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MAPKAP1 / MIP1 Antibody (Internal)
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
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- BACKGROUND
Application 
| WB, IHC-P |
|---|---|
| Primary Accession | Q9BPZ7 |
| Reactivity | Human, Mouse, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 59kDa |
| Dilution | IHC-P (5 µg/ml), WB (2 µg/ml), |
| Gene ID | 79109 |
|---|---|
| Other Names | Target of rapamycin complex 2 subunit MAPKAP1, TORC2 subunit MAPKAP1, Mitogen-activated protein kinase 2-associated protein 1, Stress-activated map kinase-interacting protein 1, SAPK-interacting protein 1, mSIN1, MAPKAP1, MIP1, SIN1 |
| Target/Specificity | 18 amino acid peptide from near the center of human MAPKAP1. |
| Reconstitution & Storage | Short term 4°C, long term aliquot and store at -20°C, avoid freeze thaw cycles. Store undiluted. |
| Precautions | MAPKAP1 / MIP1 Antibody (Internal) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | MAPKAP1 |
|---|---|
| Synonyms | MIP1, SIN1 |
| Function | Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. Within mTORC2, MAPKAP1 is required for complex formation and mTORC2 kinase activity. MAPKAP1 inhibits MAP3K2 by preventing its dimerization and autophosphorylation. Inhibits HRAS and KRAS signaling. Enhances osmotic stress-induced phosphorylation of ATF2 and ATF2-mediated transcription. Involved in ciliogenesis, regulates cilia length through its interaction with CCDC28B independently of mTORC2 complex. |
| Cellular Location | Cell membrane; Peripheral membrane protein. Cytoplasmic vesicle. Nucleus |
| Tissue Location | Ubiquitously expressed, with highest levels in heart and skeletal muscle. |
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
Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient- insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. Within mTORC2, MAPKAP1 is required for complex formation and mTORC2 kinase activity. MAPKAP1 inhibits MAP3K2 by preventing its dimerization and autophosphorylation. Inhibits HRAS and KRAS signaling. Enhances osmotic stress-induced phosphorylation of ATF2 and ATF2-mediated transcription. Involved in ciliogenesis, regulates cilia length through its interaction with CCDC28B independently of mTORC2 complex.
References
Schroder W.,et al.Gene 339:17-23(2004).
Cheng J.,et al.Mol. Cell. Biol. 25:5955-5964(2005).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Bechtel S.,et al.BMC Genomics 8:399-399(2007).
Humphray S.J.,et al.Nature 429:369-374(2004).
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