Recombinant Human Mitotic Spindle Assembly Checkpoint Protein Mad2A (MAD2L1) Protein (His-SUMO)

Name: Recombinant Human Mitotic Spindle Assembly Checkpoint Protein Mad2A (MAD2L1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-03059P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Mitotic Spindle Assembly Checkpoint Protein Mad2A (MAD2L1) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q13257
Target Symbol	MAD2L1
Synonyms	HsMAD2; MAD 2; MAD2 like 1; MAD2 mitotic arrest deficient like 1; MAD2-like protein 1; Mad2l1; MD2L1_HUMAN; Mitotic arrest deficient 2-like protein 1; Mitotic spindle assembly checkpoint protein MAD2A; REV7
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	ALQLSREQGITLRGSAEIVAEFFSFGINSILYQRGIYPSETFTRVQKYGLTLLVTTDLELIKYLNNVVEQLKDWLYKCSVQKLVVVISNIESGEVLERWQFDIECDKTAKDDSAPREKSQKAIQDEIRSVIRQITATVTFLPLLEVSCSFDLLIYTDKDLVVPEKWEESGPQFITNSEEVRLRSFTTTIHKVNSMVAYKIPVND
Expression Range	2-205aa
Protein Length	Full Length of Mature Protein
Mol. Weight	39.4kDa
Research Area	Cell Biology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	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%.
Storage	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.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. In the closed conformation (C-MAD2) forms a heterotetrameric complex with MAD1L1 at unattached kinetochores during prometaphase, the complex recruits open conformation molecules of MAD2L1 (O-MAD2) and then promotes the conversion of O-MAD2 to C-MAD2. Required for the execution of the mitotic checkpoint which monitors the process of kinetochore-spindle attachment and inhibits the activity of the anaphase promoting complex by sequestering CDC20 until all chromosomes are aligned at the metaphase plate.
Subcellular Location	Nucleus. Chromosome, centromere, kinetochore. Cytoplasm. Cytoplasm, cytoskeleton, spindle pole.
Protein Families	MAD2 family
Database References	HGNC: 6763 OMIM: 601467 KEGG: hsa:4085 STRING: 9606.ENSP00000296509 UniGene: PMID: 30346937 we demonstrate that the CDC20-MAD2 complex could also be formed independently of the SAC. Moreover, in prolonged arrest caused by nocodazole treatment, the overall levels of the CDC20-MAD2 complex are gradually, but significantly, reduced and this is associated with lower levels of cyclin B1, which brings a new insight into the mechanism of mitotic "slippage" of the arrested cells. PMID: 28112196 MAD2-p31(comet) axis may serve as a potential therapeutic target for glioma. PMID: 29408509 These results identify an unexpected dependency on TRIP13 in cells overexpressing Mad2. PMID: 28564602 this study shows that MAD2L1 is a prognostic biomarker for lung adenocarcinoma PMID: 27835911 MiR-200c-5p suppresses proliferation and metastasis of human hepatocellular carcinoma by suppressing MAD2L1 expression. PMID: 28609841 Low MAD2L1 expression is associated with Chromophobe Renal Cell Carcinomas. PMID: 28807937 TRAP1 is relevant in the control of key cell cycle regulators in tumor cells. TRAP1/TBP7 quality control of CDK1 and MAD2 contributes mechanistically to the regulation of mitotic entry and transit. PMID: 28678347 Thes authors show that p31(comet) binding to the TRIP13 N-terminal domain positions the disordered MAD2 N-terminus for engagement by the TRIP13 "pore loops", which then unfold MAD2 in the presence of ATP. PMID: 28659378 catalytic activation of the spindle assembly checkpoint depends on regulated protein-protein interactions that accelerate the spontaneous but rate-limiting conversion of MAD2 required for mitotic checkpoint complex assembly PMID: 28102834 in addition to its role in checkpoint signaling, MAD2 ensures chromosome stability through the regulation of AURORA B. PMID: 27341405 Overexpression of MAD2gamma may play a role in checkpoint disruption and is associated with resistance to cisplatin-based chemotherapy in testicular germ cell tumors. PMID: 27315568 Aberrant Mad2 expression was associated with cell proliferation and genetic instability, which may contribute to the carcinogenesis of PGI-DLBCL. Mad2 overexpression indicated a poor DFS. PMID: 27077767 interactions between Mad2 and H3K4 regulate resolution of the spindle assembly checkpoint by limiting closed Mad2 availability for Cdc20 inhibition. PMID: 27198228 we showed that BubR1 and Mad2 are overexpressed in oral squamous cell carcinoma cell lines and linked such overexpression to attenuated spindle assembly checkpoint activity. PMID: 25754611 Studied the folding/unfolding process of the open and closed conformers of human Mad2. PMID: 26489879 MAD1L1 Arg558His and MAD2L1 Leu84Met interaction with smoking increase the risk of colorectal cancer PMID: 26183163 p31comet-induced cell death is mediated by interactions with Mad2 PMID: 26544187 MAD2L1 and BUB1 may play important roles in breast cancer progression, and measuring the expression of these genes may assist the prediction of breast cancer prognosis. PMID: 26287798 We also show that replication