|Validated Species:||Human, Mouse, Rat|
Data & Images
|Product Name||Anti-Kv2.1 Picoband™ Antibody|
|Description||Rabbit IgG polyclonal antibody for Potassium voltage-gated channel subfamily B member 1(KCNB1) detection. Tested with WB, IHC-P, IHC-F in Human;Mouse;Rat.|
|Cite This Product||Anti-Kv2.1 Picoband™ Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PB9111)|
|Replacement Item||This antibody may replace the following items: sc-22379 from Santa Cruz Biotechnology.|
|Validated Species||Human, Mouse, Rat|
*Our Boster Guarantee covers the use of this product in the above tested applications.
**For positive and negative control design, consult "Tissue specificity" under Protein Target Info.
|Recommended Detection Systems||Boster recommends Enhanced Chemiluminescent Kit with anti-Rabbit IgG (EK1002) for Western blot, and HRP Conjugated anti-Rabbit IgG Super Vision Assay Kit (SV0002-1) for IHC(P) and IHC(F).
*Blocking peptide can be purchased at $50. Contact us for more information
**Boster also offers various secondary antibodies for Immunoflourescecne and IHC. Take advantage of the buy 1 primary antibody get 1 secondary antibody for free promotion for the entire year 2017!
|Immunogen||E.coli-derived human Kv2.1 recombinant protein (Position: V687-I858). Human Kv2.1 shares 88% amino acid (aa) sequence identity with both mouse and rat Kv2.1.|
|Cross Reactivity||No cross reactivity with other proteins|
|Contents||Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3.
*carrier free antibody available upon request.
|Concentration||Add 0.2ml of distilled water will yield a concentration of 500ug/ml.|
|Storage||At -20°C for one year. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for a longer time.Avoid repeated freezing and thawing.|
|Purification||Immunogen affinity purified.|
Protein Target Info (Source: Uniprot.org)
You can check the tissue specificity below for information on selecting positive and negative control.
|Protein Name||Potassium voltage-gated channel subfamily B member 1|
|Molecular Weight||95878 MW|
|Protein Function||Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain, but also in the pancreas and cardiovascular system. Contributes to the regulation of the action potential (AP) repolarization, duration and frequency of repetitive AP firing in neurons, muscle cells and endocrine cells and plays a role in homeostatic attenuation of electrical excitability throughout the brain (PubMed:23161216). Plays also a role in the regulation of exocytosis independently of its electrical function (By similarity). Forms tetrameric potassium- selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Homotetrameric channels mediate a delayed-rectifier voltage-dependent outward potassium current that display rapid activation and slow inactivation in response to membrane depolarization (PubMed:8081723, PubMed:1283219, PubMed:10484328, PubMed:12560340, PubMed:19074135, PubMed:19717558, PubMed:24901643). Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNB2; channel properties depend on the type of alpha subunits that are part of the channel (By similarity). Can also form functional heterotetrameric channels with other alpha subunits that are non-conducting when expressed alone, such as KCNF1, KCNG1, KCNG3, KCNG4, KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and KCNV1, creating a functionally diverse range of channel complexes (PubMed:10484328, PubMed:11852086, PubMed:12060745, PubMed:19074135, PubMed:19717558, PubMed:24901643). Heterotetrameric channel activity formed with KCNS3 show increased current amplitude with the threshold for action potential activation shifted towards more negative values in hypoxic-treated pulmonary artery smooth muscle cells (By similarity). Channel properties are also modulated by cytoplasmic ancillary beta subunits such as AMIGO1, KCNE1, KCNE2 and KCNE3, slowing activation and inactivation rate of the delayed rectifier potassium channels (By similarity). In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Major contributor to the slowly inactivating delayed-rectifier voltage- gated potassium current in neurons of the central nervous system, sympathetic ganglion neurons, neuroendocrine cells, pancreatic beta cells, cardiomyocytes and smooth muscle cells. Mediates the major part of the somatodendritic delayed-rectifier potassium current in hippocampal and cortical pyramidal neurons and sympathetic superior cervical ganglion (CGC) neurons that acts to slow down periods of firing, especially during high frequency stimulation. Plays a role in the induction of long-term potentiation (LTP) of neuron excitability in the CA3 layer of the hippocampus (By similarity). Contributes to the regulation of glucose-induced action potential amplitude and duration in pancreatic beta cells, hence limiting calcium influx and insulin secretion (PubMed:23161216). Plays a role in the regulation of resting membrane potential and contraction in hypoxia-treated pulmonary artery smooth muscle cells. May contribute to the