site-directed mutagenesis and electrophysiology, experimentally confirmed that the mutation of R3 charge to His in VSD III of CaV1.3 channels results in an omega-current at hyperpolarizing potentials. PMID: 28978442
CACNA1D mutations predominate in small zona glomerulosa (ZG)-like Aldosterone-producing Adenomas. PMID: 28584012
The CACNA1C-L762F mutation is associated with development of long QT syndrome through slower channel inactivation and increased sustained and window current. Timothy syndrome -associated mutations localize to specific areas of CACNA1C and are associated with a younger age at presentation, higher QTc, and 2:1 AV block than isolated LQTS-associated mutations. PMID: 27390944
Mutations in CACNA1D cause the excessive autonomous aldosterone secretion of Aldosterone-producing Adenomas. PMID: 28584016
While the relative contribution of Cav1.3 to intestinal Ca(2+) absorption and its value as a therapeutic target remain to be established, we postulate that Cav1.3 downregulation in IBD may contribute to the negative systemic Ca(2+) balance, to increased bone resorption, and to reduced bone mineral density in IBD patients. PMID: 27932504
E2 upregulated the expression of Cav1.3 for Ca2+ influx to promote the expression of p-ERK1/2 for cell proliferation in breast cancer cells PMID: 27572936
LRP1B, BRD2 and CACNA1D are new candidate genes in fetal metabolic programming of newborns exposed to maternal hyperglycemia. PMID: 26586120
CACNA1D might not be a risk gene for SCZ in Han Chinese population, which add to the current state of knowledge regarding the susceptibility of CACNA1D to schizophrenia. PMID: 26255836
patients with CACNA1D mutations displayed characteristics similar to wild-type aldosterone-producing adenomas PMID: 26606680
Studies indicate the function of L-type calcium channels Cav1.3 in chromaffin cells. PMID: 25966692
Studies indicate a role for L-type calcium channel Cav1.3 and Cav1.4 in cochlear inner hair cells (IHCs) and retinal photoreceptors (PRs). PMID: 25966695
Mutations in CACNA1D gene is associated with aldosterone-producing adenomas. PMID: 26285814
Study found that two de novo CACNA1D missense mutations affect evolutionary highly conserved regions in the channel's activation gate and disrupt normal channel activity by inducing a pronounced gain of channel function PMID: 25620733
Cav1.3 was overexpressed in atypical hyperplasia and endometrial carcinoma, and the estrogen-induced phosphorylation of downstream molecular ERK1/2 and CREB is the result of activation of the GPER pathway. PMID: 25805831
A meta-analysis of genome-wide association studies of blood pressure and hypertension in Chinese identified three new loci (CACNA1D, CYP21A2, and MED13L) and a newly discovered variant near SLC4A7. PMID: 25249183
ablation of Cav1.3 results in a decrease in the protein expression of myosin light chain 2, which interacts and increases the membrane localization of SK2 channels. PMID: 25538241
CACNA1D gene overexpression is associated with prostate cancer progression and might play an important role in Ca(2+) influx, AR activation, and cell growth in prostate cancer cells PMID: 24054868
RNA editing of CaV1.3 channels(CDI) acts to modulate CDI in ways that substantiate a recently emerging mechanism where apoCaM begins preassociated with the IQ domain and other channel elements. PMID: 24120865
in patients with aldosterone-producing adenomas, CACNA1D mutations were associated with smaller adenomas. PMID: 24866132
Results illustrate that the voltage sensors of Cav1.3 channels respond more sensitively to depolarization than those of Cav1.2 or Cav3.1 PMID: 24703308
The calcium inflow through Cav1.2 and Cav1.3 channels in murine spiral ganglion neurons. PMID: 24849370
These findings implicate gain-of-function CACNA1D Ca(2+) channel mutations in adrenal aldosterone-producing adenomas and primary aldosteronism. PMID: 23913001
A novel mechanism for modulation of the pharmacologic properties of the CaV1.3 channel is identified through posttranscriptional modification of the C terminus. PMID: 23924992
N-lobe of Ca(2+)-calmodulin binds an N-terminal spatial Ca(2+) transforming element module on the channel amino terminus, whereas the C-lobe binds an EF-hand region upstream of the IQ domain PMID: 23591884
modulation of Cav1.3 Ca channel by calreticulin may be involved in pathological settings such as autoimmune associated congenital heart block where Cav1.3 Ca channels are downregulated PMID: 23791743
conclude that the L-type calcium channel Cav1.3 is important in human glucose-induced insulin secretion, and common variants in CACNA1D might contribute to type 2 diabetes. PMID: 23229155
analysis of functional characterization of alternative splicing in the C terminus of L-type CaV1.3 channels PMID: 21998309
Functional properties of a newly identified C-terminal splice variant of Cav1.3 L-type Ca2+ channels PMID: 21998310
A novel pathway for ankyrin-B-dependent regulation of Cav1.3 channel membrane targeting and regulation is found in atrial myocytes. PMID: 21859974
CaV1.3 channels and intracellular calcium mediate osmotic stress-induced N-terminal c-Jun kinase activation and disruption of tight junctions in Caco-2 CELL MONOLAYERS. PMID: 21737448
We describe a human channelopathy (termed SANDD syndrome, sinoatrial node dysfunction and deafness) with a cardiac and auditory phenotype that closely resembles that of Cacna1d-/- mice. PMID: 21131953
These data suggest that RIM2beta contributes to the stabilization of Ca(v)1.3 gating kinetics in immature cochlear inner hair cells. PMID: 20363327
Ca(v)1.3 was the sole apical channel responsible for the PRL-stimulated transcellular calcium transport in intestine-like Caco-2 monolayer. PMID: 19885716
demonstrate (1) expression of the alpha1D Ca channel in human fetal heart, (2) inhibition of alpha1D I(Ca-L) by positive IgG, and (3) direct cross-reactivity of positive IgG with the alpha1D Ca channel protein PMID: 15939813
The modulation of alpha(1D) Ca(2+) channel by PKC was prevented by dialyzing cells with a 35-amino acid peptide mimicking the alpha(1D) NH(2)-terminal region comprising S81. PMID: 16973824
analysis of Ca2+-dependent gating of CaV1.3 L-type calcium channels by alternative splicing of a C-terminal regulatory domain PMID: 18482979
Direct interaction of otoferlin with syntaxin 1A, SNAP-25, and the L-type voltage-gated calcium channel Cav1.3. PMID: 19004828
Enhancement of calcium transport in Caco-2 monolayer through PKCzeta-dependent Cav1.3-mediated transcellular and rectifying paracellular pathways by prolactin. PMID: 19339512
Overexpression of the intracellular II-III loop domains of Cav1.2, and possibly Cav1.3, can dislodge the corresponding endogenous channels from the lipid raft regions of the membrane in rat insulinoma (INS-1) cells. PMID: 19351867
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相關(guān)疾病:
Sinoatrial node dysfunction and deafness (SANDD); Primary aldosteronism, seizures, and neurologic abnormalities (PASNA)
Expressed in pancreatic islets and in brain, where it has been seen in cerebral cortex, hippocampus, basal ganglia, habenula and thalamus. Expressed in the small cell lung carcinoma cell line SCC-9. No expression in skeletal muscle.