Recombinant Human Atp-Sensitive Inward Rectifier Potassium Channel 10 (KCNJ10) Protein (His-SUMO)

Name: Recombinant Human Atp-Sensitive Inward Rectifier Potassium Channel 10 (KCNJ10) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-10211P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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) KCNJ10.

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 Atp-Sensitive Inward Rectifier Potassium Channel 10 (KCNJ10) Protein (His-SUMO) is produced by our E.coli expression system. This is a cytoplasmic protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P78508
Target Symbol	KCNJ10
Synonyms	KCNJ10; ATP-sensitive inward rectifier potassium channel 10; ATP-dependent inwardly rectifying potassium channel Kir4.1; Inward rectifier K(+ channel Kir1.2; Potassium channel, inwardly rectifying subfamily J member 10
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	FLAKIARPKKRAETIRFSQHAVVASHNGKPCLMIRVANMRKSLLIGCQVTGKLLQTHQTKEGENIRLNQVNVTFQVDTASDSPFLILPLTFYHVVDETSPLKDLPLRSGEGDFELVLILSGTVESTSATCQVRTSYLPEEILWGYEFTPAISLSASGKYIADFSLFDQVVKVASPSGLRDSTVRYGDPEKLKLEESLREQAEKEGSALSVRISNV
Expression Range	165-379aa
Protein Length	Cytoplasmic Domain
Mol. Weight	39.8kDa
Research Area	Transport
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	May be responsible for potassium buffering action of glial cells in the brain. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium. In the kidney, together with KCNJ16, mediates basolateral K(+) recycling in distal tubules; this process is critical for Na(+) reabsorption at the tubules.
Subcellular Location	Membrane; Multi-pass membrane protein. Basolateral cell membrane.
Protein Families	Inward rectifier-type potassium channel (TC 1.A.2.1) family, KCNJ10 subfamily
Database References	HGNC: 6256 OMIM: 602208 KEGG: hsa:3766 STRING: 9606.ENSP00000357068 UniGene: PMID: 29446379 A novel mutation in the KCNJ10 and previously characterized mutation in KCNT1 were identified in boy with seizures and neurodevelopmental delay. KCNJ10 L218F mutation associated with disease resulted in reduced Kir current. PMID: 28747464 rs17375748, rs1130183, rs12133079 and rs1186688 associated with sudden infant death syndrome PMID: 28520217 kcnj10 plays a role in K(+) recycling across the basolateral membrane in corresponding nephron segments and in generating negative membrane potential--{REVIEW} PMID: 27122539 Previous research had shown that Kir4.1 protein autoantibodies were specific for multiple sclerosis but they found that they weren't. PMID: 27074083 This study identifies potential SNPs of KCNJ10 gene that may contribute to seizure susceptibility and anti-epileptic drug resistance. PMID: 25874548 disruption of cav-1 decreases basolateral K(+) channel activity and depolarizes the cell membrane potential in the DCT1 at least in part by suppressing the stimulatory effect of c-Src on Kcnj10 PMID: 25848073 anti-KIR4.1 antibody levels differed in multiple sclerosis patients during relapse and remission; as such, they may represent a marker of disease exacerbation PMID: 25392324 This study showed that rs2486253, but not rs61822012, polymorphism of KCNJ10 gene was associated with childhood idiopathic generalized epilepsy. PMID: 25008907 we confirmed the presence of anti-Kir4.1 antibodies in multiple sclerosis patients, but at a much lower prevalence than previously reported. PMID: 24756568 KCNJ10 SNP is not associated with nonsyndromic enlargement of vestibular aqueduct in Chinese patients. PMID: 25372295 No KIR4.1-specific antigen is detected in serum or cerebrospinal fluid of multiple sclerosis (MS) patients; the target antigen of MS remains elusive. PMID: 25008548 This study observed a decrease of astroglial KIR4.1 but not glial fibrillary acidic protein IR. In chronic inactive and remyelinating MS lesions, KIR4.1 IR was restored on astrocytes and found in a subset of presumably new myelinating oligodendrocytes. PMID: 24777949 study provides an explanation for the pathophysiology of the p.A167V KCNJ10 mutation, which had not been considered pathogenic on its own; findings provide evidence for functional cooperation of KCNJ10 and KCNJ16; in vitro ascertainment of KCNJ10 function may necessitate co-expression with KCNJ16 PMID: 24193250 Mislocalization of the Kir4.1 channels contributes to renal salt wasting. PMID: 24561201 KCNJ10rs1130183 did not contribute to risk of seizure susceptibility. PMID: 24378235 Study confirms that EAST syndrome can be caused by many different mutations in KCNJ10 that significantly reduce K+ conductance. PMID: 21849804 Ordered disorder of the astrocytic dystrophin-associated protein complex in the norm and pathology. PMID: 24014171 Serum antibodies to KIR4.1 are found in