Recombinant Human Potassium Voltage-Gated Channel Subfamily D Member 2 (KCND2) Protein (His)

Beta LifeScience SKU/CAT #: BLC-10293P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Potassium Voltage-Gated Channel Subfamily D Member 2 (KCND2) Protein (His)

Beta LifeScience SKU/CAT #: BLC-10293P
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.

Product Overview

Description Recombinant Human Potassium Voltage-Gated Channel Subfamily D Member 2 (KCND2) Protein (His) is produced by our Yeast expression system. This is a cytoplasmic protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb Q9NZV8
Target Symbol KCND2
Synonyms KCD2; KCND 2; KCND2; KCND2_HUMAN; KIAA1044; MGC119702; MGC119703; Potassium voltage gated channel Shal related subfamily member 2; Potassium voltage-gated channel subfamily D member 2; RK 5; RK5; Voltage gated potassium channel Kv4.2; Voltage gated potassium channel subunit Kv4.2; Voltage sensitive potassium channel; Voltage-gated potassium channel subunit Kv4.2
Species Homo sapiens (Human)
Expression System Yeast
Tag N-6His
Target Protein Sequence VSNFSRIYHQNQRADKRRAQKKARLARIRAAKSGSANAYMQSKRNGLLSNQLQSSEDEQAFVSKSGSSFETQHHHLLHCLEKTTNHEFVDEQVFEESCMEVATVNRPSSHSPSLSSQQGVTSTCCSRRHKKTFRIPNANVSGSHQGSIQELSTIQIRCVERTPLSNSRSSLNAKMEECVKLNCEQPYVTTAIISIPTPPVTTPEGDDRPESPEYSGGNIVRVSAL
Expression Range 406-630aa
Protein Length Cytoplasmic Domain
Mol. Weight 27.0kDa
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 Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain. Mediates the major part of the dendritic A-type current I(SA) in brain neurons. This current is activated at membrane potentials that are below the threshold for action potentials. It regulates neuronal excitability, prolongs the latency before the first spike in a series of action potentials, regulates the frequency of repetitive action potential firing, shortens the duration of action potentials and regulates the back-propagation of action potentials from the neuronal cell body to the dendrites. Contributes to the regulation of the circadian rhythm of action potential firing in suprachiasmatic nucleus neurons, which regulates the circadian rhythm of locomotor activity. Functions downstream of the metabotropic glutamate receptor GRM5 and plays a role in neuronal excitability and in nociception mediated by activation of GRM5. Mediates the transient outward current I(to) in rodent heart left ventricle apex cells, but not in human heart, where this current is mediated by another family member. 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. Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCND2 and KCND3; channel properties depend on the type of pore-forming alpha subunits that are part of the channel. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes. Interaction with specific isoforms of the regulatory subunits KCNIP1, KCNIP2, KCNIP3 or KCNIP4 strongly increases expression at the cell surface and thereby increases channel activity; it modulates the kinetics of channel activation and inactivation, shifts the threshold for channel activation to more negative voltage values, shifts the threshold for inactivation to less negative voltages and accelerates recovery after inactivation. Likewise, interaction with DPP6 or DPP10 promotes expression at the cell membrane and regulates both channel characteristics and activity.
Subcellular Location Cell membrane; Multi-pass membrane protein. Cell projection, dendrite. Cell junction, synapse. Perikaryon. Cell junction, synapse, postsynaptic cell membrane. Cell projection, dendritic spine. Cell junction.
Protein Families Potassium channel family, D (Shal) (TC 1.A.1.2) subfamily, Kv4.2/KCND2 sub-subfamily
Database References
Associated Diseases KNCD2 mutations have been found in a family with autism and epilepsy and may play a role in disease pathogenesis. Autism is a complex multifactorial, pervasive developmental disorder characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age. Epilepsy is characterized by paroxysmal transient disturbances of the electrical activity of the brain that may be manifested as episodic impairment or loss of consciousness, abnormal motor phenomena, psychic or sensory disturbances, or perturbation of the autonomic nervous system.
Tissue Specificity Detected in ovary, in corpus luteum and in granulosa and theca cells in the follicle (at protein level). Highly expressed throughout the brain. Detected in amygdala, caudate nucleus, cerebellum, hippocampus, substantia nigra and thalamus. Expression is no

