ADAM33 Protein, ADAM metallopeptidase domain 33


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Official Full Name ADAM metallopeptidase domain 33
Background ADAM13 was first described as a protein expressed in somatic mesoderm and neural crest cells, in developing Xenopus embryos. ADAM13 was also found in liver, heart, and intestines from adult Xenopus. ADAM13 may regulate cellular signaling via Src and Src tyrosine kinase. ADAM13 may also act as a cell attachment molecule, by binding integrins through the cysteine rich domain amoung many other roles. A member of the metalloproteinase family containing disintegrin like domains (ADAMs) the functions of ADAM13 are still poorly understood. ADAM13 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, as well as disintegrin, cysteine rich, EFG like, transmembrane and Cytoplasmic domains. ADAM13 has been shown to be proteolytically active, cleaving fibronectin after binding it to the EGF like domain. ADAM13 is also shed from cells in culture, cleaved aminoterminal from the transmembrane domain, and is released into the culture media. Shed ADAM13 is a 52 kD protein, and can form complexes with a2 macroglobulin, suggesting it is a competent protease. Xenopus ADAM13 has greatest homology with human ADAM 33 (51% identical), and is 46% identical with human or mouse ADAM12 or ADAM19. It is still unclear if any of these ADAMs are species orthologs of Xenopus ADAM13, but there are significant differences between the related sequences, suggesting that ADAM13 may be a unique protein. The full length Xenopus ADAM13 sequence codes for a 914 amino acid protein. Predicted mass is 99.749 kD, but glycosylation and cyteine rich regions give Xenopus ADAM13 an apparent MW of 120 kD unprocessed, and 97 kD processed forms, on reduced SDS PAGE gels. ADAM13 contains a putative furin cleavage site, suggesting that a prohormone convertase cleaves the propeptide domain away from the catalytic domain.
Synonyms adam13; ADAM metallopeptidase domain 33; x-adam 13; a disintegrin and metalloprotease domain 13;
    • Species :
    • Chicken
    • Human
    • Source :
    • E.coli
    • HEK293
    • Mammalian Cell
    • Wheat Germ
    • Tag :
    • GST
    • His
    • T7
    • N/A
    Species Cat.# Product name Source (Host) Tag Protein Length Price
    Human ADAM33-1484H Recombinant Human ADAM33 protein, His & T7-tagged E.coli His/T7
    Human ADAM33-289H Recombinant Human ADAM33 Protein, GST-tagged Wheat Germ GST
    Human ADAM33-290H Recombinant Human ADAM33 Protein, GST-tagged Wheat Germ GST
    Human ADAM33-9033HCL Recombinant Human ADAM33 293 Cell Lysate HEK293 N/A
    Chicken ADAM33-3673C Recombinant Chicken ADAM33 Mammalian Cell His

    ADAM33 involved in several pathways and played different roles in them. We selected most pathways ADAM33 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with ADAM33 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein

    ADAM33 has several biochemical functions, for example, metalloendopeptidase activity, protein binding, zinc ion binding. Some of the functions are cooperated with other proteins, some of the functions could acted by ADAM33 itself. We selected most functions ADAM33 had, and list some proteins which have the same functions with ADAM33. You can find most of the proteins on our site.

    Function Related Protein
    metalloendopeptidase activity UQCRC2B; ADAMTSL5; MMP19; ADAM10B; UQCRC2; MBTPS2; MMP7; ADAMTS13; HE1B; ADAM23
    protein binding SHISA5; ARL2BP; MAGI1; NAP1L1; TTC35; TRAPPC3; SLC14A2; C11orf46; SPRR2A; KIAA1217
    zinc ion binding CNBPA; RORA; GATA2A; ATXN7L3; NR5A2; RNF180; RXRGA; NRD1B; DIDO1; TGFB1I1

    ADAM33 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 ADAM33 here. Most of them are supplied by our site. Hope this information will be useful for your research of ADAM33.


    Holloway, JW; Laxton, RC; et al. ADAM33 expression in atherosclerotic lesions and relationship of ADAM33 gene variation with atherosclerosis. ATHEROSCLEROSIS 211:224-230(2010).
    Erbek, SS; Erinanc, H; et al. Expression of a disintegrin and metalloproteinase 33 protein in nasal polyposis: An immunohistochemical study. AMERICAN JOURNAL OF RHINOLOGY & ALLERGY 24:E79-E82(2010).

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