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Human Clcn1 Recombinant Protein (N-His) (HW489012)

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Overview
Catalog No.HW489012
Description
Recombinant Human Clcn1 Protein, N-His (HW489012) expressed in E. coli, spanning Leu587-Gly877. Purity: >90% by SDS-PAGE.
Highlights
  • His-Tagged — N-terminal 6×His tag for IMAC purification.
  • E. coli Expression — High-yield, cost-effective production.
  • High Purity — >90% purity verified by SDS-PAGE.
Expression systemE. coli
AccessionP35523
Protein lengthLeu587-Gly877
ApplicationsELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
SpeciesHomo sapiens (Human)
Nature Recombinant
Endotoxin level Please contact with the lab for this information.
Purity >90% as determined by SDS-PAGE.
Predicted molecular weight 34.51 kDa
Form Lyophilized
Storage buffer Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.

Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.

Reconstitution Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
Shipping In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
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.
Alternate NamesCLC1, CLCN1, Chloride channel protein 1, Chloride channel protein, skeletal muscle, ClC-1
Background

Chloride channel protein 1 is a ~108 kDa protein. Voltage-gated chloride channel involved in skeletal muscle excitability. Generates most of the plasma membrane chloride conductance in skeletal muscle fibers, stabilizes the resting membrane potential and contributes to the repolarization phase during action potential firing. Forms a homodimeric channel where each subunit has its own ion conduction pathway. Conducts double-barreled currents controlled by two types of gates, two fast glutamate gates that control each subunit independently and a slow common gate that opens and shuts off both subunits simultaneously. Has a significant open probability at muscle resting potential and is further activated upon membrane depolarization.

1. Ryan, A. et al. (2002) The Journal of physiology 545, 345-54. PMID: 12456816
2. Bennetts, B. et al. (2005) The Journal of biological chemistry 280, 32452-8. PMID: 16027167
3. Ulzi, G. et al. (2012) Journal of the neurological sciences 318, 65-71. PMID: 22521272
4. Weinberger, S. et al. (2012) The Journal of physiology 590, 3449-64. PMID: 22641783
5. Portaro, S. et al. (2015) Neuromolecular medicine 17, 285-96. PMID: 26007199
6. Ronstedt, K. et al. (2015) Scientific reports 5, 15382. PMID: 26502825
7. Vindas-Smith, R. et al. (2016) Human mutation 37, 74-83. PMID: 26510092
8. Lorenz, C. et al. (1994) Human molecular genetics 3, 941-6. PMID: 7951242
9. Steinmeyer, K. et al. (1994) The EMBO journal 13, 737-43. PMID: 8112288
10. Pusch, M. et al. (1994) Biophysical journal 66, 149-52. PMID: 8130334
Note For research use only
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