Recombinant Rana temporaria Alpha-crystallin A chain (CRYAA)

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Description

Compound Overview

Recombinant Rana temporaria Alpha-Crystallin A Chain (CRYAA) is a 149-amino-acid protein (residues 1–149) expressed in yeast with a C-terminal polyhistidine (His) tag for purification . It belongs to the small heat shock protein (sHSP) family and functions as a molecular chaperone, preventing protein aggregation under stress conditions. This protein is critical for lens transparency in vertebrates and plays roles in cellular stress response and structural stability .

Sequence and Modifications

  • Post-Translational Modifications: Produced in yeast, enabling eukaryotic modifications such as glycosylation and phosphorylation .

Biophysical Properties

PropertyValue
Molecular Weight~19–20 kDa (predicted)
Purity>90% (SDS-PAGE)
BufferTris-based, 50% glycerol
StabilityStable at -20°C; avoid freeze-thaw cycles

Production and Purification

  • Expression System: Yeast (Saccharomyces cerevisiae), chosen for cost-efficiency and ability to perform eukaryotic post-translational modifications .

  • Purification: Affinity chromatography via His tag .

  • Yield: 0.2–2 mg/mL post-lyophilization .

Advantages of Yeast Expression

  • Cost-Effective: Higher yield compared to mammalian systems .

  • Native Conformation: Supports proper folding and functional modifications (e.g., glycosylation) .

Research Applications

  • ELISA: Primary application for antigen detection .

  • Chaperone Activity: Prevents aggregation of denatured proteins, analogous to human CRYAA .

  • Lens Biology Studies: Used to investigate crystallin’s role in lens transparency and cataract formation .

Protein Interactions

A human proteome microarray study (17,225 proteins) identified 127 CRYAA interactors, including:

  • DNA Repair Proteins: RAD51, PTTG2, PMS2 .

  • Cytoskeletal Regulators: LIMA1 (actin stabilization), TUBAL3 (microtubule integrity) .

Functional Clusters

ClusterKey ProteinsRole
Cell Cycle RegulationHCLS1, KLHDC6Mitotic progression
Stress ResponseHSPB4, SGCDChaperone activity
DNA RepairRAD51, EYA4Genome stability maintenance

Comparative Analysis with Orthologs

FeatureR. temporaria CRYAA Human CRYAA
Host SystemYeastE. coli, HEK-293
Amino Acid Range1–1491–173
TagHisHis, GST
ApplicationsELISAWB, SDS-PAGE, functional assays

Future Directions

  • Structural Studies: Cryo-EM analysis to resolve chaperone-substrate interactions.

  • Therapeutic Potential: Explore CRYAA’s role in preventing amyloidogenesis in neurodegenerative diseases .

Product Specs

Form
Lyophilized powder. We will ship the in-stock format by default. If you have specific format requirements, please note them when ordering.
Lead Time
Delivery times vary based on purchasing method and location. Consult your local distributor for specifics. All proteins are shipped with standard blue ice packs. Request dry ice in advance for an extra fee.
Notes
Avoid repeated freezing and thawing. Working aliquots are stable at 4°C for up to one week.
Reconstitution
Briefly centrifuge the vial before opening. Reconstitute in sterile deionized water to 0.1-1.0 mg/mL. Add 5-50% glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final glycerol concentration is 50%.
Shelf Life
Shelf life depends on storage conditions, buffer components, temperature, and protein stability. Liquid form is generally stable for 6 months at -20°C/-80°C. Lyophilized form is generally stable for 12 months at -20°C/-80°C.
Storage Condition
Store at -20°C/-80°C upon receipt. Aliquot for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
The tag type is determined during manufacturing. Please inform us if you require a specific tag, and we will prioritize its development.
Synonyms
CRYAAAlpha-crystallin A chain; Fragment
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
1-149
Protein Length
full length protein
Purity
>85% (SDS-PAGE)
Species
Rana temporaria (European common frog)
Target Names
CRYAA
Target Protein Sequence
QVFGEGMFDY DLFPFLTSTV SPHYRHGLLR GFMDSGISEV RSDRDRFTIN LDVKHFSPDD LTVKILDDFV EIHGKHSERQ DDHGYISREF HRRYRLPSNL DQSSISCSLS ADGILTFSGP KMMSNLVSSH SERPIPVSRE EKPTSAPSS
Uniprot No.

Target Background

Function
Contributes to lens transparency and refractive index. May function as a chaperone, preventing protein aggregation under various stress conditions.
Protein Families
Small heat shock protein (HSP20) family
Subcellular Location
Cytoplasm. Nucleus.

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