MBLAC2 Protein, metallo-beta-lactamase domain containing 2


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Official Full Name metallo-beta-lactamase domain containing 2
Synonyms MBLAC2;metallo-beta-lactamase domain containing 2;33711;ENSG00000176055;5q14.3;MGC46734, DKFZp686P15118;metallo-beta-lactamase domain-containing protein 2;metallo-beta-lactamase domain-containing protein 2;
    • Species :
    • Chicken
    • Human
    • Rhesus Macaque
    • Zebrafish
    • Source :
    • HEK293
    • Mammalian Cell
    • Tag :
    • His
    • N/A
    Species Cat.# Product name Source (Host) Tag Protein Length Price
    Human MBLAC2-4442HCL Recombinant Human MBLAC2 293 Cell Lysate HEK293 N/A
    Rhesus Macaque MBLAC2-2695R Recombinant Rhesus monkey MBLAC2 Protein, His-tagged Mammalian Cell His
    Chicken MBLAC2-3246C Recombinant Chicken MBLAC2 Mammalian Cell His
    Zebrafish MBLAC2-6659Z Recombinant Zebrafish MBLAC2 Mammalian Cell His

    MBLAC2 involved in several pathways and played different roles in them. We selected most pathways MBLAC2 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with MBLAC2 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein

    MBLAC2 has several biochemical functions, for example, hydrolase activity, metal ion binding, molecular_function. Some of the functions are cooperated with other proteins, some of the functions could acted by MBLAC2 itself. We selected most functions MBLAC2 had, and list some proteins which have the same functions with MBLAC2. You can find most of the proteins on our site.

    Function Related Protein
    hydrolase activity BLM; HDHD3; YDJC; RAG1; HINT3; KLK1B3; MCPT8; IHHA; ATP1A1A.1; SHHA
    metal ion binding ADCY8; AMY2B; GM5136; ATP1A3; CYP2P9; NFS1; AIFM3; GNAI3; ZC3H15; BA1
    molecular_function LRCH2; ADPRM; CDR2; CCDC6A; MBOAT1; PHF16; SAGB; ZSWIM7; DGCR6; C11orf58

    MBLAC2 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 MBLAC2 here. Most of them are supplied by our site. Hope this information will be useful for your research of MBLAC2.

    Makris, Thomas M.; Knoot, Cory J.; et al. Structure of a Dinuclear Iron Cluster-Containing beta-Hydroxylase Active in Antibiotic Biosynthesis. BIOCHEMISTRY 52:6662-6671(2013).
    Guo, Yu; Wang, Jing; et al. A structural view of the antibiotic degradation enzyme NDM-1 from a superbug. PROTEIN & CELL 2:384-394(2011).

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