| Field | Specification |
|---|---|
| Mfr No | |
| Activity | |
| Alternative Names | Voltage-gated K(+) channel HuKI1 |
| Conjugate | |
| Endotoxin Level | |
| Expression System | |
| Form | Liquid or Lyophilized powder |
| Function | |
| Molecular Weight | |
| Product Type | |
| Protein Length | |
| Purity | |
| Reconstitution | |
| Species | |
| Storage | |
| Target | |
| UniProt # |
Overview
Recombinant Human Potassium voltage-gated channel subfamily A member 1 (KCNA1), partial is a recombinant protein reagent for research-use applications such as assay development, binding studies, and mechanistic experiments. It corresponds to KCNA1 (Homo sapiens (Human)) and is intended for RUO workflows where a defined protein standard or functional input is needed.
Key elements and design rationale
- Expression system: E.coli (expression context can influence folding and PTMs).
- Expression region: 1-154aa (region choice can affect activity and binding readouts).
- Conjugate(s)/tag: N-terminal 6xHis-tagged (can support detection or purification depending on format).
- Molecular weight: 22.2 kDa (useful for interpreting gel migration and size-exclusion profiles).
When comparing results across assays, consider that expression system and expressed region can alter glycosylation, disulfide formation, and oligomerization state, which may shift apparent potency or binding behavior in vitro.
Biological background
Voltage-gated potassium channel that mediates transmbrane potassium transport in excitable mbranes, primarily in the brain and the central nervous syst, but also in the kidney . Contributes to the regulation of the mbrane potential and nerve signaling, and prevents neuronal hyperexcitability . Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the mbrane . Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNA7, and possibly other family mbers as well; channel properties depend on the type of alpha subunits that are part of the channel . Channel properties are modulated by Cytoplasmic domain beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation of delayed rectifier potassium channels . In vivo, mbranes 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 mber. Homotetrameric KCNA1 forms a delayed-rectifier potassium channel that opens in response to mbrane depolarization, followed by slow spontaneous channel closure . In contrast, a heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid inactivation . Regulates neuronal excitability in hippocampus, especially in mossy fibers and medial perforant path axons, preventing neuronal hyperexcitability. Response to toxins that are selective for KCNA1, respectively for KCNA2, suggests that heteromeric potassium channels composed of both KCNA1 and KCNA2 play a role in pacaking and regulate the output of deep cerebellar nuclear neurons . May function as down-stream effector for G protein-coupled receptors and inhibit GABAergic inputs to basolateral amygdala neurons . May contribute to the regulation of neurotransmitter release, such as gamma-aminobutyric acid (GABA) release . Plays a role in regulating the generation of action potentials and preventing hyperexcitability in myelinated axons of the vagus nerve, and thereby contributes to the regulation of heart contraction . Required for normal neuromuscular responses . Regulates the frequency of neuronal action potential firing in response to mechanical stimuli, and plays a role in the perception of pain caused by mechanical stimuli, but does not play a role in the perception of pain due to heat stimuli . Required for normal responses to auditory stimuli and precise location of sound sources, but not for sound perception . The use of toxins that block specific channels suggest that it contributes to the regulation of the axonal release of the neurotransmitter dopamine . Required for normal postnatal brain development and normal proliferation of neuronal precursor cells in the brain . Plays a role in the reabsorption of Mg2+ in the distal convoluted tubules in the kidney and in magnesium ion homeostasis, probably via its effect on the mbrane potential .
Research relevance and current trends
- Reagent standardization: using recombinant proteins as reference materials for quantitative calibration and cross-study comparability.
- Interaction-focused studies: mapping binding partners, affinity changes, and structure–function relationships across variants or domains.
- Multi-omic readouts: combining recombinant perturbations with transcript, protein, and functional endpoints to connect mechanism to phenotype.
Common research applications
- Assay development and validation: use as a defined input or standard where protein identity is required.
- Binding studies: evaluate interaction strength and specificity using plate-based or biophysical formats.
- Cell-response profiling: add protein to cultured cells and interpret downstream marker changes with appropriate controls.
Interpretation is most robust when signal changes are evaluated relative to matched controls (buffer-only, unrelated protein controls, or pathway controls) and when readouts are compared across dose and time.
Notes for experimental interpretation
- Isoforms and PTMs can influence binding and activity; ensure the expressed region and expression system match your experimental needs.
- Species differences may affect receptor binding or antibody recognition; confirm species/source alignment with your model.
