Anti-SK2 potassium channel Antibody Biotin Conjugate (K78/29)
Our mouse SK2 potassium channel biotin conjugate monoclonal antibody from NeuroMab is produced in-house from clone K78/29. It detects human, mouse, and rat SK2 potassium channel and is purified by Protein A chromatography. Works in ELISA, IHC, ICC, WB.
Human, Mouse, Rat
ELISA, ICC, IHC, WB
Mouse
SKU: 75-403-BTN
Ships: 1-5 business days
Product Details
SK2 potassium channel
Potassium calcium-activated channel subfamily N member 2 is encoded by the gene KCNN2. KCNN2 is a member of the potassium KCNN family, KCa2.2/KCNN2 subfamily. KCNN2 is an integral membrane protein that forms a voltage-independent calcium-activated channel with three other calmodulin-binding subunits. Activation of KCNN2 leads to membrane hyperpolarization. KCNN2 is expressed in the brain. Diseases associated with KCNN2 include Dyskeratosis Congenita, Autosomal Dominant 3 and Coronary Aneurysm.
Purified by Protein A chromatography
Lot dependent: provided at 0.3-0.5 mg/mL
Monoclonal
K78/29
IgG1
ELISA, ICC, IHC, WB
Mouse
Kcnn2
50-80 kDa (and larger due to isoforms and dimerization/aggregation)
Synthetic peptide amino acids 546-562 (ENYDKHVTYNAERSRSS, cytoplasmic C-terminus) of rat SK2 (accession number P70604)
Rat
Human, Mouse, Rat
Aliquot and store at ≤ -20°C for long term storage. For short term storage, store at 2-8°C. For maximum recovery of product, centrifuge the vial prior to removing the cap.
Liquid
Produced by in vitro bioreactor culture of hybridoma line followed by Protein A affinity chromatography and conjugation of purified mAb. Purified mAbs are >90% specific antibody.
PBS with 0.09% azide
Biotin
Does not cross-react with other SK channels
These antibodies are to be used as research laboratory reagents and are not for use as diagnostic or therapeutic reagents in humans.
United States
12 months from date of receipt
KCa2.2; Small conductance calcium-activated potassium channel protein 2; SKCa 2; SK2; SKCa2
P70604
UniProt Summary: Small conductance calcium-activated potassium channel that mediates the voltage-independent transmembrane transfer of potassium across the cell membrane through a constitutive interaction with calmodulin which binds the intracellular calcium allowing its opening. The current is characterized by a voltage-independent activation, an intracellular calcium concentration increase-dependent activation and a single-channel conductance of about 3 picosiemens. Also presents an inwardly rectifying current, thus reducing its already small outward conductance of potassium ions, which is particularly the case when the membrane potential displays positive values, above + 20 mV. The inward rectification could be due to a blockade of the outward current by intracellular divalent cations such as calcium and magnesium and could also be due to an intrinsic property of the channel pore, independent of intracellular divalent ions. There are three positively charged amino acids in the S6 transmembrane domain, close to the pore, that collectively control the conductance and rectification through an electrostatic mechanism. Additionally, electrostatic contributions from these residues also play an important role in determining the intrinsic open probability of the channel in the absence of calcium, affecting the apparent calcium affinity for activation. Forms an heteromeric complex with calmodulin, which is constitutively associated in a calcium-independent manner. Channel opening is triggered when calcium binds the calmodulin resulting in a rotary movement leading to the formation of the dimeric complex to open the gate. Plays a role in the repolarization phase of cardiac action potential.
UniProt Summary: Small conductance calcium-activated potassium channel that mediates the voltage-independent transmembrane transfer of potassium across the cell membrane through a constitutive interaction with calmodulin which binds the intracellular calcium allowing its opening. The current is characterized by a voltage-independent activation, an intracellular calcium concentration increase-dependent activation and a single-channel conductance of about 3 picosiemens. Also presents an inwardly rectifying current, thus reducing its already small outward conductance of potassium ions, which is particularly the case when the membrane potential displays positive values, above + 20 mV. The inward rectification could be due to a blockade of the outward current by intracellular divalent cations such as calcium and magnesium and could also be due to an intrinsic property of the channel pore, independent of intracellular divalent ions. There are three positively charged amino acids in the S6 transmembrane domain, close to the pore, that collectively control the conductance and rectification through an electrostatic mechanism. Additionally, electrostatic contributions from these residues also play an important role in determining the intrinsic open probability of the channel in the absence of calcium, affecting the apparent calcium affinity for activation. Forms an heteromeric complex with calmodulin, which is constitutively associated in a calcium-independent manner. Channel opening is triggered when calcium binds the calmodulin resulting in a rotary movement leading to the formation of the dimeric complex to open the gate. Plays a role in the repolarization phase of cardiac action potential.
54262
Shipped on ice packs

