KCNQ1 Protein (AA 1-668) (Strep Tag)

Catalog No. ABIN3134696

This Recombinant KCNQ1 protein is produced in Cell-free protein synthesis (CFPS).

Quick Overview for KCNQ1 Protein (AA 1-668) (Strep Tag) (ABIN3134696)

Target: KCNQ1 (Potassium Voltage-Gated Channel, KQT-Like Subfamily, Member 1 (KCNQ1))

Protein Type: Recombinant

Origin: Mouse

Source: Cell-free protein synthesis (CFPS)

Application: ELISA, SDS-PAGE (SDS), Western Blotting (WB)

Purity: approximately 70-80 % as determined by SDS PAGE, Western Blot and analytical SEC (HPLC).

Grade: custom-made

Product Details

Protein Characteristics: AA 1-668

Purification tag / Conjugate: This KCNQ1 protein is labelled with Strep Tag.

Sequence: MDTASSPPSA ERKRAGWSRL LGARRGSAVV KKCPFSLELA EGGPEGSTVY APIAPTGAPG LAPPMSTPVS PAPAPADLGP RPRVSLDPRV SIYSARRPLL ARTHIQGRVY NFLERPTGWK CFVYHFTVFL IVLVCLIFSV LSTIEQYAAL ATGTLFWMEI VLVVFFGTEY VVRLWSAGCR SKYVGIWGRL RFARKPISII DLIVVVASMV VLCVGSKGQV FATSAIRGIR FLQILRMLHV DRQGGTWRLL GSVVFIHRQE LITTLYIGFL GLIFSSYFVY LAEKDAVNES GRIEFGSYAD ALWWGVVTVT TIGYGDKVPQ TWVGKTIASC FSVFAISFFA LPAGILGSGF ALKVQQKQRQ KHFNRQIPAA ASLIQTAWRC YAAENPDSAT WKIYVRKPAR SHTLLSPSPK PKKSVMVKKK KFKLDKDNGM SPGEKMFNVP HITYDPPEDR RPDHFSIDGY DSSVRKSPTL LEVSTPHFLR TNSFAEDLDL EGETLLTPIT HVSQLRDHHR ATIKVIRRMQ YFVAKKKFQQ ARKPYDVRDV IEQYSQGHLN LMVRIKELQR RLDQSIGKPS LFIPISEKSK DRGSNTIGAR LNRVEDKVTQ LDQRLVIITD MLHQLLSMQQ GGPTCNSRSQ VVASNEGGSI NPELFLPSNS LPTYEQLTVP QTGPDEGS
Sequence without tag. The proposed Strep-Tag is based on experience with the expression system. Our team may suggest an additional tag depending on the complexity of the protein. If you have a special request, please contact us..

Characteristics: Key Benefits:

• Made in Germany - from design to production - by highly experienced protein experts.
• Protein expressed with ALiCE® and purified in one-step affinity chromatography
• State-of-the-art algorithm used for plasmid design (Gene synthesis).

This protein is a predefined custom protein and will be made for the first time for your order. Our experts in the lab try to ensure that you receive soluble protein.

The big advantage of ordering our predefined custom proteins in comparison to ordering custom made proteins from other companies is that there is no financial obligation in case the protein cannot be expressed or purified.

Expression System:

• ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
• During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein!

Concentration:

• The concentration of our recombinant proteins is measured using the absorbance at 280nm.
• The protein's absorbance will be measured against its specific reference buffer.
• We use the Expasy's ProtParam tool to determine the absorption coefficient of each protein.

Purification: One-step Strep-tag purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®).

Application Details

Application Notes: In addition to the applications listed above we expect the protein to work for functional studies as well. As the protein has not been tested for functional studies yet we cannot offer a guarantee though.

Comment:

ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein!

Restrictions: For Research Use only

Handling

Format: Liquid

Buffer: The buffer composition is at the discretion of the manufacturer.
Standard Storage Buffer: PBS pH 7.4, 10 % Glycerol Might differ depending on protein.

Handling Advice: Avoid repeated freeze-thaw cycles.

Storage: -80 °C

Storage Comment: Store at -80°C.

Expiry Date: 12 months

Target Details

Target: KCNQ1 (Potassium Voltage-Gated Channel, KQT-Like Subfamily, Member 1 (KCNQ1))

Alternative Name: Kcnq1

Background: Potassium voltage-gated channel subfamily KQT member 1 (IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1) (KQT-like 1) (Voltage-gated potassium channel subunit Kv7.1),FUNCTION: Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon (By similarity) (PubMed:16314573, PubMed:11120752, PubMed:15004216). Associates with KCNE beta subunits that modulates current kinetics (By similarity) (PubMed:17597584, PubMed:15004216). Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selective outward current (By similarity) (PubMed:8900282). Promotes also a delayed voltage activated potassium current showing outward rectification characteristic (By similarity). During beta-adrenergic receptor stimulation participates in cardiac repolarization by associating with KCNE1 to form the I(Ks) cardiac potassium current that increases the amplitude and slows down the activation kinetics of outward potassium current I(Ks) (By similarity) (PubMed:15004216, PubMed:17597584). Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current (By similarity). When associated with KCNE3, forms the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions (By similarity). This interaction with KCNE3 is reduced by 17beta-estradiol, resulting in the reduction of currents (By similarity). During conditions of increased substrate load, maintains the driving force for proximal tubular and intestinal sodium ions absorption, gastric acid secretion, and cAMP-induced jejunal chloride ions secretion (PubMed:16314573). Allows the provision of potassium ions to the luminal membrane of the secretory canaliculus in the resting state as well as during stimulated acid secretion (PubMed:19491250). When associated with KCNE2, forms an heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (By similarity). When associated with KCNE4, inhibits voltage-gated potassium channel activity (By similarity). When associated with KCNE5, this complex only conducts current upon strong and continued depolarization (By similarity). Also forms a heterotetramer with KCNQ5, has a voltage-gated potassium channel activity (By similarity). Binds with phosphatidylinositol 4,5-bisphosphate (By similarity). KCNQ1-KCNE2 channel associates with Na(+)-coupled myo-inositol symporter in the apical membrane of choroid plexus epithelium and regulates the myo-inositol gradient between blood and cerebrospinal fluid with an impact on neuron excitability. {ECO:0000250|UniProtKB:P51787, ECO:0000250|UniProtKB:Q9Z0N7, ECO:0000269|PubMed:11120752, ECO:0000269|PubMed:15004216, ECO:0000269|PubMed:16314573, ECO:0000269|PubMed:17597584, ECO:0000269|PubMed:19491250, ECO:0000269|PubMed:24595108, ECO:0000269|PubMed:8900282}.

Molecular Weight: 74.5 kDa

UniProt: P97414

Pathways: Negative Regulation of Hormone Secretion, Sensory Perception of Sound