05-1044
Anti-Sin1 Antibody, clone 1C7.2
clone 1C7.2, from mouse
别名:
MEKK2-interacting protein 1, Mitogen-activated protein kinase 2-associated protein 1, SAPK-interacting protein 1, Stress-activated map kinase-interacting protein 1, TORC2 subunit MAPKAP1, mitogen-activated protein kinase associated protein 1, ras inhibit
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About This Item
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生物来源
mouse
质量水平
抗体形式
purified antibody
抗体产品类型
primary antibodies
克隆
1C7.2, monoclonal
种属反应性
rat, mouse, human
技术
immunofluorescence: suitable
immunohistochemistry: suitable (paraffin)
immunoprecipitation (IP): suitable
western blot: suitable
同位素/亚型
IgG2aκ
NCBI登记号
UniProt登记号
运输
wet ice
靶向翻译后修饰
unmodified
基因信息
human ... MAPKAP1(79109)
一般描述
Sin1 (stress-activated protein kinase (SAPK)-interacting protein 1, MAPKAP1) is an essential component of the Torc2 complex. mTORC2 is comprised of mTOR, a large Ser/Thr protein kinase along with Sin1, GL (mLST8), Protor1, Protor2, and Rictor. The complex that is activated primarily downstream of PI3 Kinase and is known to affect cell proliferation and survival primarily by phosphorylating Akt on Ser473. Additionally, the mTORC2 complex is also known to effect cytoskeletal organization and migration by exerting its effects through Rac, Rho, and PKC. Sin1 is also known to directly interact without proteins that include Ras, SPAKs, and JNK.
Sin1 is known to have multiple alternative splicing isoforms. Full-length Sin1 is a 522aa protein (59kDa). Sin1 (Isoform 5) (36 kDa) has exon 6 spliced to an alternative exon 7a that results in the loss of both the RBD and PHL domains. Sin1Isoform 2) (55 kDa) lacks exon 7 and lacks the RBD. Sin1 (Isoform 3) (53 kDa) lacks exon 8 lacks the PHL domain. Sin1 (Isoform 4) (37 kDa) lacks exon 1.
Sin1 is known to have multiple alternative splicing isoforms. Full-length Sin1 is a 522aa protein (59kDa). Sin1 (Isoform 5) (36 kDa) has exon 6 spliced to an alternative exon 7a that results in the loss of both the RBD and PHL domains. Sin1Isoform 2) (55 kDa) lacks exon 7 and lacks the RBD. Sin1 (Isoform 3) (53 kDa) lacks exon 8 lacks the PHL domain. Sin1 (Isoform 4) (37 kDa) lacks exon 1.
特异性
Detects Sin-1 and its isoforms.
Other species have not been tested.
免疫原
Full-length Human Sin1 GST-fusion protein.
应用
Detect Sin1 using this Anti-Sin1 Antibody, clone 1C7.2 validated for use in WB, IP, IH(P) & IF.
质量
Western Blot Analysis:
This lot detected Sin1 at 1:1,000 dilution in A431 cell lysate resolved via SDS-PAGE and transferred to PVDF.
This lot detected Sin1 at 1:1,000 dilution in A431 cell lysate resolved via SDS-PAGE and transferred to PVDF.
目标描述
Sin1 is 59 kDa Isoforms are 36, 37, 41, 53, 54, and 55 kDa
外形
Format: Purified
Purified mouse monoclonal in 0.1M Tris-Glycine (pH 7.4), 150mM NaCl with 0.05% NaN3.
其他说明
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
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储存分类代码
12 - Non Combustible Liquids
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
Medical science monitor : international medical journal of experimental and clinical research, 23, 3666-3672 (2017-07-29)
BACKGROUND Protein kinase C zeta (PKC ζ) plays an important role in insulin induced glycometabolism and insulin receptor (IR) associated signaling pathways. The full activation of PKC ζ depends on its translocation from cytosol to membrane and phosphorylation at Thr410.
MicroRNA-7 regulates the mTOR pathway and proliferation in adult pancreatic ?-cells.
Diabetes null
Endocrine, metabolic & immune disorders drug targets, 23(9), 1186-1200 (2023-02-08)
The RAS system is involved in the regulation of islet function, but its regulation remains unclear. This study investigates the role of an islet-specific miR-375 in the effect of RAS system on islet β-cells. miR-375 mimics and inhibitors were transfected
Isolation of the mTOR complexes by affinity purification.
Methods in Molecular Biology null
Cancers, 13(10) (2021-06-03)
The serine/threonine kinase AKT is a major effector during phosphatidylinositol 3-kinase (PI3K)-driven cell signal transduction in response to extracellular stimuli. AKT activation mechanisms have been extensively studied; however, the mechanism underlying target of rapamycin complex 2 (mTORC2) phosphorylation of AKT
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