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MKL1 Antibody (Center)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | Q969V6 |
| Other Accession | NP_065882.1 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 98919 Da |
| Antigen Region | 497-525 aa |
| Gene ID | 57591 |
|---|---|
| Other Names | MKL/myocardin-like protein 1, Megakaryoblastic leukemia 1 protein, Megakaryocytic acute leukemia protein, Myocardin-related transcription factor A, MRTF-A, MKL1, KIAA1438, MAL |
| Target/Specificity | This MKL1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 497-525 amino acids from the Central region of human MKL1. |
| Dilution | WB~~1:1000 E~~Use at an assay dependent concentration. |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | MKL1 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | MRTFA (HGNC:14334) |
|---|---|
| Function | Transcription coactivator that associates with the serum response factor (SRF) transcription factor to control expression of genes regulating the cytoskeleton during development, morphogenesis and cell migration (PubMed:26224645). The SRF-MRTFA complex activity responds to Rho GTPase-induced changes in cellular globular actin (G- actin) concentration, thereby coupling cytoskeletal gene expression to cytoskeletal dynamics. MRTFA binds G-actin via its RPEL repeats, regulating activity of the MRTFA-SRF complex. Activity is also regulated by filamentous actin (F-actin) in the nucleus. |
| Cellular Location | Cytoplasm. Nucleus Note=Subcellular location is tightly regulated by actin both in cytoplasm and nucleus: high levels of G-actin in the nucleus observed during serum deprivation lead to low levels of nuclear MRTFA, while reduced levels of nuclear G-actin result in accumulation of MRTFA in the nucleus (By similarity). G-actin-binding in the cytoplasm inhibits nuclear import by masking the nuclear localization signal (NLS) (By similarity). In contrast, binding to nuclear globular actin (G-actin) promotes nuclear export to the cytoplasm (By similarity). Nuclear localization is regulated by MICAL2, which mediates depolymerization of nuclear actin, which decreases nuclear G-actin pool, thereby promoting retention of MRTFA in the nucleus and subsequent formation of an active complex with SRF (PubMed:24440334). Nuclear import is mediated by importins KPNA4 and KPNB1 (By similarity) {ECO:0000250|UniProtKB:Q8K4J6, ECO:0000269|PubMed:24440334} |
| Tissue Location | Ubiquitously expressed, has been detected in lung, placenta, small intestine, liver, kidney, spleen, thymus, colon, muscle, heart and brain (PubMed:11344311). Expressed in peripheral blood mononuclear cells (at protein level) (PubMed:26224645) |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
The protein encoded by this gene interacts with the transcription factor myocardin, a key regulator of smooth muscle cell differentiation. The encoded protein is predominantly nuclear and may help transduce signals from the cytoskeleton to the nucleus. This gene is involved in a specific translocation event that creates a fusion of this gene and the RNA-binding motif protein-15 gene. This translocation has been associated with acute megakaryocytic leukemia.
References
Gilles, L., et al. Blood 114(19):4221-4232(2009)
Hinohara, K., et al. Hum. Genet. 126(4):539-547(2009)
Estrada, K., et al. Hum. Mol. Genet. 18(18):3516-3524(2009)
Brandt, D.T., et al. Nat. Cell Biol. 11(5):557-568(2009)
Medjkane, S., et al. Nat. Cell Biol. 11(3):257-268(2009)
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