Human TGM2 - Recombinant Protein | Custom Made-To-Order

Name: Human TGM2 (Protein-Glutamine Gamma-Glutamyltransferase 2) - Recombinant Protein
Brand: Beta LifeScience
SKU: BLT-03024P
Price: 445.0 USD
Availability: InStock

SDS-PAGE analysis of Human TGM2 (Protein-Glutamine Gamma-Glutamyltransferase 2) - Recombinant Protein, CAT# BLT-03024P, showing >85% purity under 15% SDS-PAGE (Reduced)

Price Save $150

Size

100ug

Quantity

Quantity Pricing

Pack Size	Price (USD)
500 µg	$1,030 (Fall Promotion)
1 mg	$1,870 (Fall Promotion)

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Product Overview

Product Name	Recombinant Human Transglutaminase 2 (TGM2) Protein
Product Overview	This recombinant human Transglutaminase 2 (TGM2) protein includes amino acids 1-687aa of the target gene is expressed in E.coli.The protein is supplied in lyophilized form and formulated in phosphate buffered saline (pH7.4) containing 0.01% sarcosyl, 5% trehaloseprior to lyophilization.
Target Uniprot Id	P21980
Recommended Name	Protein-glutamine gamma-glutamyltransferase 2
Gene Name	TGM2
Synonyms	Protein-glutamine gamma-glutamyltransferase 2 isoform a, Transglutaminase 2, G-ALPHA-h, GNAH, HEL-S-
Species	Human
Predicted Molecular Mass	100 kDa
Expression System	E.coli
Expression Range	1-687aa
Tag	N-6His
Purity	>85%
Formulation	Lyophilized
Buffer	Phosphate buffered saline (pH7.4) containing 0.01% sarcosyl, 5%Trehalose
Storage Condition	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Reconstitution Instruction	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Applications	Positive Control; Immunogen; SDS-PAGE; WB
Target 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.; Has cytotoxic activity: is able to induce apoptosis independently of its acyltransferase activity.
Subcellular Location	Cytoplasm, cytosol. Nucleus. Chromosome. Secreted, extracellular space, extracellular matrix. Cell membrane. Mitochondrion.; [Isoform 2]: Cytoplasm, perinuclear region.
Protein Family	Transglutaminase superfamily, Transglutaminase family

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FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.