Anti-KCNAB2 Polyclonal Antibody (HA563014) is a rabbit polyclonal antibody detecting KCNAB2 in WB, IHC, ELISA. Suitable for Human, Mouse, Rat, Dog, and Cat.
Highlights
●Affinity Purified — Minimal background and high purity for reliable results.
●Multi-Application — Validated across multiple applications.
●Multi-Species — Cross-reactive for translational research.
Species reactivity
Human, Mouse, Rat, Dog, Cat, Bovine, Pig, Zebrafish, African clawed frog, Alpaca, Camel, Chicken, Duck, Ferret, Goose, Horse, Pigeon, Rabbit, Red fox, Sheep, Tree shrew, Turkey
Applications
WB,IHC,ELISA
Host species
Rabbit
Isotype
IgG
Species
Homo sapiens (Human)
Clonality
Polyclonal
Immunogen
E. coli - derived recombinant human KCNAB2 (Gln37-Ser367).
Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.
Product Usage Information
Application
Dilution
ELISA
1:5000-1:20000
IHC
1:50-1:500
WB
1:500-1:2000
Stability and Storage
Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
Voltage-gated potassium channel subunit beta-2 (KCNAB2) is a ~41 kDa protein. Regulatory subunit of the voltage-gated potassium (Kv) Shaker channels composed of pore-forming and potassium-conducting alpha subunits and of regulatory beta subunits. The beta-2/KCNAB2 cytoplasmic subunit promotes potassium channel closure via a mechanism that does not involve physical obstruction of the channel pore. Promotes the inactivation of Kv1.4/KCNA4 and Kv1.5/KCNA5 alpha subunit-containing channels. Displays nicotinamide adenine dinucleotide phosphate (NADPH)-dependent aldoketoreductase activity by catalyzing the NADPH-dependent reduction of a wide range of aldehyde and ketone substrates. Substrate specificity includes methylglyoxal, 9,10-phenanthrenequinone, prostaglandin J2, 4-nitrobenzaldehyde, 4-nitroacetophenone and 4-oxo-trans-2-nonenal (in vitro, no physiological substrate identified yet).
1. McCormack, K. et al. (2002) The Journal of biological chemistry 277, 13219-28. PMID: 11825900
2. McCormack, K. et al. (1995) FEBS letters 370, 32-6. PMID: 7649300
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