Recombinant Rat Alpha-crystallin A chain (Cryaa)

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Code CSB-EP006007RA
Abbreviation Recombinant Rat Cryaa protein
MSDS
Size $256
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Purity
Greater than 95% as determined by SDS-PAGE.
Activity
Not Test
Target Names
Cryaa
Uniprot No.
Research Area
Neuroscience
Species
Rattus norvegicus (Rat)
Source
E.coli
Expression Region
1-196aa
Target Protein Sequence
MDVTIQHPWFKRALGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISELMTHMWFVMHQPHAGNPKNNPGKVRSDRDKFVIFLDVKHFSPEDLTVKVLEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFSGPKVQSGLDAGHSERAIPVSREEKPSSAPSS
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.
Mol. Weight
29.4 kDa
Protein Length
Full Length
Tag Info
C-terminal 6xHis-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.

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Target Background

Function
Contributes to the transparency and refractive index of the lens. 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.; Inhibits bacterial growth in the lens.
Gene References into Functions
  1. Rat crystallin alpha A a encode activated chaperones. PMID: 26378715
  2. Cryaa is a moonlighting protein that functions as a heat shock protein as well as a lens crystalline. PMID: 7556464
  3. The alphaA- and alphaB-crystallin peptides inhibited stress-induced aggregation of four client proteins, and the alphaA-acetyl peptide was more effective than the native peptide against three of the client proteins. PMID: 23508955
  4. alphaA-crystallin and alphaB-crystallin reside in separate subcellular compartments in the developing ocular lens PMID: 23071119
  5. The main differences, which could be attributed to the cataract-specific processes, are the faster decay of the content of gamma-crystallins and the significant decrease of unmodified alphaA-crystallin abundance in the senescent rat lenses. PMID: 21677790
  6. Curcumin suppressed the expression of selenite-induced alphaA- and alphaB-crystallin and Hsp 70, and may therefore suppress cataract formation in rat pups PMID: 21311744
  7. hydroxylation and subsequent phosphorylation of a proline residue in alpha-crystallin A in the eye as well as in heart tissue of rat. PMID: 20682783
  8. An important role is demonstrated for the C-terminal extension of alpha A crystallin, Arg-163 in particular, whereas no significant role is found for the C-terminal flexible tail in the oligomer assembly of alpha A-crystallin. PMID: 14529298
  9. In samples from rats of all ages, the content of alpha A crystallin is significantly decreased in the oldest rats, indicative that protection against stress-induced protein aggregation is compromised in the aged retina. PMID: 14690441
  10. The results indicate that elevated expression of alpha-crystallins in some tissues may have implications in pathophysiology of diabetic complications. PMID: 16309625
  11. The role of arginine-163 is to provide a positive charge for intersubunit electrostatic interactions in the carboxy-terminal domain of alpha A-crystallin. PMID: 17176090
  12. alpha A-K11T and alpha B-K90T/K92T mutants showed the largest decrease in glycation and increase in chaperone activity. PMID: 18158587
  13. Enhanced survival of axotomized axons was observed beyond the crush site after a single intravitreal administration of alpha-crystallin at the time of axotomy. PMID: 18551258

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Subcellular Location
Cytoplasm. Nucleus.
Protein Families
Small heat shock protein (HSP20) family
Tissue Specificity
Highly expressed in eye lens. Also expressed in non-lenticular tissues such as brain, spleen, liver, lung, skin, small intestine and a several epithelial and fibroblast cell lines with highest levels in spleen.
Database Links
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