Crystallin, beta A1 Proteine (CRYBA1)

Crystallins are the dominant structural components of the vertebrate eye lens.. Zusätzlich bieten wir Ihnen Crystallin, beta A1 Antikörper (45) und Crystallin, beta A1 Kits (3) und viele weitere Produktgruppen zu diesem Protein an.

alle Proteine anzeigen Gen GeneID UniProt
CRYBA1 1411 P05813
CRYBA1 12957  
CRYBA1 25583 P14881
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Showing 8 out of 12 products:

Katalog Nr. Origin Quelle Konjugat Bilder Menge Anbieter Lieferzeit Preis Details
Insektenzellen Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Anmelden zum Anzeigen 50 Days
$5,960.83
Details
Insektenzellen Maus His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Anmelden zum Anzeigen 50 Days
$5,960.83
Details
Wheat germ Human GST tag 10 μg Anmelden zum Anzeigen 11 bis 12 Tage
$414.29
Details
HEK-293 Cells Human Myc-DYKDDDDK Tag Validation with Western Blot 20 μg Anmelden zum Anzeigen 10 bis 12 Tage
$554.07
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Hefe Huhn His tag   1 mg Anmelden zum Anzeigen 60 bis 71 Tage
$2,531.83
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Hefe Ratte His tag   1 mg Anmelden zum Anzeigen 60 bis 71 Tage
$2,531.83
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Hefe Rind (Kuh) His tag   1 mg Anmelden zum Anzeigen 60 bis 71 Tage
$2,531.83
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Escherichia coli (E. coli) Maus T7 tag,His tag 100 μg Anmelden zum Anzeigen 15 bis 18 Tage
$704.00
Details

CRYBA1 Proteine nach Spezies und Herkunft

Origin Exprimiert in Konjugat
Human , ,
, ,
Mouse (Murine) ,
,
Rat (Rattus)

Weitere Proteine zu Crystallin, beta A1 (CRYBA1) Interaktionspartnern

Human Crystallin, beta A1 (CRYBA1) Interaktionspartner

  1. We identified a de novo in-frame 3-bp deletion in the proband with an autosomal dominant congenital cataract, but not in her parents, in an Iranian family. This mutation has occurred de novo on a paternal gamete during spermatogenesis. The in-silico results predicted the interaction of CRYBA1 protein with the other CRY (zeige CRY2 Proteine) as well as proteins responsible for eye cell signaling.

  2. association between a frameshift mutation in exon 6 of CRYBA1/A3 and congenital cataracts

  3. Data indicate that alpha-crystallin B chain (zeige CRYAB Proteine) and beta-crystallin A3-cyrstallins dissociate to the monomers upon racemization of d-aspartic acids (Asp (zeige ASIP Proteine)).

  4. A novel splice site mutation in CRYBA1/A3 is associated with autosomal dominant nuclear cataracts in a Chinese family.

  5. A splice site mutation (c.215+1G>A) at the first base of intron 3 of the crystallin beta A3/A1 (CRYBA3/A1) gene has been identified in Chinese congenital polymorphic cataract patients.

  6. ThebetaA3-crystallin and betaB1-crystallin (zeige CRYBB1 Proteine) homomers and the betaA3/betaB1-crystallin (zeige CRYBB1 Proteine) heteromer all undergo similar five-state folding pathways which include one dimeric and two monomeric intermediates.

  7. A G-->T splice site mutation of CRYBA1/A3 associated with autosomal dominant suture cataracts in a Chinese family.

  8. The c.279-281delGAG mutation in CRYBA1 is responsible for the autosomal dominant congenital nuclear cataract disease in this Chinese family.

  9. This is the first report of a phenotype of progressive nuclear and cortical cataracts related to the CRYBA3/A1 mutation IVS3+1 G>A.

  10. This study is the first report relating a mutation of CRYBA1/A3 to posterior polar cataract.

Mouse (Murine) Crystallin, beta A1 (CRYBA1) Interaktionspartner

  1. CRYbetaA3/A1-crystallin has a role in preventing nuclear cataract impaired lysosomal cargo clearance and calpain activation

  2. Data suggest a mechanism by which betaA3/A1-crystallin regulates lysosomal function by modulating the activity of V-ATPase (zeige ATP6V1H Proteine).

  3. Data show that betaA3/A1-crystallin affects the signal transducer and activator of transcription 3 (STAT3 (zeige STAT3 Proteine)) activation in optic nerve astrocytes.

  4. loss of CRYBA1 causes lysosomal dysregulation leading to the impairment of both autophagy and phagocytosis

  5. p53 (zeige TP53 Proteine) can regulate lens differentiation by controlling expression of the differentiation genes coding for the lens crystallins.

  6. The thermodynamic consequences of the loss of beta A3-crystallin terminal extensions by in vivo proteolytic processing could increase their tendency to associate and so promote the formation of higher order associates in the aging and cataractous lens.

Cow (Bovine) Crystallin, beta A1 (CRYBA1) Interaktionspartner

  1. Results show that both betaB2- and betaA3-crystallin bind calcium with moderate affinity.

Crystallin, beta A1 (CRYBA1) Protein Überblick

Protein Überblick

Crystallins are the dominant structural components of the vertebrate eye lens.

Genbezeichner und Symbole assoziert mit Crystallin, beta A1 Proteine (CRYBA1)

  • crystallin beta A4 S homeolog (cryba4.S)
  • crystallin beta A1 (CRYBA1)
  • crystallin beta A1 (cryba1)
  • crystallin beta A1 (Cryba1)
  • crystallin, beta A1 (Cryba1)
  • crystallin beta A1 L homeolog (cryba1.L)
  • crystallin, beta A1a (cryba1a)
  • BA3/A1 Protein
  • BA3A1C Protein
  • beta-A3 Protein
  • Cryb Protein
  • CRYB1 Protein
  • cryba1 Protein
  • CRYBA3 Protein
  • CTRCT10 Protein
  • MGC64403 Protein
  • MGC132102 Protein
  • zgc:92688 Protein

Bezeichner auf Proteinebene für Crystallin, beta A1 Proteine (CRYBA1)

crystallin, beta A4 , crystallin, beta A1 , beta-crystallin A3 , beta-crystallin A1 , beta A1-crystallin , beta A3-crystallin , crystallin, beta A3 , eye lens structural protein , beta-A1-crystallin , beta-A3/A1-crystallin , beta-A3 crystallin , beta-A3/A1 crystalline , betaA3-crystallin , beta A3 crystallin , lens structural protein

GENE ID SPEZIES
380523 Xenopus laevis
468199 Pan troglodytes
716819 Macaca mulatta
100125179 Xenopus (Silurana) tropicalis
100379565 Cavia porcellus
100229047 Taeniopygia guttata
100519211 Sus scrofa
1411 Homo sapiens
12957 Mus musculus
25583 Rattus norvegicus
494645 Xenopus laevis
396499 Gallus gallus
491178 Canis lupus familiaris
282202 Bos taurus
436683 Danio rerio
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