Recombinant Bovine Alpha-crystallin A chain (CRYAA)

Code CSB-YP006007BO
MSDS
Size Pls inquire
Source Yeast
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Code CSB-EP006007BO
MSDS
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Source E.coli
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Code CSB-EP006007BO-B
MSDS
Size Pls inquire
Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP006007BO
MSDS
Size Pls inquire
Source Baculovirus
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Code CSB-MP006007BO
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
CRYAA
Uniprot No.
Alternative Names
CRYAA; CRYA1Alpha-crystallin A chain [Cleaved into: Alpha-crystallin A(1-172); Alpha-crystallin A(1-168)]
Species
Bos taurus (Bovine)
Expression Region
1-173
Target Protein Sequence
MDIAIQHPWF KRTLGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ SLFRTVLDSG ISEVRSDRDK FVIFLDVKHF SPEDLTVKVQ EDFVEIHGKH NERQDDHGYI SREFHRRYRL PSNVDQSALS CSLSADGMLT FSGPKIPSGV DAGHSERAIP VSREEKPSSA PSS
Protein Length
Full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
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 before Lyophilization
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℃/-80℃. 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
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
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.
Gene References into Functions
  1. Data show that both green and red light wavelengths induce structural changes in betaL-crystalline. PMID: 26656181
  2. For moderate O-GlcNAcylation on bovine crystalline alpha, the preferred amino acids were Pro > Ala > Gly at position -2, Ala > Thr >Val > Lys > Pro at position -1, and Ala > Gly > Arg > Glu at position +2. PMID: 24760753
  3. We show that proteases with the potential to generate alphaA-66-80 peptide are present in bovine and human lenses. PMID: 23410823
  4. These results show that between pH 7 and 10 the protein undergoes a reversible thermal transition. PMID: 21445944
  5. alpha-crystallin is characterized by homogeneous distribution of scattering density in the domains inaccessible for water penetration PMID: 21314599
  6. Results show that structural perturbations by high hydrostatic pressures enhance the chaperone-like activity of alpha-crystallin. PMID: 12485117
  7. new light on structural properties of alpha-crystallin and its superhydration properties and have important implications for understanding the mechanism of the chaperone-like action of this protein in the lens and non-ocular tissues PMID: 14616086
  8. Alpha-crystallin, in the presence of the sorbitol dehydrogenase (SDH) pyridine cofactor NAD(H), can exert a remarkable chaperone action by favoring the recovery of the enzyme activity from chemically denaturated SDH up to 77%. PMID: 15747064
  9. Conserved triad in alphaA-crystallin contributes to stability of higher order oligomers but is not essential for formation of tetramers. PMID: 17960114
  10. The spatial distributions of alpha-crystallin and its modified forms in bovine and rabbit lenses, were analysed. PMID: 18334935
  11. The results are consistent with the hypothesis that short-range, weak, attractive interactions between alpha- and gamma-crystallins are necessary for maximum transparency of the lens. PMID: 18509547
  12. Mass spectrometry analysis and a database search identified carbamylated proteins originating from alphaA-crystallin, betaB2- and gammaS-(betaS)-crystallins. PMID: 19085379
  13. The structure and properties of alpha-crystallin have changed relatively little during the evolutionary period from the emergence of sharks and mammals. PMID: 19956560

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Subcellular Location
Cytoplasm. Nucleus.
Protein Families
Small heat shock protein (HSP20) family
Database Links

KEGG: bta:281718

STRING: 9913.ENSBTAP00000004073

UniGene: Bt.397

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