the majority of children with acquired demylinating disease but not in children with other diseases or in healthy controls. PMID: 24415573 the modulation of tyrosine phosphorylation of KCNJ10 should play a role in regulating membrane transport function in DCT1. PMID: 23873931 We found no evidence for a significant association between mutations of KCNJ10 and FOXI1 with SLC26A4 in Pendred syndrome/enlarged vestibular aqueducts. PMID: 23965030 The results of this study indicated that alterations in expression of Kir4.1 occurring in epilepsy-associated lesions are possibly influenced by the local inflammatory environment and in particular by the inflammatory cytokine IL-1beta. PMID: 23270518 Oligodendrocyte precursor cells establish themselves progressively through postnatal upregulation of Kir4.1 potassium channels. PMID: 23392672 The subcellular co-localisation of K(ir)4.1 and AQP4 in the supporting cells of the cochlea described in this study resembles that of the astroglia of the central nervous system and the glial Mueller cells in the retina. PMID: 22802001 This study demonistrated that Loss of perivascular Kir4.1 potassium channels in the sclerotic hippocampus of patients with mesial temporal lobe epilepsy. PMID: 22878665 No KCNJ10 mutations were present in bilateral deafness patients with inner ear malformation. PMID: 22412181 Downregulation of Kir4.1 channels aggravates the visual impairment caused by the initial photoreceptor degeneration. PMID: 22055109 Gain-of-function defects in Kir4.1 causes dysfunction in astrocytic-dependent potassium buffering and contributes to autism/epilepsy phenotype by altering neuronal excitability and synaptic function. PMID: 21458570 extracellular volume recordings indicate that compromised K(+) spatial buffering in brain underlies the epilepsy phenotype associated with human KCNJ10 mutations PMID: 21748805 Role of KCNJ10 function in the physiology of proximal and possibly also the distal retina. Impact of KCNJ10 mutations on the electroretinogram in four unrelated patients with EAST syndrome. PMID: 21300747 Mutations in the K+ channel gene KCNJ10 (Kir4.1) cause the autosomal recessive EAST syndrome which is characterized by epilepsy, ataxia, sensorineural deafness, and a salt-wasting tubulopathy. PMID: 21221631 This study suggests that the SNPs within the kcnj10 genes we examined do not play a major role in schizophrenia in the Han Chinese population. PMID: 20933057 CaR decreases cell surface expression of Kir4.1 channels via a mechanism that involves Galpha(q) and caveolin. PMID: 21084311 Perturbed pH gating may underlie the loss of channel function for the disease-associated mutant Kir4.1 channels and may have important physiologic consequences. [review] PMID: 21088294 The Kir4.1 channel transgene plays a role in setting the membrane potential of glial cells and in maintaining potassium permeability in glial-conditioned Kir4.1 knock-out mice. PMID: 21106816 SLC26A4, FOXI1 and KCNJ10 are not major determinants in unilateral deafness and enlarged vestibular aqueduct PMID: 20621367 When expressed in CHO and HEK293 cells, the KCNJ10 mutations R65P, G77R, and R175Q caused a marked impairment of channel function PMID: 20651251 Variations in the AQP4 and the KCNJ10/KCNJ9 region are likely to be associated with temporal lobe epilepsy. PMID: 19864112 molecular analysis on chromosome 1q as a candidate gene for Type 2 diabetes in Pima Indians PMID: 12401729 Arg271Cys missense variation in KCNJ10 (or a nearby variation) is related to general seizure susceptibility in humans. PMID: 15120748 Our results support previous evidence that the common KCNJ10 Arg271Cys missense variation influences seizure susceptibility of common IGE syndromes. PMID: 15725393 Calcium-sensing receptor interacts directly with Kir4.1 and Kir4.2 and can decrease their currents. PMID: 17122384 The results showed that the expression of Kir 4.1 mRNA and protein, as well as the Kir 4.1 immunoreactivity score (IRS), increased markedly with increasing pathologic grade. PMID: 18191638 identifY previously unidentified KCNJ10 missense or nonsense mutations on both alleles in all subjects affected by a unique human syndrome, and establish the essential role of basolateral K(+) channels in renal electrolyte homeostasis. PMID: 19289823 Mutations in KCNJ10 cause a specific disorder. Our findings indicate that KCNJ10 plays a major role in renal salt handling and possibly also in blood-pressure maintenance and its regulation. PMID: 19420365 mutations in the inwardly rectifying K(+) channel gene KCNJ10 are associated with nonsyndromic hearing loss in carriers of SLC26A4 mutations with an EVA/PS phenotype. PMID: 19426954

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.