Recombinant Human Target Of Rapamycin Complex 2 Subunit Mapkap1 (MAPKAP1) Protein (His-SUMO)

Name: Recombinant Human Target Of Rapamycin Complex 2 Subunit Mapkap1 (MAPKAP1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09518P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) MAPKAP1.

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Product Overview

Description	Recombinant Human Target Of Rapamycin Complex 2 Subunit Mapkap1 (MAPKAP1) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9BPZ7
Target Symbol	MAPKAP1
Synonyms	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)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	AFLDNPTIILAHIRQSHVTSDDTGMCEMVLIDHDVDLEKIHPPSMPGDSGSEIQGSNGETQGYVYAQSVDITSSWDFGIRRRSNTAQRLERLRKERQNQIKCKNIQWKERNSKQSAQELKSLFEKKSLKEKPPISGKQSILSVRLEQCPLQLNNPFNEYSKFDGKGHVGTTATKKIDVYLPLHSSQDRLLPMTVVTMASARVQDLIGLICWQYTSEGREPKLNDNVSAYCLHIAEDDGEVDTDFPPLDSNEPIHKFGFSTLALVEKYSSPGLTSKESLFVRINAAHGFSLIQVDNTKVTMKEILLKAVKRRKGSQKVSGPQYRLEKQSEPNVAVDLDSTLESQSAWEFCLVRENSSRADGVFEEDSQIDIATVQDMLSSHHYKSFKVSMIHRLRFTTDVQLGISGDKVEIDPVTNQKASTKFWIKQKPISIDSDLLCACDLAEEKSPSHAIFKLTYLSNHDYKHLYFESDAATVNEIVLKVNYILESRASTARADYFAQKQRKLNRRTSFSFQKEKKSGQQ
Expression Range	2-522aa
Protein Length	Full Length of Mature Protein
Mol. Weight	75.0kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
Subcellular Location	Cell membrane; Peripheral membrane protein. Cytoplasmic vesicle. Nucleus.
Protein Families	SIN1 family
Database References	HGNC: 18752 OMIM: 610558 KEGG: hsa:79109 STRING: 9606.ENSP00000265960 UniGene: PMID: 28751630 SIN1 plays an important role in breast cancer. PMID: 27780891 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 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 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 Intracellular localization of mTORC2 component, mSin1, contributes to regulation of Akt phosphorylation. PMID: 28143890 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 MAPKAP1 may represent a novel anti-infection and anti-fibrogenesis genomic locus in chronic schistosomiasis japonica. PMID: 25153992 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 DNA-PKcs-mTORC2(SIN1) association is required for UVB-induced Akt Ser-473 phosphorylation and cell survival. PMID: 24365180 Estradiol and mTORC2 cooperate to enhance prostaglandin biosynthesis and tumorigenesis in TSC2-deficient lymphangioleiomyomatosis cells. PMID: 24395886 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 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 SIN1 plays an important role in hepatocellular carcinoma invasion and metastasis by facilitating epithelial-mesenchymal transition. PMID: 23564492 structures show that the C-termini of Avo1 and Sin1 both have the pleckstrin homology (PH) domain fold PMID: 22505404 mSIN1 protein mediates SGK1 protein interaction with mTORC2 protein complex and is required for selective activation of the epithelial sodium channel PMID: 21757730 There is an increased mitochondrial dependence upon mTORC2 dependent cell growth due to PTEN loss PMID: 21170086 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 The human Sin1 proteins form a complex with Jun N-terminal kinase. PMID: 15722200 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 Sin1 is necessary for the assembly of TORC2 and for its capacity to phosphorylate Akt/PKB. PMID: 16919458 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 Sin1 together with Rictor are key components of mTORC2 and play an essential role in Akt phosphorylation and signaling PMID: 17043309 Sin1 may contribute to ATF-2 signaling specificity by acting as a nuclear scaffold. PMID: 17054722 These data suggest that Sin1 is a mammalian Ras-inhibitor. PMID: 17303383 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 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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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.