Recombinant Human MAD Protein (Flag Tag)

Name: Recombinant Human MAD Protein (Flag Tag)
Brand: Beta LifeScience
SKU: BL-110PC
Availability: InStock

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Tag	Flag
Host Species	Human
Accession	NM_002357.
Synonym	MXD1; MAD1; MGC104659.
Background	MAX dimerization protein belongs to a subfamily of MAX-interacting proteins. This protein competes with MYC for binding to MAX to form a sequence-specific DNA-binding complex, acting as a transcriptional repressor (while MYC appears to function as an activator) and is a candidate tumor suppressor. Both Myc and Mad, as well as the more recently described Mnt and Mga proteins, form heterodimers with Max, permitting binding to specific DNA sequences. These DNA-bound heterodimers recruit coactivator or corepressor complexes that generate alterations in chromatin structure, which in turn modulate transcription (1). The wild-type c-Myc and c-Myc/MadBR proteins have indistinguishable biological activity and target gene recognition in vivo (2).
Description	Recombinant Human MAD Protein was expressed in E.coli. This protein is fused with a Flag tag and purified using our unique purification methods.
Source	E.coli
AA Sequence	MAAAVRMNIQ MLLEAADYLE RREREAEHGY ASMLPYNNKD RDALKRRNKS KKNNSSSRST HNEMEKNRRA HLRLCLEKLK GLVPLGPESS RHTTLSLLTK AKLHIKKLED CDRKAVHQID QLQREQRHLK RQLEKLGIER IRMDSIGSTV SSERSDSDRE EIDVDVESTD YLTGDLDWSS SSVSDSDERG SMQSLGSDEG YSSTSIKRIK LQDSHKACLG L
Molecular Weight	26.6 kDa.
Purity	>90% purity by SDS-PAGE
Endotoxin	<0.1 ng/µg (1 EU/µg) as determined by LAL test.
Formulation	Recombinant Human MAD Protein is supplied in 20mM Tris-HCl pH7.9,100mM NaCl, 0.2mM EDTA, 1mM DTT and 20% glycerol.
Usage	For Research Use Only
Storage	Stored the protein at -70°C before use. Avoid repeated freeze thaw cycles.

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.