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Crystallin, beta A1 Proteins (CRYBA1)

Crystallins are the dominant structural components of the vertebrate eye lens.. Additionally we are shipping Crystallin, beta A1 Antibodies (39) and Crystallin, beta A1 Kits (2) and many more products for this protein.

list all proteins Gene Name GeneID UniProt
CRYBA1 1411 P05813
CRYBA1 12957  
CRYBA1 25583 P14881
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Top Crystallin, beta A1 Proteins at antibodies-online.com

Showing 7 out of 11 products:

Catalog No. Origin Source Conjugate Images Quantity Supplier Delivery Price Details
HOST_Escherichia coli (E. coli) Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 29 to 34 Days
$4,331.68
Details
HOST_Escherichia coli (E. coli) Mouse His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 29 to 34 Days
$4,331.68
Details
HOST_Wheat germ Human GST tag 10 μg Log in to see 9 Days
$405.71
Details
Yeast Chicken His tag   1 mg Log in to see 56 to 66 Days
$2,531.83
Details
Yeast Rat His tag   1 mg Log in to see 56 to 66 Days
$2,531.83
Details
Yeast Cow His tag   1 mg Log in to see 56 to 66 Days
$2,531.83
Details
HOST_Human Human Un-conjugated   20 μg Log in to see 9 to 11 Days
$785.40
Details

CRYBA1 Proteins by Origin and Source

Origin Expressed in Conjugate
Human , ,
,
Mouse (Murine)

Rat (Rattus)

More Proteins for Crystallin, beta A1 (CRYBA1) Interaction Partners

Human Crystallin, beta A1 (CRYBA1) interaction partners

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

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

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

  4. 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.

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

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

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

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

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

  10. The DeltaG91 mutation in CRYBA3/A1 is associated with an autosomal dominant congenital nuclear lactescent cataract

Mouse (Murine) Crystallin, beta A1 (CRYBA1) interaction partners

  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 (show ATP6V1H Proteins).

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

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

  5. p53 (show TP53 Proteins) 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) interaction partners

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

Crystallin, beta A1 (CRYBA1) Protein Profile

Protein Summary

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

Gene names and symbols associated with Crystallin, beta A1 Proteins (CRYBA1)

  • crystallin, beta A4 (cryba4)
  • crystallin, beta A1 (CRYBA1)
  • crystallin, beta A1 (cryba1)
  • crystallin, beta A1 (Cryba1)
  • crystallin, beta A1 (LOC100229047)
  • beta-crystallin A3-like (LOC100519211)
  • 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

Protein level used designations for Crystallin, beta A1 Proteins (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 SPECIES
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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