IHC image of CSB-PA004398LA01HU diluted at 1:100 and staining in paraffin-embedded human kidney tissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a biotinylated secondary antibody and visualized using an HRP conjugated SP system.
Immunofluorescence staining of SH-SY5Y cells with CSB-PA004398LA01HU at 1:50, counter-stained with DAPI. The cells were fixed in 4% formaldehyde, permeabilized using 0.2% Triton X-100 and blocked in 10% normal Goat Serum. The cells were then incubated with the antibody overnight at 4°C. The secondary antibody was Alexa Fluor 488-congugated AffiniPure Goat Anti-Rabbit IgG(H+L).
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用途:
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
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-1B gives rise to N-type calcium currents. N-type calcium channels belong to the 'high-voltage activated' (HVA) group and are specifically blocked by omega-conotoxin-GVIA (AC P01522) (AC P01522). They are however insensitive to dihydropyridines (DHP). Calcium channels containing alpha-1B subunit may play a role in directed migration of immature neurons.
基因功能參考文獻(xiàn):
Cav2.2 alpha1 subunit alone could form a complex with the AMPAR in heterologous cells. The cell-surface AMPAR was increased by co-expression of Cav2.2 alpha1 subunit. PMID: 29448101
CACNA1B protein expressions in tumorous tissues were correlated with NSCLC patients' clinical characteristics and overall survival. CACNA1B mRNA and protein expression levels were higher in NSCLC tumorous tissues than in nontumorous tissues. PMID: 28127114
These results do not support a causal association between the CACNA1B c.4166G>A; (p.R1389H) variant and M-D. PMID: 26157024
AP-1 binding motifs, present only in exon 37a, enhance intracellular trafficking of exon 37a-containing Ca(V)2.2 to the axons and plasma membrane of rat dorsal root ganglia neurons PMID: 26511252
CACNA1B mutation is linked to unique myoclonus-dystonia syndrome. PMID: 25296916
The first disease connection for Cav2.2 channels [review] PMID: 26218636
The interaction between LC1 and the N-type channel (CaV2.2 channel) was demonstrated. PMID: 24566975
with membrane-localized CaV beta subunits, CaV2.2 channels are subject to Gbetagamma-mediated voltage-dependent inhibition, whereas cytosol-localized beta subunits confer more effective PIP2-mediated voltage-independent regulation PMID: 25225550
Results show that GABA(B) receptors R1 and R2 must be activated for the modulation of N-type (Ca(v)2.2) calcium channels by analgesic alpha-conotoxins Vc1.1 and RgIA. PMID: 22613715
new mechanistic perspectives, and reveal unexpected variations in determinants, underlying inhibition of Ca(V)1.2/Ca(V)2.2 channels by distinct RGK GTPases. PMID: 22590648
Ca(2+) exits the channel through the Cav2.2. PMID: 22491326
polymorphisms and haplotypes in the human CACNA1B gene show significant differences between cerebral infarction and control patients PMID: 21166801
Results suggest that a 39 bp DNA element in the N-type voltage-gated calcium channel alpha1B gene might act as repressor in non-neuronal cells through specific interactions with DNA. PMID: 12018859
molecular dissection of calcium current mechanosensitivity- electrophysiology of N-type calcium channels PMID: 12414690
the C-terminal region of Ca(v)2.2 does not have a critical role in regulation of the calcium channel PMID: 14602720
Cav2.2 alpha2delta auxiliary subunit binds to omega-conotoxins PMID: 15166237
Activation of PKC resulted in its recruitment to and phosphorylation of Ca(V)2.2 channels, but PKC phosphorylation did not dissociate Ca(V)2.2 channel/syntaxin 1A complexes. PMID: 15607937
The Y388S mutation had no effect on current density and cell surface expression of Ca(V)2.2/alpha2delta-2/beta1b channels expressed in human embryonic kidney tsA-201 cells, when equivalent proportions of cDNA were used. PMID: 16627564
Our studies of the e37a/e37b splice site reveal a multifunctional domain in the C-terminus of Ca(V)2.2 that regulates the overall activity of N-type calcium channels in nociceptors. PMID: 16857708
The orientation of the Ca(v)beta subunit relative to the alpha(1)2.2 subunit is critical, and suggests additional points of contact between these subunits are required for Ca(v)beta to regulate channel activity. PMID: 18958281
Isoform Alpha-1b-1 and isoform Alpha-1b-2 are expressed in the central nervous system, but not in skeletal muscle or aorta. Expressed in the cerebral white matter, cortex, hippocampus, basal ganglia, and cerebellum.