Recombinant Human Target of rapamycin complex 2 subunit MAPKAP1 (MAPKAP1)

Code CSB-EP857767HU
MSDS
Size $224
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP857767HU could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) MAPKAP1.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP857767HU could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) MAPKAP1.
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Product Details

Purity
Greater than 90% as determined by SDS-PAGE.
Target Names
MAPKAP1
Uniprot No.
Research Area
Signal Transduction
Alternative Names
MAPKAP 1; MAPKAP1; MEKK2 interacting protein 1; MGC2745; MIP 1; MIP1; Mitogen activated protein kinase associated protein 1; Mitogen-activated protein kinase 2-associated protein 1; mSIN1; OTTHUMP00000064207; Ras inhibitor MGC2745; SAPK interacting protein 1; SAPK-interacting protein 1; SIN 1; SIN1_HUMAN; SIN1b; SIN1g; Stress activated map kinase interacting protein 1; Stress activated protein kinase interacting 1; Stress-activated map kinase-interacting protein 1; Target of rapamycin complex 2 subunit MAPKAP1; TORC2 subunit MAPKAP1
Species
Homo sapiens (Human)
Source
E.coli
Expression Region
2-522aa
Target Protein Sequence
AFLDNPTIILAHIRQSHVTSDDTGMCEMVLIDHDVDLEKIHPPSMPGDSGSEIQGSNGETQGYVYAQSVDITSSWDFGIRRRSNTAQRLERLRKERQNQIKCKNIQWKERNSKQSAQELKSLFEKKSLKEKPPISGKQSILSVRLEQCPLQLNNPFNEYSKFDGKGHVGTTATKKIDVYLPLHSSQDRLLPMTVVTMASARVQDLIGLICWQYTSEGREPKLNDNVSAYCLHIAEDDGEVDTDFPPLDSNEPIHKFGFSTLALVEKYSSPGLTSKESLFVRINAAHGFSLIQVDNTKVTMKEILLKAVKRRKGSQKVSGPQYRLEKQSEPNVAVDLDSTLESQSAWEFCLVRENSSRADGVFEEDSQIDIATVQDMLSSHHYKSFKVSMIHRLRFTTDVQLGISGDKVEIDPVTNQKASTKFWIKQKPISIDSDLLCACDLAEEKSPSHAIFKLTYLSNHDYKHLYFESDAATVNEIVLKVNYILESRASTARADYFAQKQRKLNRRTSFSFQKEKKSGQQ
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
75.0kDa
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 6xHis-SUMO-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.

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Target Background

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.
Gene References into Functions
  1. SIN1 interacted and co-located with PKC zeta by pleckstrin homology (PH) domain. Downregulation of SIN1 severely impaired PKC zeta translocation and phosphorylation induced by insulin. PMID: 28751630
  2. SIN1 plays an important role in breast cancer. PMID: 27780891
  3. In colorectal cancer tissues, the Sin1 protein but not mRNA was significantly upregulated while Pdcd4 protein was downregulated, suggesting that loss of Pdcd4 might correlate with Sin1 protein level but not mRNA level in colorectal cancer. PMID: 28692058
  4. SIN1 plays an important role in non-small cell lung cancer; SIN1 is a potential biomarker and a promising target in the treatment of NSCLC PMID: 27993679
  5. This study provides evidence that Sin1, a known element of the mammalian target of rapamycin complex 2 (mTORC2), is required for Interferon-gamma-induced phosphorylation and activation of AKT and that such activation mediates downstream regulation of mTORC1 and its effectors. PMID: 28174303
  6. Intracellular localization of mTORC2 component, mSin1, contributes to regulation of Akt phosphorylation. PMID: 28143890
  7. Akt phosphorylates SIN1 at T86, enhancing mTORC2 kinase activity, which leads to phosphorylation of Akt S473 by mTORC2, thereby catalyzing full activation of Akt. PMID: 26235620
  8. MAPKAP1 may represent a novel anti-infection and anti-fibrogenesis genomic locus in chronic schistosomiasis japonica. PMID: 25153992
  9. mitogen-activated protein kinase associated protein 1 rs10118570 may be an important protective factor for developing better management strategies in lung squamous cell carcinoma. PMID: 24926550
  10. DNA-PKcs-mTORC2(SIN1) association is required for UVB-induced Akt Ser-473 phosphorylation and cell survival. PMID: 24365180
  11. Estradiol and mTORC2 cooperate to enhance prostaglandin biosynthesis and tumorigenesis in TSC2-deficient lymphangioleiomyomatosis cells. PMID: 24395886
  12. results reveal a Sin1-phosphorylation-dependent mTORC2 regulation, providing a potential molecular mechanism by which mutations in the mTORC1-S6K-Sin1 signalling axis might cause aberrant hyper-activation of the mTORC2-Akt pathway PMID: 24161930
  13. NBS1 interacts with the mTOR/Rictor/SIN1 complex through the a.a. 221-402 domain and contributes to the activation of Akt activity. PMID: 23762398
  14. SIN1 plays an important role in hepatocellular carcinoma invasion and metastasis by facilitating epithelial-mesenchymal transition. PMID: 23564492
  15. structures show that the C-termini of Avo1 and Sin1 both have the pleckstrin homology (PH) domain fold PMID: 22505404
  16. mSIN1 protein mediates SGK1 protein interaction with mTORC2 protein complex and is required for selective activation of the epithelial sodium channel PMID: 21757730
  17. There is an increased mitochondrial dependence upon mTORC2 dependent cell growth due to PTEN loss PMID: 21170086
  18. Results demonstrate that Sin1 transcripts can use alternative polyadenylation signals and describe a number of Sin1 splice variants that potentially encode functionally different isoforms. PMID: 15363842
  19. The human Sin1 proteins form a complex with Jun N-terminal kinase. PMID: 15722200
  20. A novel MEKK2-interacting protein, Mip1, that regulates MEKK2 dimerization and activation by forming a complex with inactive and nonphosphorylated MEKK2, was identified. PMID: 15988011
  21. Sin1 is necessary for the assembly of TORC2 and for its capacity to phosphorylate Akt/PKB. PMID: 16919458
  22. Results reveal that the SIN1-rictor-mTOR function in Akt-Ser473 phosphorylation is required for TORC2 function in cell survival but is dispensable for TORC1 function. PMID: 16962653
  23. Sin1 together with Rictor are key components of mTORC2 and play an essential role in Akt phosphorylation and signaling PMID: 17043309
  24. Sin1 may contribute to ATF-2 signaling specificity by acting as a nuclear scaffold. PMID: 17054722
  25. These data suggest that Sin1 is a mammalian Ras-inhibitor. PMID: 17303383
  26. MIP-1 delta expression is increased in RBM (RCC (Renal Cell Carcinoma) bone metastasis) relative to RCC and bone marrow, and may promote RBM-induced osteolysis by stimulating recruitment/differentiation of osteoclast precursors into mature osteoclasts PMID: 18316587
  27. SIN1 and PCBP2 are generally coregulated with large numbers of genes implicated in both cell survival and death and in cellular stress responses, including RNA translation and processing PMID: 18687895

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Subcellular Location
Cell membrane; Peripheral membrane protein. Cytoplasmic vesicle. Nucleus.
Protein Families
SIN1 family
Tissue Specificity
Ubiquitously expressed, with highest levels in heart and skeletal muscle.
Database Links

HGNC: 18752

OMIM: 610558

KEGG: hsa:79109

STRING: 9606.ENSP00000265960

UniGene: Hs.495138

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