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Official Full Name crystallin, alpha A
Background Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Defects in this gene cause autosomal dominant congenital cataract (ADCC).
Synonyms CRYAA; crystallin, alpha A; CRYA1; alpha-crystallin A chain; HSPB4; Heat shock protein beta 4; short form; Acry 1; Acry-1; Alpha crystallin A chain; CRYA 1; CRYAA_HUMAN; Crystallin Alpha 1; Crystallin alpha A; Heat shock protein beta-4; HSPB 4; Zonular Central Nuclear Cataract; OTTHUMP00000109430; crystallin, alpha-1; human alphaA-crystallin (CRYA1)
    • Species :
    • Chicken
    • Human
    • Mouse
    • Rat
    • Zebrafish
    • Source :
    • E.coli
    • E.Coli or Yeast
    • HEK293
    • HEK293T
    • Mammalian Cell
    • Wheat Germ
    • Tag :
    • GST
    • His
    • Myc/DDK
    • N/A
    Species Cat.# Product name Source (Host) Tag Protein Length Price
    Human CRYAA-1925H Recombinant Human CRYAA Protein, GST-tagged Wheat Germ GST
    Human CRYAA-26676TH Recombinant Human CRYAA E.coli N/A
    Human CRYAA-26991TH Recombinant Human CRYAA, His-tagged E.coli His
    Human CRYAA-2879H Recombinant Human CRYAA Protein, Myc/DDK-tagged, C13 and N15-labeled HEK293T Myc/DDK
    Human CRYAA-309H Recombinant Human Crystallin Alpha A E.coli N/A
    Human CRYAA-7267HCL Recombinant Human CRYAA 293 Cell Lysate HEK293 N/A
    Mouse Cryaa-2325M Recombinant Mouse Cryaa Protein, Myc/DDK-tagged HEK293T Myc/DDK
    Mouse CRYAA-3933M Recombinant Mouse CRYAA Protein Mammalian Cell His
    Mouse Cryaa-7175M Recombinant Mouse Cryaa Protein E.coli
    Rat Cryaa-3344R Recombinant Rat Cryaa, His-tagged E.Coli or Yeast His
    Chicken CRYAA-2495C Recombinant Chicken CRYAA Mammalian Cell His
    Zebrafish CRYAA-9417Z Recombinant Zebrafish CRYAA Mammalian Cell His

    CRYAA involved in several pathways and played different roles in them. We selected most pathways CRYAA participated on our site, such as Protein processing in endoplasmic reticulum, which may be useful for your reference. Also, other proteins which involved in the same pathway with CRYAA were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein
    Protein processing in endoplasmic reticulum MAPK8B; BCL2A; UBQLNL; SEC61A1; SSR2; STT3A; CUL1B; UBE2J2; VIMP; ERO1LB

    CRYAA has several biochemical functions, for example, identical protein binding, metal ion binding, protein binding. Some of the functions are cooperated with other proteins, some of the functions could acted by CRYAA itself. We selected most functions CRYAA had, and list some proteins which have the same functions with CRYAA. You can find most of the proteins on our site.

    Function Related Protein
    identical protein binding GPSM2; ACPP; C1QTNF9; C; RASSF1; OAT; ACTG1; IFI203; ZBTB16; HAND1
    metal ion binding CYP2AA7; MT1; KSR2; ZGPAT; RCVRNA; ZNF726; TPP1; GNE; HAGH; ZNF691
    protein binding MAPK3; MESDC1; NUMA1; LCK; UBQLN4; NGLY1; ZNF16; CCDC123; RRM2B; SP2
    structural constituent of eye lens CRYBB3; BFSP1; CRYBA2; LIM2.3; CRYBB2; BFSP2; ASL1; CRYGN2; CRYGB; ASL2
    unfolded protein binding CALR; GRPEL1; TAPBP; CLPXA; CALR3; MKKS; TTC1; LMAN1; HSP90AB1; DNAJB11

    CRYAA has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with CRYAA here. Most of them are supplied by our site. Hope this information will be useful for your research of CRYAA.


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