- Use concept-level controls such as negative controls (no protein), matrix controls, or orthogonal readouts to support conclusions.
What is protein expression and purification?
Why is there no/low protein expression?
b. Rare codons. You should optimize codons, use strains supplementing rare codons, induce at lower temperature or grow in poor media.
c. Protein toxicity. You should use promoters with tighter regulation or lower plasmid copy number. Use pLysS/pLysE bearing strains in T7-based systems or strains that are better for the expression of toxic proteins. Start induction at high OD and shorten induction time. Add glucose when using expression vectors containing lac-based promoters.
How to avoid inclusion bodies and improve soluble expression?
b. Incorrect disulfide bond formation. You should add fusion partners, including thioredoxin, DsbA, DsbC. Clone in a vector containing secretion signal peptide to cell periplasm. Use gamiB (DE3)strains with oxidative cytoplasmic environment. Lower inducer concentration and induction temperature.
c. Incorrect folding. You should use a fusion partner. Co-express with molecular chaperones. Use strains with cold-adapted chaperones. Supplement media with chemical chaperones and cofactors. Reduce the inducer concentration and add fresh media. Induce for a shorter time at low temperature.
Why is the molecular weight of protein smaller than the predicted?
b. Imbalanced translation process of fusion protein. You should change another fusion tag or move fusion tag to C-terminal. You should induce for a shorter time at low temperature or change to poor media.
c. Protein degradation. You should replace specific protease sites. Use protease deficient strains. Induce at high OD. You should induce for a shorter time at low temperature or use protease inhibitors when breaking cells.
Why is the actual band size different from the predicted?
b. Post-translational cleavage. Many proteins are synthesized as pro-proteins, and then cleaved to give the active form.
c. Splice variants. Alternative splicing may create different sized proteins from the same gene.
d. Relative charge. The composition of amino acids have different relative charge which will affect the electrophoretic mobility.
e. Multimers such as dimerisation of a protein. This is usually prevented in reducing conditions, although strong interactions can result in the appearance of higher bands.
f. Protein structure such as disulfide bond, protein secondary structure or protein 3D structure formation.
g. Hydrophobic proteins, such as transmembrane proteins, may have difficulties in migrating into the gel, and thus resulting in different multi-banded patterns.
How to express a protein with bioactivity? Why is the protein inactive?
a. Low solubility of the protein. You should fuse desired protein to a fusion partners and lower temperature.
b. Lack of essential post translational modification. You should change another expression system.
c. Incomplete folding. You should use a fusion partner and use strains with cold-adapted chaperones. Co-express with molecular chaperones at lower temperature. Monitor disulfide bond formation and allow further folding in vitro.
d. Mutations in cDNA. You should sequence plasmid before and after induction or use a recA− strain to ensure plasmid stability. Transform E. coli before each expression round.
Why are our protein products almost invisible in pipes?
Tips: Before opening the lid, we recommend to centrifuge in a small centrifuge for 20-30 seconds firstly to ensure that the contents are on the bottom of the tube. Our quality control steps ensure that the amount of protein contained in each tube is accurate, although sometimes you can’t see the protein powder, but the protein content in the tube is still very accurate.
How is the protein purified? Is the purity guaranteed?
Although we guarantee a minimum purity standard of >85%, some of the proteins we prepared have a purity of 95% or even 97%.
How should I reconstitute and store the products?
As for short-term storage or usage, please use sterile deionized water to completely reconstitute proteins to 0.1-1.0 mg/mL. Aliquot after 10-15 minutes if needed and store at 4℃.
As for long-term storage, the cytokines or recombinant proteins are recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
What types of tags do you use for fusion?
What is the impact of a given tag type and any potential biological activity of the protein?
Can you remove the endotoxin?
Can you offer aseptic manufacture processing?
How to determine species cross-reactivity of cytokines?
b. Many mouse cytokines may also have effect on human cells, however, the activity may be lower than the corresponding human cytokines.
c. One of the few human cytokines will be more active than corresponding mouse cytokines when acting on mouse cells, such as IL-7.
d. Interferon, GM-CSF, IL-3 and IL-4 and other cytokines are species-specific and almost have no activity on non-homologous cells.
e. In contrast, fibroblast growth factor (FGF) and neurotrophin are highly conserved and both have good activity on cells of different species.
What is the general preservative? Which kind of preservative do you usually add?
What is the general protectant? What kind of protectant do you usually add?
Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.
