SMC2 Antibody [P11C8] Datasheet

Biological Description

Specificity	SMC2 Antibody [P11C8] detects endogenous levels of total SMC2 protein.
Background	SMC2 forms the core ATPase subunit of condensin I and II complexes alongside SMC4 within the structural maintenance of chromosomes protein family, enabling chromosome compaction essential for mitotic segregation. The protein features N- and C-terminal nucleotide-binding domains that heterodimerize through a central hinge region, creating a ring-like structure that encircles chromatin while coiled-coil segments facilitate auxiliary subunit binding. SMC2-SMC4 heterodimers generate ATP-dependent positive supercoils in DNA when interacting with type II topoisomerases, driving axial chromosome shortening from prophase through anaphase while auxiliary subunits CAP-H/CAP-D/CAP-G (condensin I) or CAP-H2/CAP-D3/CAP-G2 (condensin II) modulate DNA-binding affinity and loop extrusion. Condensin II accumulates at centromeres during prometaphase, promoting H3S10 phosphorylation and sister chromatid resolution, whereas condensin I localizes along chromosome arms to maintain mitotic fidelity. ATPase activity cycles through ATP binding at the SMC2/SMC4 interface, head-head dimerization, hinge-mediated DNA capture, and powered translocation along chromatin fibers. Depletion expands mitotic chromosome volume, disrupts pericentromeric compaction, and impairs bipolar spindle attachment, leading to anaphase bridges and cytokinesis failure. Maternal SMC2 supports oocyte chromosome condensation and zygotic pronuclear congression, with knockout causing developmental arrest. In hyperproliferative states, β-catenin/TCF4 transcriptionally upregulates SMC2 to sustain rapid mitotic cycling in colorectal tumors.

Specificity

SMC2 Antibody [P11C8] detects endogenous levels of total SMC2 protein.

Background

SMC2 forms the core ATPase subunit of condensin I and II complexes alongside SMC4 within the structural maintenance of chromosomes protein family, enabling chromosome compaction essential for mitotic segregation. The protein features N- and C-terminal nucleotide-binding domains that heterodimerize through a central hinge region, creating a ring-like structure that encircles chromatin while coiled-coil segments facilitate auxiliary subunit binding. SMC2-SMC4 heterodimers generate ATP-dependent positive supercoils in DNA when interacting with type II topoisomerases, driving axial chromosome shortening from prophase through anaphase while auxiliary subunits CAP-H/CAP-D/CAP-G (condensin I) or CAP-H2/CAP-D3/CAP-G2 (condensin II) modulate DNA-binding affinity and loop extrusion. Condensin II accumulates at centromeres during prometaphase, promoting H3S10 phosphorylation and sister chromatid resolution, whereas condensin I localizes along chromosome arms to maintain mitotic fidelity. ATPase activity cycles through ATP binding at the SMC2/SMC4 interface, head-head dimerization, hinge-mediated DNA capture, and powered translocation along chromatin fibers. Depletion expands mitotic chromosome volume, disrupts pericentromeric compaction, and impairs bipolar spindle attachment, leading to anaphase bridges and cytokinesis failure. Maternal SMC2 supports oocyte chromosome condensation and zygotic pronuclear congression, with knockout causing developmental arrest. In hyperproliferative states, β-catenin/TCF4 transcriptionally upregulates SMC2 to sustain rapid mitotic cycling in colorectal tumors.

Usage Information

Application

WB, IP

Dilution

WB	IP
1:1000	1:50

Reactivity

Human, Rat, Monkey

Source

Rabbit Monoclonal Antibody

MW

140 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

References

https://pubmed.ncbi.nlm.nih.gov/23095742/
https://pubmed.ncbi.nlm.nih.gov/31816133/

Application Data

WB

Validated by Selleck

Lane 1: Hela, Lane 2: COS, Lane 3: H-4-II-E