Rabbit Anti-Human SMC1A (a.a. 685-1034) Polyclonal antibody

Name: Rabbit Anti-Human SMC1A (a.a. 685-1034) Polyclonal antibody
SKU: DPABH-19192
Rating: 5 (1 reviews)

Rabbit Anti-Human SMC1A (a.a. 685-1034) Polyclonal antibody for WB, IF, IHC, ELISA

COA

SDS

Datasheet

Key features and details

Target: Human SMC1A
Host: Rabbit
Application: WB, IF, IHC, ELISA
Species Reactivity: Human, Mouse

Summary

Specifications

Antibody Isotype

IgG

Species Reactivity

Human; Mouse

Immunogen

Recombinant human SMC1A protein; Source: E. coli derived, PGEX-4T; Tag: GST; Domain: 685-1034 aa of BC112127

Conjugate

Unconjugated

Applications

Application Notes

WB: 1:1000-1:4000
IHC: 1:50-1:500

General Notes

This product (Catalog No. DPABH-19192) is a rabbit-derived polyclonal antibody raised against human SMC1A, targeting the amino acid region 685–1034 of the protein. This antibody exhibits cross-reactivity with Human SMC1A from mouse. It has been affinity purified by Protein A. Structural maintenance of chromosomes protein 1A (SMC1A) is involved in chromosome cohesion during cell cycle and in DNA repair. It is a central component of cohesin complex which is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint.
DPABH-19192 is suitable for use in Western blot (WB) (1:1,000–1:4,000), IHC (1:50–1:500) applications.
DPABH-19192 is supplied as a liquid formulation in PBS with 0.02% sodium azide and 50% glycerol, pH 7.3. For long-term storage, keep at −20 °C. For short-term use, store at 2–8 °C. Avoid repeated freeze–thaw cycles to maintain antibody integrity and performance.

Target

Alternative Names

CDLS2; DXS423E; KIAA0178; SB1.8; SMC 1 alpha; SMC 1A; SMC protein 1A; SMC1; SMC1A; SMC1alpha; SMC1L1; SMCB

Entrez Gene ID

8243

UniProt ID

Q14683

Citations

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Documents

pdf COA

pdf SDS

pdf Datasheet

QA & Reviews

Customer Reviews

References

Phosphorylation of SMC1A promotes hepatocellular carcinoma cell proliferation and migration

INTERNATIONAL JOURNAL OF BIOLOGICAL SCIENCES

Authors: Zhang, Ying; Yi, Fei; Wang, Liang; Wang, Zhuo; Zhang, Naijin; Wang, Zhijun; Li, Ziwei; Song, Xiaoyu; Wei, Shi; Cao, Liu

Abstract

Structural maintenance of chromosomes protein 1A (SMC1A) has been implicated in the development of a variety of cancer types. However, its role in hepatocellular carcinoma remains unknown. In this study, we found that phosphorylated SMC1A was highly expressed in HepG2 and Bel7402 cells when compared with other cancer cell lines. Furthermore, SMC1A knockdown dramatically reduced HepG2 and Bel7402 cell proliferation and migration. Re-expressing phosphomimetic mutants S957DS966D significantly enhanced the proliferation and migration of SMC1A knockdown HepG2 and Bel7402 cells. In addition, phosphorylated SMC1A promotes hepatocellular carcinoma cells growth in vivo. Importantly, the expression of phosphorylated SMC1A was significantly higher in human hepatocellular carcinomacells when compared to peri-tumor benign hepatocytes, and its overexpression was significantly associated with worse prognostic outcomes. These observations suggest that phosphorylation of SMC1A is a vital event in tumorigenesis and disease progression in hepatocellular carcinoma thus necessitating further investigation.

NIPBL Controls RNA Biogenesis to Prevent Activation of the Stress Kinase PKR

CELL REPORTS

Authors: Yuen, Kobe C.; Xu, Baoshan; Krantz, Ian D.; Gerton, Jennifer L.

Abstract

NIPBL, a cohesin loader, has been implicated in transcriptional control and genome organization. Mutations in NIPBL, cohesin, and its deacetylase HDAC8 result in Cornelia de Lange syndrome. We report activation of the RNA-sensing kinase PKR in human lymphoblastoid cell lines carrying NIPBL or HDAC8 mutations, but not SMC1A or SMC3 mutations. PKR activation can be triggered by unmodified RNAs. Gene expression profiles in NIPBL-deficient lymphoblastoid cells and mouse embryonic stem cells reveal lower expression of genes involved in RNA processing and modification. NIPBL mutant lymphoblastoid cells show reduced proliferation and protein synthesis with increased apoptosis, all of which are partially reversed by a PKR inhibitor. Non-coding RNAs from an NIPBL mutant line had less m(6) A modification and activated PKR activity in vitro. This study provides insight into the molecular pathology of Cornelia de Lange syndrome by establishing a relationship between NIPBL and HDAC8 mutations and PKR activation.