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Western blotAntibody data
- Antibody Data
- Antigen structure
- References [4]
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- Product number
- ABIN350420 - Provider product page
- Provider
- antibodies-online
- Proper citation
- Antibodies-Online Cat#ABIN350420, RRID:AB_10787506
- Product name
- anti-Potassium Large Conductance Calcium-Activated Channel, Subfamily M, beta Member 2 (KCNMB2) (N-Term) antibody
- Antibody type
- Polyclonal
- Antigen
- A synthetic peptide from the n-terminal region of human KCNMB2 (Maxi K channel subunit beta-2) conjugated to an immunogenic carrier protein was used as the immunogen. The antigen is homologous in rat and mouse.
- Reactivity
- Human
- Host
- Rabbit
- Epitope
- N-Term
- Vial size
- 100 μL
- Storage
- Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability.
- Handling
- Avoid freeze and thaw cycles.
Submitted references Inactivation of BK channels by the NH2 terminus of the beta2 auxiliary subunit: an essential role of a terminal peptide segment of three hydrophobic residues.
NMR structure of the "ball-and-chain" domain of KCNMB2, the beta 2-subunit of large conductance Ca2+- and voltage-activated potassium channels.
A neuronal beta subunit (KCNMB4) makes the large conductance, voltage- and Ca2+-activated K+ channel resistant to charybdotoxin and iberiotoxin.
Molecular basis of fast inactivation in voltage and Ca2+-activated K+ channels: a transmembrane beta-subunit homolog.
Xia XM, Ding JP, Lingle CJ
The Journal of general physiology 2003 Feb;121(2):125-48
The Journal of general physiology 2003 Feb;121(2):125-48
NMR structure of the "ball-and-chain" domain of KCNMB2, the beta 2-subunit of large conductance Ca2+- and voltage-activated potassium channels.
Bentrop D, Beyermann M, Wissmann R, Fakler B
The Journal of biological chemistry 2001 Nov 9;276(45):42116-21
The Journal of biological chemistry 2001 Nov 9;276(45):42116-21
A neuronal beta subunit (KCNMB4) makes the large conductance, voltage- and Ca2+-activated K+ channel resistant to charybdotoxin and iberiotoxin.
Meera P, Wallner M, Toro L
Proceedings of the National Academy of Sciences of the United States of America 2000 May 9;97(10):5562-7
Proceedings of the National Academy of Sciences of the United States of America 2000 May 9;97(10):5562-7
Molecular basis of fast inactivation in voltage and Ca2+-activated K+ channels: a transmembrane beta-subunit homolog.
Wallner M, Meera P, Toro L
Proceedings of the National Academy of Sciences of the United States of America 1999 Mar 30;96(7):4137-42
Proceedings of the National Academy of Sciences of the United States of America 1999 Mar 30;96(7):4137-42
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