LRRC38

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LRRC38

Official Full Name leucine rich repeat containing 38
Synonyms LRRC38; leucine rich repeat containing 38; leucine-rich repeat-containing protein 38; RP4-597A16.1
    • Species :
    • Mouse
    • Source :
    • Mammalian Cell
    • Tag :
    • His
    Species Cat.# Product name Source (Host) Tag Protein Length Price
    Mouse LRRC38-9270M Recombinant Mouse LRRC38 Protein Mammalian Cell His

    LRRC38 involved in several pathways and played different roles in them. We selected most pathways LRRC38 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with LRRC38 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein

    LRRC38 has several biochemical functions, for example, molecular_function. Some of the functions are cooperated with other proteins, some of the functions could acted by LRRC38 itself. We selected most functions LRRC38 had, and list some proteins which have the same functions with LRRC38. You can find most of the proteins on our site.

    Function Related Protein
    molecular_function SSUH2.3; MORC4; AP1S3; V1RD19; GTSE1; BCO1L; ITFG3; TIGD3; ANKRD13B; GPR52

    LRRC38 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 LRRC38 here. Most of them are supplied by our site. Hope this information will be useful for your research of LRRC38.

    Shimizu, A; Matsushita, T; et al. Identification of the amino acid residues of the platelet glycoprotein Ib (GPIb) essential for the von Willebrand factor binding by clustered charged-to-alanine scanning mutagenesis. JOURNAL OF BIOLOGICAL CHEMISTRY 279:16285-16294(2004).
    AfsharKharghan, V; Lopez, JA; et al. Bernard-Soulier syndrome caused by a dinucleotide deletion and reading frameshift in the region encoding the glycoprotein Ib alpha transmembrane domain. BLOOD 90:2634-2643(1997).
    Remy, JJ; Couture, L; et al. Mapping of HCG-receptor complexes. MOLECULAR AND CELLULAR ENDOCRINOLOGY 125:79-91(1996).
    MAKHOV, AM; HANNAH, JH; et al. FILAMENTOUS HEMAGGLUTININ OF BORDETELLA-PERTUSSIS - A BACTERIAL ADHESIN FORMED AS A 50-NM MONOMERIC RIGID-ROD BASED ON A 19-RESIDUE REPEAT MOTIF RICH IN BETA-STRANDS AND BETA-TURNS. JOURNAL OF MOLECULAR BIOLOGY 241:110-124(1994).

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