regulation of the duration of both the action potential of cardiomyocytes and the heart ventricular repolarization QT interval. Contributes to the pronounced pro-apoptotic potassium current surge during neuronal apoptotic cell death in response to oxidative injury. May confer neuroprotection in response to hypoxia/ischemic insults by suppressing pyramidal neurons hyperexcitability in hippocampal and cortical regions (By similarity). Promotes trafficking of KCNG3, KCNH1 and KCNH2 to the cell surface membrane, presumably by forming heterotetrameric channels with these subunits (PubMed:12060745). Plays a role in the calcium-dependent recruitment and release of fusion-competent vesicles from the soma of neurons, neuroendocrine and glucose- induced pancreatic beta cells by binding key components of the fusion machinery in a pore-independent manner (By similarity). .|
|Tissue Specificity||Expressed in neocortical pyramidal cells (PubMed:24477962). Expressed in pancreatic beta cells (at protein level) (PubMed:12403834, PubMed:14988243). Expressed in brain, heart, lung, liver, colon, kidney and adrenal gland (PubMed:19074135). Expressed in the cortex, amygdala, cerebellum, pons, thalamus, hypothalamus, hippocampus and substantia nigra (PubMed:19074135). .|
|Sequence Similarities||Belongs to the potassium channel family. B (Shab) (TC 1.A.1.2) subfamily. Kv2.1/KCNB1 sub-subfamily.|
|Subcellular Localization||Cell membrane . Perikaryon . Cell projection, axon . Cell projection, dendrite . Membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane . Cell junction, synapse . Cell junction, synapse, synaptosome . Lateral cell membrane . Cell membrane, sarcolemma . Localizes to high-density somatodendritic clusters and non-clustered sites on the surface of neocortical and hippocampal pyramidal neurons in a cortical actin cytoskeleton-dependent manner (PubMed:24477962). Localizes also to high-density clusters in the axon initial segment (AIS), at ankyrin-G-deficient sites, on the surface of neocortical and hippocampal pyramidal neurons (PubMed:24477962). KCNB1-containing AIS clusters localize either in close apposition to smooth endoplasmic reticulum cisternal organelles or with GABA-A receptor-containing synapses of hippocampal and cortical pyramidal neurons, respectively (PubMed:24477962). Localizes to high-density clusters on the cell surface of atrial and ventricular myocytes and at the lateral plasma membrane in epithelial cells. Localizes both to the axial and transverse tubules (T tubule) and sarcolemma in ventricular myocytes. Associated with lipid raft domains. In cortical neurons, apoptotic injuries induce de novo plasma membrane insertion in a SNARE-dependent manner causing an apoptotic potassium current surge. .|
|Alternative Names||Potassium voltage-gated channel subfamily B member 1 ;Delayed rectifier potassium channel 1 ;DRK1 ;h-DRK1 ;Voltage-gated potassium channel subunit Kv2.1 ;KCNB1 ;|
Background for Potassium voltage-gated channel subfamily B member 1
Dilution Ratios/Recommended Concentrations
At Boster we strive to provide the best Anti-Kv2.1 Picoband™ Antibody by testing all applications on non-spiked tissues and cell lines to ensure that the affinity of the antibody is enough to react to the endogenouse level of the target protein. Read more about our QC panel here.
|Recommended dilution ratios are listed below:|
Immunohistochemistry(Frozen Section), 0.5-1μg/ml, Mouse, Rat, -|
Immunohistochemistry(Paraffin-embedded Section), 0.5-1μg/ml, Human, Mouse, Rat, By Heat
Western blot, 0.1-0.5μg/ml, Human, Mouse, Rat
**Boster provides high sensitivity secondary antibody kits for Western blotting and IHC. For more info see Related Products below.
Anti-Kv2.1 Picoband™ Antibody Images
Click the images to enlarge.
All lanes: Anti KV2.1 (PB9111) at 0.5ug/ml
WB: Recombinant Human kv2.1 Protein 0.5ng
Predicted bind size: 47KD
Observed bind size: 47KD
All lanes: Anti KV2.1 (PB9111) at 0.5ug/ml
Lane 1: Rat Brain Tissue Lysate at 50ug
Lane 2: Mouse Brain Tissue Lysate at 50ug
Predicted bind size: 96KD
Observed bind size: 96KD
IHC(P): Human Lung Cancer Tissue
IHC(P): Rat Brain Tissue
IHC(P): Mouse Brain Tissue
IHC(F): Rat Brain Tissue
IHC(F): Mouse Brain Tissue
1. Post-translational modification:phosphorylation, methylation, glycosylation etc. These modifications prevent SDS molecules from binding to the target protein and thus make the band size appear larger than expected
2. Post-translational cleavage: this can cause smaller bands and or multiple bands
3. Alternative splicing: the same gene can have alternative splicing patterns generating different size proteins, all with reactivities to the antibody.
4. Amino Acid R chain charge: SDS binds to positive charges. The different size and charge of the Amino Acid side chains can affect the amount of SDS binding and thus affect the observed band size.
5. Multimers: Multimers are usually broken up in reducing conditions. However if the interactions between the multimers are strong, the band may appear higher.,