LRRC19 Protein, leucine rich repeat containing 19

LRRC19

Home / Products / LRRC19

LRRC19

Official Full Name leucine rich repeat containing 19
Synonyms LRRC19; leucine rich repeat containing 19; leucine-rich repeat-containing protein 19; FLJ21302
    • Species :
    • Human
    • Mouse
    • Source :
    • Mammalian Cell
    • Wheat Germ
    • Tag :
    • His
    • N/A
    Species Cat.# Product name Source (Host) Tag Protein Length Price
    Human LRRC19-4681H Recombinant Human LRRC19 Protein Wheat Germ N/A
    Mouse LRRC19-9254M Recombinant Mouse LRRC19 Protein Mammalian Cell His

    LRRC19 involved in several pathways and played different roles in them. We selected most pathways LRRC19 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with LRRC19 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein

    LRRC19 has several biochemical functions, for example, molecular_function. Some of the functions are cooperated with other proteins, some of the functions could acted by LRRC19 itself. We selected most functions LRRC19 had, and list some proteins which have the same functions with LRRC19. You can find most of the proteins on our site.

    Function Related Protein
    molecular_function TMX2; TRANK1; TMEM89; RGAG4; LHFPL2A; ZNF697; CNRIP1A; SIPA1L1; IFFO2; ARPC5L

    LRRC19 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 LRRC19 here. Most of them are supplied by our site. Hope this information will be useful for your research of LRRC19.

    Sardar, PS; Maity, SS; et al. Characterization of the tryptophan residues of human placental ribonuclease inhibitor and its complex with bovine pancreatic ribonuclease A by steady-state and time-resolved emission spectroscopy. JOURNAL OF PHYSICAL CHEMISTRY B 110:21349-21356(2006).
    Heathfield, TF; Onnerfjord, P; et al. Cleavage of fibromodulin in cartilage explants involves removal of the N-terminal tyrosine sulfate-rich region by proteolysis at a site that is sensitive to matrix metalloproteinase-13. JOURNAL OF BIOLOGICAL CHEMISTRY 279:6286-6295(2004).

    Related Services & Products

    Apply For A Coupon

    $50 OFF Your First Purchase

    Apply For a Coupon

    Enter your email here to subscribe.

    creative biomart inc.

    Easy access to products and services you need from our library via powerful searching tools.

    Follow Us

    Copyright © 2007 – 2020 Creative BioMart. All Rights Reserved. Terms and Conditions | Privacy Policy