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Official Full Name CASK interacting protein 1
Synonyms CASKIN1;CASK interacting protein 1;20879;ENSG00000167971;ANKS5A;16p13.3;caskin-1;caskin-1;CASK-interacting protein 1;
    • Species :
    • Human
    • Mouse
    • Source :
    • Mammalian Cell
    • Tag :
    • His
    Species Cat.# Product name Source (Host) Tag Protein Length Price
    Human CASKIN1-1126H Recombinant Human CASKIN1 Mammalian Cell His
    Mouse CASKIN1-2746M Recombinant Mouse CASKIN1 Protein Mammalian Cell His

    caskin1 involved in several pathways and played different roles in them. We selected most pathways caskin1 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with caskin1 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein

    caskin1 has several biochemical functions, for example, protein binding, protein domain specific binding. Some of the functions are cooperated with other proteins, some of the functions could acted by caskin1 itself. We selected most functions caskin1 had, and list some proteins which have the same functions with caskin1. You can find most of the proteins on our site.

    Function Related Protein
    protein binding ARMCX1; C1D; MAPK7; EIF2AK3; Fzd4; S100A9; SLC22A17; AXIN2; RAB8A; ARL2BP
    protein domain specific binding YWHAZ; ARFIP2B; STMN3; GUSB; STX1A; HAND2; MPP5; DRD3; MYO1D; WNT3

    caskin1 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 caskin1 here. Most of them are supplied by our site. Hope this information will be useful for your research of caskin1.

    CASK; npm_alk

    Anjum, R; Ayoubian, H; et al. Differential synaptic distribution of the scaffold proteins Cask and Caskin1 in the bovine retina. MOLECULAR AND CELLULAR NEUROSCIENCE 62:19-29(2014).
    Pesti, S; Balazs, A; et al. Complex formation of EphB1/Nck/Caskin1 leads to tyrosine phosphorylation and structural changes of the Caskin1 SH3 domain. CELL COMMUNICATION AND SIGNALING 10:-(2012).

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