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Human CRYAA Recombinant Protein (N-His) (HC982012)

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Overview
Catalog No.HC982012
Description
Recombinant Human CRYAA Protein, N-His (HC982012) expressed in E. coli, spanning Met1-Ser173. 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
AccessionP02489
Protein lengthMet1-Ser173
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 22.07 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-crystallin A chain, Alpha-crystallin A(1-162), Alpha-crystallin A(1-168), Alpha-crystallin A(1-172), CRYA1, CRYAA, HSPB4, Heat shock protein beta-4, Heat shock protein family B member 4, HspB4
Background

Alpha-crystallin A chain is a ~19 kDa protein. Contributes to the transparency and refractive index of the lens. In its oxidized form (absence of intramolecular disulfide bond), acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA.

1. Richter, L. et al. (2008) American journal of medical genetics. Part A 146A, 833-42. PMID: 18302245
2. Murugesan, R. et al. (2007) Molecular vision 13, 2301-9. PMID: 18199971
3. Bhagyalaxmi, SG. et al. (2009) Biochimica et biophysica acta 1792, 974-81. PMID: 19595763
4. Nagaraj, RH. et al. (2012) Biochimica et biophysica acta 1822, 120-9. PMID: 22120592
5. Kaiser, CJO. et al. (2019) Nature structural & molecular biology 26, 1141-1150. PMID: 31792453
6. Chaves, JM. et al. (2017) Biochemical and biophysical research communications 494, 402-408. PMID: 28935373
Note For research use only
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Formula
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