perturbations result in relocalization of MAD1/MAD2 in human cells, suggesting that the role of SAC in DNA repair is conserved. PMID: 25898113 Data indicate the structure of the intermediate conformer of the multistate checkpoint protein mitotic arrest deficient 2 (Mad2) protein. PMID: 26305957 WT1 has a role in interacting MAD2 and regulating mitotic checkpoint function PMID: 25232865 In conclusion, the results presented here suggest that Mad2 and BubR1 could be used as prognostic markers of tumor progression and new pharmacological targets in the treatment for gastric cancer . PMID: 25483095 Co-depletion of MAD2 and BUBR1 causes cell cycle arrest and cell death in addition to aneuploidy. PMID: 24687487 hMAD2 also binds to the hREV7-binding sequence in hREV3, whereas hMAD2 does not bind to a similar sequence in ADAM9 or ELK-1 and hREV7 does not bind to the hMAD2-binding sequence in hMAD1 or hCDC20. PMID: 20088965 CDC20, MAD2 and Aurora-B protein expression are associated with chromosomal abnormalities and poor prognosis in patients with myelodysplastic syndromes. PMID: 25637637 the interaction of FAT10 with MAD2 is a key mechanism underlying the promalignant property of FAT10 PMID: 25422469 MAD2 and CDC20 overexpression was increased in high-grade squamous intraepithelial lesions and squamous cell carcinomas, suggesting their involvement in the initiation of cervical cancers. PMID: 25083970 MAD2 may be involved in oral carcinogenesis and may represent an important prognostic factor associated with a more malignant phenotype of oral squamous cell carcinoma. PMID: 25503128 This article reviews Mad1 and Mad2 - structural and functional relationship with implication in genetic diseases, specifically in cancer. [review] PMID: 24724894 The interconversion between two distinct conformations of open- and closed-states might facilitate the functional activity of the Mad2 protein. PMID: 24690997 Results showed that neither variants in BUB3 nor variants in MAD2L1 caused any significant effect on the risk of breast cancer PMID: 24711138 In ovarian carcinoma, tumors showing reduced nuclear MAD2 intensity identifying patients with a poorer recurrence-free survival prognosis. PMID: 24792619 The expression and localization of Mad2 and Cdc20 is regulated by subcellular Chk1 during the metaphase-anaphase transition. PMID: 24747134 MiR-28-5p is a critical regulator of Mad2 translation and mitotic checkpoint function. PMID: 24491803 attenuating the affinity of p31(Comet) for Mad2 by phosphorylation promotes SAC activity in mitosis. Specifically, phosphorylation of Ser-102 weakens p31(Comet)-Mad2 binding and enhances p31(Comet)-mediated bypass of the SAC. PMID: 24596092 Results show that Mad1-Mad2 must be targeted to nuclear pore complexes (NPCs) in order to produce the premitotic Cdc20 inhibitor, which ensures that anaphase and mitotic exit are robustly coupled to the establishment and correction of kinetochore-microtubule attachments. PMID: 24581499 results strongly suggest that PP2A is a good therapeutic target in Mad2-overexpressing tumors PMID: 24425774 Studied the significance of budding uninhibited by benzimidazoles-1 (Bub1) and mitotic arrest deficient-2 (Mad2) expression in endometrial carcinoma. PMID: 24654460 Tpr is a kinetochore-independent, rate-limiting factor required to mount and sustain a robust SAC response. PMID: 24344181 sustained MPS1 activity is required for maintaining both the MAD1.C-MAD2 complex and open MAD2 (O-MAD2) at unattached kinetochores to facilitate C-MAD2 production PMID: 24151075 increased expression of CDC20 and MAD2 is related to poor prognosis of urothelial carcinoma of the human bladder PMID: 23995871 Mad2 protein is co-localizes and associated with chk1 increase after DNA damage. PMID: 23454898 Mad2 Binding Induces a Functional Switch in Cdc20,Enabling BubR1 Binding. PMID: 23791783 MAD2 expression levels can indicate sensitivity to anticancer agents, and risk for recurrence in ovarian serous adenocarcinoma. PMID: 22797604 data validate the correlation between upregulation of Mad2 and osteosarcoma advancement, and that the underlying mechanisms involve the increase of invasiveness and cancer stem cell properties PMID: 22992948 Weakened spindle checkpoint with reduced expression of Mad2 is associated with resistance to paclitaxel in ovarian cells. PMID: 21063845 The germline transmission of exonic deletion of MAD2 is possibly associated with its loss of expression resulting in abnormal spindle assembly checkpoint function, subsequent aneuploidy and pregnancy loss. PMID: 22869558 The Mad2 and the APC/C competed for Cdc20 in vitro, and a Cdc20 mutant that does not bind stably to Mad2 abrogated the SAC in vivo. PMID: 23007648 The mitotic Checkpoint Complex is assembled by first forming a BUBR1:BUB3:CDC20 complex in G2 and then selectively incorporating MAD2 in the closed conformation during mitosis. PMID: 22037211

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.