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As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation (By similarity)..
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Data suggest that CIA2B and MMS19 physically interact with C-terminus of viperin/RSAD2; CIAO1 appears to function as primary viperin-interacting protein; CIA2A binds to N-terminus of viperin in CIAO1-, CIA2B-, and MMS19-independent fashion. (CIA2B = metallochaperone CIA2B/FAM96B; MMS19 = transcription factor MMS19; CIAO1 = cytosolic iron-sulfur assembly component 1; CIA2A = metallochaperone CIA2A/Fam96a)
CIA2B-CIA1 (show CIAO1 Proteins)-MMS19 (show MMS19 Proteins) and CIA2A-CIA1 (show CIAO1 Proteins) assist different branches of Fe/S protein (show CDSN Proteins) assembly and intimately link this process to cellular iron regulation via IRP1 (show ACO1 Proteins) Fe/S cluster maturation and IRP2 (show IREB2 Proteins) stabilization.
Co-localization experiments by fluorescent confocal microscopy revealed that FAM96B colocalized with prelamin A in HEK (show EPHA3 Proteins)-293 cells.
The mammalian proteins MMS19, MIP18, and ANT2 are involved in cytoplasmic iron-sulfur cluster protein assembly.
these findings suggest that FAM96B acts as a regulator of E2-2 (show TCF4 Proteins) through the control of its protein expression.
As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation (By similarity).
MSS19-interacting protein of 18 kDa
, mitotic spindle-associated MMXD complex subunit MIP18