Mouse TGM2 protein (Recombinant) (N-His) (STJP009798)
SPECIFICATIONS
HostE.coli
ImmunogenMus musculus (Mouse)
General Information
| Short Description | Recombinant-Mouse TGM2-N-His protein was developed from e.coli for the region N-His. For use in research applications. |
| Applications | ELISA/Immunogen/SDS-PAGE/WB |
| Host | E.coli |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Dilution Range | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Formulation | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
| Storage Instruction | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at-20 to-80°C for twelve months from the date of receipt. |
Target Information
| Gene Symbol | Tgm2 |
| Gene ID | 21817 |
| Uniprot ID | TGM2_MOUSE |
| Immunogen | Mus musculus (Mouse) |
| Immunogen Region | Asp151-Ala686 |
Additional Info
| Function | Calcium-dependent acyltransferase that catalyzes the formation of covalent bonds between peptide-bound glutamine and various primary amines, such as gamma-amino group of peptide-bound lysine, or mono- and polyamines, thereby producing cross-linked or aminated proteins, respectively. Involved in many biological processes, such as bone development, angiogenesis, wound healing, cellular differentiation, chromatin modification and apoptosis. Acts as a protein-glutamine gamma-glutamyltransferase by mediating the cross-linking of proteins, such as ACO2, HSPB6, FN1, HMGB1, RAP1GDS1, SLC25A4/ANT1, SPP1 and WDR54. Under physiological conditions, the protein cross-linking activity is inhibited by GTP.inhibition is relieved by Ca(2+) in response to various stresses. When secreted, catalyzes cross-linking of proteins of the extracellular matrix, such as FN1 and SPP1 resulting in the formation of scaffolds. Plays a key role during apoptosis, both by (1) promoting the cross-linking of cytoskeletal proteins resulting in condensation of the cytoplasm, and by (2) mediating cross-linking proteins of the extracellular matrix, resulting in the irreversible formation of scaffolds that stabilize the integrity of the dying cells before their clearance by phagocytosis, thereby preventing the leakage of harmful intracellular components. In addition to protein cross-linking, can use different monoamine substrates to catalyze a vast array of protein post-translational modifications: mediates aminylation of serotonin, dopamine, noradrenaline or histamine into glutamine residues of target proteins to generate protein serotonylation, dopaminylation, noradrenalinylation or histaminylation, respectively. Mediates protein serotonylation of small GTPases during activation and aggregation of platelets, leading to constitutive activation of these GTPases. Plays a key role in chromatin organization by mediating serotonylation and dopaminylation of histone H3. Catalyzes serotonylation of 'Gln-5' of histone H3 (H3Q5ser) during serotonergic neuron differentiation, thereby facilitating transcription. Acts as a mediator of neurotransmission-independent role of nuclear dopamine in ventral tegmental area (VTA) neurons: catalyzes dopaminylation of 'Gln-5' of histone H3 (H3Q5dop), thereby regulating relapse-related transcriptional plasticity in the reward system. Regulates vein remodeling by mediating serotonylation and subsequent inactivation of ATP2A2/SERCA2. Also acts as a protein deamidase by mediating the side chain deamidation of specific glutamine residues of proteins to glutamate. Catalyzes specific deamidation of protein gliadin, a component of wheat gluten in the diet. May also act as an isopeptidase cleaving the previously formed cross-links. Also able to participate in signaling pathways independently of its acyltransferase activity: acts as a signal transducer in alpha-1 adrenergic receptor-mediated stimulation of phospholipase C-delta (PLCD) activity and is required for coupling alpha-1 adrenergic agonists to the stimulation of phosphoinositide lipid metabolism. |
| Protein Name | Protein-Glutamine Gamma-Glutamyltransferase 2Isopeptidase Tgm2Protein-Glutamine Deamidase Tgm2Protein-Glutamine Dopaminyltransferase Tgm2Protein-Glutamine Histaminyltransferase Tgm2Protein-Glutamine Noradrenalinyltransferase Tgm2Protein-Glutamine Serotonyltransferase Tgm2Tissue TransglutaminaseTtgTransglutaminase IiTgase IiTransglutaminase-2Tg2Tgase-2Tgase2 |
| Database Links | |
| Cellular Localisation | CytoplasmCytosolNucleusChromosomeSecretedExtracellular SpaceExtracellular MatrixCell MembraneMitochondrionMainly Localizes To The CytosolPresent At Much Lower Level In The Nucleus And ChromatinAlso Secreted Via A Non-Classical Secretion Pathway To The Extracellular Matrix |
| Alternative Protein Names | Protein-Glutamine Gamma-Glutamyltransferase 2 proteinIsopeptidase Tgm2 proteinProtein-Glutamine Deamidase Tgm2 proteinProtein-Glutamine Dopaminyltransferase Tgm2 proteinProtein-Glutamine Histaminyltransferase Tgm2 proteinProtein-Glutamine Noradrenalinyltransferase Tgm2 proteinProtein-Glutamine Serotonyltransferase Tgm2 proteinTissue Transglutaminase proteinTtg proteinTransglutaminase Ii proteinTgase Ii proteinTransglutaminase-2 proteinTg2 proteinTgase-2 proteinTgase2 proteinTgm2 protein |
Information sourced from Uniprot.org