Recombinant Human Calcium-Activated Potassium Channel Subunit Alpha-1 (KCNMA1) Protein (His-HPC4)

Name: Recombinant Human Calcium-Activated Potassium Channel Subunit Alpha-1 (KCNMA1) Protein (His-HPC4)
Brand: Beta LifeScience
SKU: BLC-05240P
Availability: InStock

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) KCNMA1.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Calcium-Activated Potassium Channel Subunit Alpha-1 (KCNMA1) Protein (His-HPC4) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q12791
Target Symbol	KCNMA1
Synonyms	subfamily M subunit alpha-1; BK channel; BKCA alpha; BKCA alpha subunit; BKTM; Calcium-activated potassium channel; Calcium-activated potassium channel subunit alpha-1; Drosophila slowpoke like; hSlo; K(VCA)alpha; KCa1.1; KCMA1_HUMAN; KCNMA; KCNMA1; Maxi K channel; Maxi Potassium channel alpha ; MaxiK; SAKCA; SLO alpha; SLO; Slo homolog; Slo-alpha; Slo1; Slowpoke homolog
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	C-6His-HPC4
Target Protein Sequence	VVCGHITLESVSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEGDDAICLAELKLGFIA
Expression Range	411-560aa
Protein Length	Partial
Mol. Weight	20.0 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Potassium channel activated by both membrane depolarization or increase in cytosolic Ca(2+) that mediates export of K(+). It is also activated by the concentration of cytosolic Mg(2+). Its activation dampens the excitatory events that elevate the cytosolic Ca(2+) concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Plays a key role in controlling excitability in a number of systems, such as regulation of the contraction of smooth muscle, the tuning of hair cells in the cochlea, regulation of transmitter release, and innate immunity. In smooth muscles, its activation by high level of Ca(2+), caused by ryanodine receptors in the sarcoplasmic reticulum, regulates the membrane potential. In cochlea cells, its number and kinetic properties partly determine the characteristic frequency of each hair cell and thereby helps to establish a tonotopic map. Kinetics of KCNMA1 channels are determined by alternative splicing, phosphorylation status and its combination with modulating beta subunits. Highly sensitive to both iberiotoxin (IbTx) and charybdotoxin (CTX).
Subcellular Location	Cell membrane; Multi-pass membrane protein.
Protein Families	Potassium channel family, Calcium-activated (TC 1.A.1.3) subfamily, KCa1.1/KCNMA1 sub-subfamily
Database References	HGNC: 6284 OMIM: 600150 KEGG: hsa:3778 UniGene: PMID: 29211342 KCNMA1 mutation causes epilepsy and changes voltage gating but not calcium sensitivity. PMID: 29330545 Data suggest that large-conductance calcium-activated potassium channels, alpha subunit (BK channel) mutations affect the Ca2 +-sensing more than the voltage- sensing mechanism. PMID: 28966112 An important role of BKCa in proliferation and migration of endometrial cancer HEC-1-B cells. PMID: 29477869 Study identified a novel tumor suppressive gene, KCNMA1, which is frequently inactivated in gastric cancer because of promoter methylation. KCNMA1 exerts a tumor suppressive function by regulating the PTK2 expression to activate the PI3K-AKT pathway. PMID: 28231797 High BKCA expression is associated with breast cancer. PMID: 26993604 Heme-independent activation of the CFTR channel and the Slo1 BKCa channel by carbon monoxide (CO) may represent two different modes of gating regulation of ion channels by CO. In the case of CFTR, Fe3+ is bound to the R-ICL3 interface.15,16 This interfacial Fe3+ site is formed by traditional coordination ligands such as H950 and H954 from ICL3 and C832 and D836 from the R domain.[Review] PMID: 28474046 High BK channel is associated with glioblastoma. PMID: 26893360 Oxidant signaling underlies PKGIalpha modulation of Ca2+ sparks and BKCa in myogenically active arterioles PMID: 27729549 These results provide further insights into the mechanism of modulation of the different N-terminal regions of the BKCa channel by beta-subunits. PMID: 28750098 Thiourea derivative, compound 326, stimulates the activity of large-conductance, calcium-activated potassium channels. PMID: 28075010 Implicating both KCa1.1 and KCa3.1 channels. PMID: 28028617 These results identify KCa1.1 channels as crucial regulators of skeletal myogenesis. PMID: 27763639 Results show that reduced miR-17 expression is correlated with increased expression of KCNMA1 in malignant pleural mesothelioma. Computational analysis identified KCNMA1 gene is a direct target of miR-17. PMID: 27245839 These findings provide significant new evidence that BKalphaDeltae2 can modulate cellular responses to physiological stimuli in human chondrocyte and contribute under pathophysiological conditions, such as osteoarthritis. PMID: 27758860 Our report defines a novel autosomal recessive KCNMA1-related epileptic phenotype that encompasses cerebellar atrophy without paroxysmal dyskinesia, and highlights the sensitivity of the developing brain to both increased and decreased activity of the KCNMA1-encoded channels PMID: 27567911 A directed proteomic approach discovered the novel interaction of BKCa with Tom22, a component of the mitochondrion outer membrane import system, and the adenine nucleotide translocator (ANT). PMID: 27592226 GSK3b may up-regulate BK channels, an effect disrupted by lithium or additional expression of AKT and possibly participating in the regulation of cell volume and excitability. PMID: 27537208 MiR-31 represses KCNMA1 expression. PMID: 26386726 By