Mouse Mdm2 - Recombinant Protein | Custom Made-To-Order

Name: Mouse Mdm2 (E3 Ubiquitin-Protein Ligase Mdm2) - Recombinant Protein
Brand: Beta LifeScience
SKU: BLT-07180P
Price: 445.0 USD
Availability: InStock

SDS-PAGE analysis of Mouse Mdm2 (E3 Ubiquitin-Protein Ligase Mdm2) - Recombinant Protein, CAT# BLT-07180P, showing >95% 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 Mouse Mdm2 p53 Binding Homolog (MDM2) Protein
Product Overview	This recombinant mouse Mdm2 p53 Binding Homolog (MDM2) protein includes amino acids 1-310aa of the target gene is expressed in E.coli.The protein is supplied in liquid or lyophilized powder form and formulated in PBSprior to lyophilization.
Target Uniprot Id	P23804
Recommended Name	E3 ubiquitin-protein ligase Mdm2
Gene Name	Mdm2
Synonyms	HDMX; hdm2; Mouse Double Minute 2,Human Homolog Of p53-Binding Protein; Oncoprotein Mdm2
Species	Mouse
Predicted Molecular Mass	48 kDa
Expression System	E.coli
Expression Range	1-310aa
Tag	N-6His
Purity	>95%
Formulation	Liquid or Lyophilized powder
Buffer	PBS
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	E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome. Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Also acts as a ubiquitin ligase E3 toward itself, ARRB1 and ARBB2. Permits the nuclear export of p53/TP53. Promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein. Inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation. Component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in stabilizing p53/TP53. Also component of the TRIM28/KAP1-ERBB4-MDM2 complex which links growth factor and DNA damage response pathways. Mediates ubiquitination and subsequent proteasome degradation of DYRK2 in nucleus. Ubiquitinates IGF1R and SNAI1 and promotes them to proteasomal degradation. Ubiquitinates DCX, leading to DCX degradation and reduction of the dendritic spine density of olfactory bulb granule cells. Ubiquitinates DLG4, leading to proteasomal degradation of DLG4 which is required for AMPA receptor endocytosis. Negatively regulates NDUFS1, leading to decreased mitochondrial respiration, marked oxidative stress, and commitment to the mitochondrial pathway of apoptosis. Binds NDUFS1 leading to its cytosolic retention rather than mitochondrial localization resulting in decreased supercomplex assembly (interactions between complex I and complex III), decreased complex I activity, ROS production, and apoptosis.
Subcellular Location	Nucleus, nucleoplasm. Cytoplasm. Nucleus, nucleolus. Nucleus.
Protein Family	MDM2/MDM4 family
Tissue Specificity	Ubiquitously expressed at low-level throughout embryo development and in adult tissues. MDM2-p90 is much more abundant than MDM2-p76 in testis, brain, heart, and kidney, but in the thymus, spleen, and intestine, the levels of the MDM2 proteins are roughly

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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.