Specification
| Description | Recombinant protein from the full-length sequence of Homo sapiens metallo-beta-lactamase domain containing 2 (MBLAC2) (NM_203406). |
| Organism | Homo sapiens (Human) |
| Expression Host | Human Cells |
| Tag Info | His or DYKDDDDK. Please contact us if you need further information or require specific designed tag. |
| Purity | Greater than 90% by SDS-PAGE gel |
| Uniprot ID | Q68D91 |
| Entry Name | MBLC2_HUMAN |
| Gene Names | MBLAC2 |
| Alternative Gene Names | |
| Alternative Protein Names | Acyl-coenzyme A thioesterase MBLAC2 (Acyl-CoA thioesterase MBLAC2) (EC 3.1.2.2) (Beta-lactamase MBLAC2) (EC 3.5.2.6) (Metallo-beta-lactamase domain-containing protein 2) (Palmitoyl-coenzyme A thioesterase MBLAC2) |
| Application | Antigens, Western, ELISA and other in vitro binding or in vivo functional assays, and protein-protein interaction studies; For research & development use only! |
| Buffer | Purified protein formulated in a sterile solution of PBS buffer, pH7.2, without any preservatives |
| Endotoxin | Endotoxin level is < 0.1 ng/µg of protein (<1EU /µg) |
| Length | 279 |
| Molecular Weight(Da) | 31372 |
| Protein Sequence | (The sequence of expressed protein may have some variation from the sequence shown below. Please contact us for the exact sequence.) MSALEWYAHKSLGDGIFWIQERFYESGNRANIWLVRGSEQDVVIDTGLGLRSLPEYLYSSGLLQDREAKEDAARRPLLAVATHVHFDHSGGLYQFDRVAVHHAEAEALARGDNFETVTWLSDSEVVRTPSPGWRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKILFSGDVVYDGSLIDWLPYSRISDYVGTCERLIELVDRGLVEKVLPGHFNTFGAERLFRLASNYISKAGICHKVSTFAMRSLASLALRVTNSRTSP |
Background
| Function | FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH (PubMed:33219126). Has an acyl-CoA thioesterase activity towards the long chain fatty acyl-CoA thioester palmitoyl-CoA (hexadecanoyl-CoA; C16:0-CoA) (PubMed:33219126). Displays a substrate preference for fatty acyl-CoAs with chain-lengths C12-C18 (PubMed:33219126). Possesses beta-lactamase activity, catalyzing the hydrolysis of penicillin G and nitrocefin (PubMed:31434986). Exhibits no activity towards other beta-lactam antibiotic classes including cephalosporins (cefotaxime) and carbapenems (imipenem) (PubMed:31434986). {ECO:0000269|PubMed:31434986, ECO:0000269|PubMed:33219126}. |
| Pathway | |
| Protein Families | Metallo-beta-lactamase superfamily, Glyoxalase II family |
| Tissue Specificity |
QC Data
| Note | Please contact us for QC Data |
| Product Image (Reference Only) |  |