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Human CTNNA2 Recombinant Protein (N-His) (HC915012)

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Overview
Catalog No.HC915012
Description
Recombinant Human CTNNA2 Protein, N-His (HC915012) expressed in E. coli, spanning Met1-Ala260. 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
AccessionP26232
Protein lengthMet1-Ala260
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 30.85 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 NamesAlpha N-catenin, Alpha-catenin-related protein, CAPR, CTNNA2, Catenin alpha-2
Background

Catenin alpha-2 is a ~105 kDa protein. May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system. Required for proper regulation of cortical neuronal migration and neurite growth. It acts as a negative regulator of Arp2/3 complex activity and Arp2/3-mediated actin polymerization. It thereby suppresses excessive actin branching which would impair neurite growth and stability. Regulates morphological plasticity of synapses and cerebellar and hippocampal lamination during development.

1. Schaffer, AE. et al. (2018) Nature genetics 50, 1093-1101. PMID: 30013181
Note For research use only
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Formula
Mass (g) = Concentration (mol/L) × Volume (L) × MW (g/mol)
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Formula
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Stock Solution
C₁ (Stock Conc.)
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V₁ (Stock Vol.)
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Working Solution
C₂ (Working Conc.)
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