introducing lanthanide binding tags in the extracellular region of the alpha- or beta1-subunit, we determined (i) a basic extracellular map of the BK channel, (ii) beta1-subunit-induced rearrangements of the voltage sensor in alpha-subunits, and (iii) the relative position of the beta1-subunit within the alpha/beta1-subunit complex. PMID: 27217576 Suggest that BK channel modulation by auxiliary gamma subunits depends on intra- and/or juxta-membrane mechanisms. PMID: 26009545 Suberoylanilide hydroxamic acid enhanced the expression of malignant genes such as KCNMA1 in lung cancer cells remaining after treatment, creating a more drug-resistant state. PMID: 25796627 We conclude that arachidonic acid itself selectively activates the beta1-associated BKCa channel, destabilizing its closed state probably by interacting with the beta1-subunit, without modifying the channel voltage sensitivity PMID: 24375290 The present study revealed that 11,12-EET targets the TRPV4-TRPC1-KCa1.1 complex to induce smooth muscle cell hyperpolarization and vascular relaxation in human LIMAs. PMID: 25511389 DS-201 selectively targets the pore-forming alpha subunit of human BKCa channels, thus enhancing the channel activities and increasing the subunit expression and trafficking. PMID: 25345746 Bisphenol A activates BK alpha via an extracellular site and that Bisphenol A-sensitivity is increased by the beta1 subun PMID: 24476761 show that Slo1 is localized to the sperm flagellum and is inhibited by progesterone. Inhibition of hKSper by progesterone may depolarize the spermatozoon to open the calcium channel CatSper PMID: 24137539 our results strongly suggest that AT1R regulates BK channels through a close protein-protein interaction involving multiple BK regions and independent of G-protein activation. PMID: 25070892 hSlo1c associates with Cav-1 in human brain microvascular endothelial cells.A 57-amino acid (966-1022) fragment in hSlo1c was identified to be critical for hSlo1c/Cav-1 interaction. PMID: 24705869 Recombinant martentoxin selectively blocks KCNMA1/KCNMB4 channels. PMID: 24759175 HIV and methamphetamine -induced elevated miR-9 lead to suppression of miR-response element-containing splice variants of KCNMA1 PMID: 23508624 Overexpression of JAK2 in alveolar rhabdomyosarcoma cells significantly enhanced BK channel mRNA and protein abundance. PMID: 24696148 The reduced KCa1.1 channel protein expression was also observed. PMID: 24260325 Here we examined the action of docosahexaenoic acid on the Slo1 channel without any auxiliary subunit and sought to elucidate the biophysical mechanism and the molecular determinants of the DHA sensitivity. PMID: 24127525 N-terminal isoforms of the large-conductance Ca(2)-activated K channel are differentially modulated by the auxiliary beta1-subunit. PMID: 24569989 Overexpression of KCNMA1, the pore-forming subunit of BK, overcame the reduction of airway surface liquid volume induced by IFN-gamma. PMID: 24414257 The SLO1 gating ring is not required for voltage activation but is required for Ca2+ and Mg2+ activation. PMID: 24067659 A novel Cav3-KCa1.1 signaling complex has been identified where Cav3-mediated calcium entry enables KCa1.1 activation over a wide range of membrane potentials. PMID: 23626738 BK-IS1 (44-113) alpha subunit has been over-expressed using a bacterial system and purified in the presence of detergent micelles for multidimensional heteronuclear nuclear magnetic resonance (NMR) structural studies. PMID: 23831469 BK(Ca) as a crucial part of the signaling cascade of LH/hCG in Leydig cells. PMID: 23267835 These results strongly suggest that cav3 possesses direct interaction with KCa1.1, presumably at the same domain for cav1 binding. PMID: 23237801 whole-cell current, spontaneous transient outward current, and Ca(2+) sensitivity of BK(Ca) channels are reduced in human vascular smooth muscle cells. This may account for the dysfunction of artery relaxation in primary hypertension. PMID: 23232643 enhanced expression of KCNMA1 correlates with and contributes to high proliferation rate and malignancy of breast cancer. PMID: 22899999 Phosphodiesterase blockade causes relaxation of human urinary bladder smooth muscle by increasing transient K(Ca)1.1 channel current activity, hyperpolarizing cell membrane potential, and decreasing the global intracellular Ca(2+). PMID: 22896041 TM1 of the beta2-subunit physically binds to the transmembrane S1 domain of the alpha-subunit of BK potassium channels PMID: 22710124 The effects of protein kinase C on Slo surface expression might be indirect; when clustered on hair cell membranes, Slo contributes to increasing amounts of channel clusters on high-frequency responsiveness of hair-cell membranes. PMID: 22538239 Multiple cholesterol recognition/interaction amino acid consensus (CRAC) motifs in cytosolic C tail of Slo1 subunit determine cholesterol sensitivity of Ca2+- and voltage-gated K+ (BK) channels. PMID: 22474334 These studies identify for the first time a central role for beta-catenin in mediating Slo surface expression. PMID: 22194818 BK(Ca) channels are involved in the response of podocytes to chronic hypoxia via the upregulation of the beta4-subunit. PMID: 22446331 Cym04 reversibly left-shifts the Slo1 half-activation voltage. It interacts with the S6/RCK linker & mimics site-specific shortening of this passive spring, transmiting force from the cytosolic gating ring structure opening the channel's gate. PMID: 22331907

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.