ISLR2

  • Official Full Name

    immunoglobulin superfamily containing leucine-rich repeat 2
  • Synonyms

    ISLR2;immunoglobulin superfamily containing leucine-rich repeat 2;immunoglobulin superfamily containing leucine-rich repeat protein 2;leucine-rich repeat domain and immunoglobulin domain containing axon extension protein;leucine-rich repeat domain and
Cat.# Product name Source (Host) Species Tag Protein Length Price
ISLR2-2190Z Recombinant Zebrafish ISLR2 Mammalian Cells Zebrafish His
ISLR2-3459C Recombinant Chicken ISLR2 Mammalian Cells Chicken His

    Involved Pathway

    ISLR2 involved in several pathways and played different roles in them. We selected most pathways ISLR2 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with ISLR2 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

    ISLR2 has several biochemical functions, for example, . Some of the functions are cooperated with other proteins, some of the functions could acted by ISLR2 itself. We selected most functions ISLR2 had, and list some proteins which have the same functions with ISLR2. You can find most of the proteins on our site.

    Function Related Protein

    Interacting Protein

    ISLR2 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 ISLR2 here. Most of them are supplied by our site. Hope this information will be useful for your research of ISLR2.

    Resources

    References

    • Soudi, M; Zamocky, M; et al. Molecular Evolution, Structure, and Function of Peroxidasins. CHEMISTRY & BIODIVERSITY 9:1776-1793(2012).
    • Wu, MH; Huang, C; et al. LRRC4, a putative tumor suppressor gene, requires a functional leucine-rich repeat cassette domain to inhibit proliferation of glioma cells in vitro by modulating the extracellular signal-regulated kinase/protein kinase B/nuclear factor-kappa B pathway. MOLECULAR BIOLOGY OF THE CELL 17:3534-3542(2006).

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