CRYGN

  • Official Full Name

    crystallin, gamma N
  • Overview

    CRYGN belongs to the Crystallins family. Crystallins are divided into alpha, beta and gamma families, and the beta and gamma-crystallins also comprise a superfamily. Crystallins are the major proteins of the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. The CRYGN is differentially regulated after early development, and are involved in cataract formation as a result of either age-related protein degradation or genetic mutation.
Cat.# Product name Source (Host) Species Tag Protein Length Price
CRYGN-3948M Recombinant Mouse CRYGN Protein Mammalian Cell Mouse His
CRYGN-4007C Recombinant Chicken CRYGN Mammalian Cell Chicken His
CRYGN-6944H Recombinant Human Crystallin, Gamma N, His-tagged E.coli Human His 1-182aa
CRYGN-7256HCL Recombinant Human CRYGN 293 Cell Lysate HEK293 Human Non
CRYGN-2004M Recombinant Mouse CRYGN Protein, His (Fc)-Avi-tagged HEK293 Mouse His&Fc&Avi
CRYGN-2004M-B Recombinant Mouse CRYGN Protein Pre-coupled Magnetic Beads HEK293 Mouse

    Involved Pathway

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

    Pathway Name Pathway Related Protein

    Protein Function

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

    Function Related Protein

    Interacting Protein

    CRYGN 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 CRYGN here. Most of them are supplied by our site. Hope this information will be useful for your research of CRYGN.

    Resources

    References

    • Nagaraj, RH; Nahomi, RB; et al. Acetylation of alpha A-crystallin in the human lens: Effects on structure and chaperone function. BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE 1822:120-129(2012).
    • Mailankot, M; Nagaraj, RH; et al. Induction of indoleamine 2,3-dioxygenase by interferon-gamma in human lens epithelial cells: Apoptosis through the formation of 3-hydroxykynurenine. INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY 42:1446-1454(2010).

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