Mouse Ripk3 - Recombinant Protein | Custom Made-To-Order

Name: Mouse Ripk3 (Receptor-Interacting Serine/Threonine-Protein Kinase 3) - Recombinant Protein
Brand: Beta LifeScience
SKU: BLT-08834P
Price: 545.0 USD
Availability: InStock

Beta Lifescience recombinant protein notice with SDS-PAGE availability in next QC run

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Size

100ug

Quantity

Quantity Pricing

Pack Size	Price (USD)
500 µg	$1,375
1 mg	$2,245

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Product Overview

Product Name	Recombinant Mouse Receptor Interacting Serine Threonine Kinase 3 (RIPK3) Protein
Product Overview	This recombinant mouse Receptor Interacting Serine Threonine Kinase 3 (RIPK3) protein includes amino acids 16-239 of the target gene is expressed in E.coli.The protein is supplied in lyophilized form and formulated in PBS pH 7.4, 0.01% SKL, 5% Trehalose, 1% Mannitolprior to lyophilization.
Target Uniprot Id	Q9QZL0
Recommended Name	Receptor-interacting serine/threonine-protein kinase 3
Gene Name	Ripk3
Synonyms	RIP3; RIP-like protein kinase 3; Receptor-interacting protein 3
Species	Mouse
Predicted Molecular Mass	28kDa
Expression System	E.coli
Expression Range	16-239
Tag	N-6His
Purity	>90%
Formulation	Lyophilized
Buffer	PBS pH 7.4, 0.01% SKL, 5% Trehalose, 1% Mannitol
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
Research Area	Others
Target Function	Serine/threonine-protein kinase that activates necroptosis and apoptosis, two parallel forms of cell death. Necroptosis, a programmed cell death process in response to death-inducing TNF-alpha family members, is triggered by RIPK3 following activation by ZBP1. Activated RIPK3 forms a necrosis-inducing complex and mediates phosphorylation of MLKL, promoting MLKL localization to the plasma membrane and execution of programmed necrosis characterized by calcium influx and plasma membrane damage. In addition to TNF-induced necroptosis, necroptosis can also take place in the nucleus in response to orthomyxoviruses infection: following ZBP1 activation, which senses double-stranded Z-RNA structures, nuclear RIPK3 catalyzes phosphorylation and activation of MLKL, promoting disruption of the nuclear envelope and leakage of cellular DNA into the cytosol. Also regulates apoptosis: apoptosis depends on RIPK1, FADD and CASP8, and is independent of MLKL and RIPK3 kinase activity. Phosphorylates RIPK1: RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation. In some cell types, also able to restrict viral replication by promoting cell death-independent responses. In response to flavivirus infection in neurons, promotes a cell death-independent pathway that restricts viral replication: together with ZBP1, promotes a death-independent transcriptional program that modifies the cellular metabolism via up-regulation expression of the enzyme ACOD1/IRG1 and production of the metabolite itaconate. Itaconate inhibits the activity of succinate dehydrogenase, generating a metabolic state in neurons that suppresses replication of viral genomes. RIPK3 binds to and enhances the activity of three metabolic enzymes: GLUL, GLUD1, and PYGL. These metabolic enzymes may eventually stimulate the tricarboxylic acid cycle and oxidative phosphorylation, which could result in enhanced ROS production.
Subcellular Location	Cytoplasm, cytosol. Nucleus.
Protein Family	Protein kinase superfamily, TKL Ser/Thr protein kinase family
Tissue Specificity	Expressed in embryo and in adult spleen, liver, testis, heart, brain and lung.

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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.