Gene Functions References

  1. A mutation, V404M, in the Kv4.2 channel subunit is associated with infant-onset epilepsy and autism. V404M enhances inactivation of channels that have not opened but dramatically impairs inactivation after opening. Authors show that increased side-chain volume is largely responsible for these seemingly paradoxical effects. PMID: 29581270
  2. Our results do not support the notion that accessory KChIP2 binding is a prerequisite for dendritic trafficking and functional surface expression of Kv4.2 channels, however, accessory KChIP2 binding may play a potential role in Kv4.2 modulation during intrinsic plasticity processes. PMID: 29385176
  3. Ca(2+)/calcineurin (CaN)/nuclear factor of activated T-cells (NFAT) c4 axis is required for neuritin-induced Kv4.2 transcriptional expression and potentiation of IA densities in cerebellum granule neurons. PMID: 27307045
  4. closed-state inactivation in Kv4.2 channels is a multistep process PMID: 26745419
  5. The study provides the first piece of evidence for the role of H2S in regulating Ito potassium channels and also the specific motif in an ion channel labile for H2S regulation. PMID: 25756524
  6. The stoichiometry of the Kv4.2-DPP10 complex was variable depending on the relative expression level of each subunit, with a preference for 4:2 stoichiometry PMID: 26209633
  7. The findings of this study suggest that variations in KCND2 genes are associated with both mild and severe persistent breast pain after breast cancer surgery. PMID: 25599232
  8. A rare genetic mutation of the KCND2 gene, p.D612N, was identified in a single patient. Co-expression of mutant and wild-type KCND2 with KChIP2 demonstrated a gain-of-function phenotype. PMID: 25214526
  9. study identified a de novo variant p.Val404Met in KCND2 in a family with identical twins affected with autism and severe seizures; findings suggest KCND2 is the causal gene for epilepsy in this family and has a role in the etiology of autism PMID: 24501278
  10. Subunit counting by single-molecule imaging revealed that the bound number of KChIP4 in each Kv4.2.KChIP4 complex was dependent on the expression level of KChIP4. PMID: 24811166
  11. reflected in the immunoblotting data KV4.2 receptors were detected at higher levels of expression in patient with cortical dysplasia with intractable epilepsy. PMID: 25003238
  12. KCND2 is expressed in human skin, but has not been associated with aging. PMID: 24037343
  13. WT PrP(C), in a DPP6-dependent manner, modulated Kv4.2 channel properties, causing an increase in peak amplitude PMID: 24225951
  14. Our results support the hypothesis that KChIPs enhances Kv4.2 functional expression by a 1 : 1 suppression of the N-terminal FERN domain and by producing additional positive regulatory effects on functional channel expression. PMID: 23692269
  15. Autoantibodies from patients with encephalitis are specific for DPPX (a subunit of Kv4.2) without reacting to Kv4.2. PMID: 23225603
  16. Seizures in Kv4.2 transgenic mice rapidly redistribute K+ channel subunit Kv4.2 to the neuronal surface, implicating a molecular substrate for the increased K+ current. PMID: 22122031
  17. KChIP2 differentially regulates total and cell surface Kv4.2 protein expression and Kv4 current densities. PMID: 20709747
  18. MiRP3 modulates Kv4.2 current activation, inactivation and recovery from inactivation. MiRP3 shifts the half-maximal voltage for activation and slows time to peak ~ 100%. PMID: 20498229
  19. PSD-95 increased the amount of Kv1.4, but not Kv4.2, in lipid rafts. PMID: 14559911
  20. Kv4.2 and K+ channel-interacting protein 2 make up a complex of Ito channels PMID: 14623880
  21. Data show that KChIP1, KChIP2.1, and KChIP2.2 could form homo- as well as hetero-oligomers, and that this oligomerization did not perturb their interaction with Kv4.2 potassium channel. PMID: 15358149
  22. mutations in KCND2 and KCND3 are not a frequent cause of long QT syndrome PMID: 15563876
  23. Data show that the Kv4.2 voltage-dependent potassium channel acts as a fast-responding steroid sensor in human granulosa cells. PMID: 15991246
  24. Traffic of Kv4.2 is coat protein complex I (COPI)-dependent. PMID: 16260497
  25. the C-terminal domain of Kv4.2 plays a critical role in voltage-dependent activation and functional expression that is mediated by direct interaction between the Kv4.2 C terminus and KChIP2 PMID: 16820361
  26. Electrophysiological analysis indicates attenuated K+ current density in cells expressing this Kv4.2-N587fsX1 mutant channel, which is consistent with a model of aberrant neuronal excitability characteristic of TLE. PMID: 16934482
  27. two Ca2+-dependent posttranslational events regulate the activity of DREAM on Kv4.2 channel function PMID: 17102134
  28. Our results further suggest distinct mechanisms for Kv4.2 gating modulation by KChIPs and DPPs. PMID: 17981906
  29. biophysical and biochemical methods indicate that I(SA) channels carry four subunits each of Kv4.2 and DPP6. PMID: 18364354
  30. rodent and human Abeta are effective in modulating K currents PMID: 18463498
  31. An ALA-scanning mutagenesis in the S4-S5 linker region, the initial part of S5, and the distal part of S6, in X. laevis oocytes showed that temporary uncoupling at the interface between V sensor and cytoplasmic gate may underlie closed-state inactivation. PMID: 19171772
  32. SAP97 is a major partner for surface expression and CaMKII-dependent regulation of cardiac Kv4.2 and kv4.3 channels. PMID: 19213956
  33. the inhibition of maximal amplitude of Kv4.2 channels by arachidonic acid can explain the inhibition of somatodendritic I(A) in hippocampal neurons PMID: 19453640
  34. This study indicated that Kv4.2 is expressed in both neuronal and glial cells and its regulation may involve potassium channel interacting proteins, alterations in the subcellular localization of the channel. PMID: 19596445

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.

Recently viewed