Datasheet

Biological Description

Specificity	Mad1 Mouse mAb detects endogenous levels of total Mad1 protein.
Background	Mad1 (Mitotic Arrest Deficient 1) is a crucial component of the spindle assembly checkpoint (SAC) family, ensuring precise chromosome segregation by preventing anaphase initiation until all chromosomes are correctly attached to spindle microtubules. Mad1 is a 718-amino acid homodimeric coiled-coil protein, with the C-terminal domain (CTD) playing a pivotal role in its function and regulatory control. The CTD harbors motifs vital for Mad1’s growth-inhibitory activity and ability to repress Myc-dependent transcription. Deletion of its last 18 amino acids (region V) abolishes these functions; however, deleting both region V and adjacent region IV restores them, revealing a complex phosphorylation-regulated interplay within these domains. The CTD also facilitates Mad1’s kinetochore targeting and interaction with checkpoint proteins like Bub1, forming a multivalent interface essential for recruiting Mad2 to unattached kinetochores. This recruitment catalyzes Mad2 conformational activation and mitotic checkpoint complex (MCC) assembly, which inhibits the anaphase-promoting complex/cyclosome (APC/C), thereby delaying anaphase until proper attachment is achieved. Regulatory phosphorylation by kinases such as Mps1 and Bub1 modulates Mad1’s activity, while p31^comet^ serves as an inhibitor once kinetochores are correctly attached. Mad1 also influences transcriptional repression through interaction with Myc-Max complexes, impacting cell cycle progression. Dysregulation of Mad1 functions leads to chromosome instability and aneuploidy, contributing to tumorigenesis.

Specificity

Mad1 Mouse mAb detects endogenous levels of total Mad1 protein.

Background

Mad1 (Mitotic Arrest Deficient 1) is a crucial component of the spindle assembly checkpoint (SAC) family, ensuring precise chromosome segregation by preventing anaphase initiation until all chromosomes are correctly attached to spindle microtubules. Mad1 is a 718-amino acid homodimeric coiled-coil protein, with the C-terminal domain (CTD) playing a pivotal role in its function and regulatory control. The CTD harbors motifs vital for Mad1’s growth-inhibitory activity and ability to repress Myc-dependent transcription. Deletion of its last 18 amino acids (region V) abolishes these functions; however, deleting both region V and adjacent region IV restores them, revealing a complex phosphorylation-regulated interplay within these domains. The CTD also facilitates Mad1’s kinetochore targeting and interaction with checkpoint proteins like Bub1, forming a multivalent interface essential for recruiting Mad2 to unattached kinetochores. This recruitment catalyzes Mad2 conformational activation and mitotic checkpoint complex (MCC) assembly, which inhibits the anaphase-promoting complex/cyclosome (APC/C), thereby delaying anaphase until proper attachment is achieved. Regulatory phosphorylation by kinases such as Mps1 and Bub1 modulates Mad1’s activity, while p31^comet^ serves as an inhibitor once kinetochores are correctly attached. Mad1 also influences transcriptional repression through interaction with Myc-Max complexes, impacting cell cycle progression. Dysregulation of Mad1 functions leads to chromosome instability and aneuploidy, contributing to tumorigenesis.

Usage Information

Application

WB, IF

Dilution

WB

1:2000

Reactivity

human

Source

Mouse

MW

~83 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/24477934/
https://pubmed.ncbi.nlm.nih.gov/10825189/

Mad1 Mouse mAb

Biological Description

Usage Information

References

Application Data