Biotinylated Recombinant Human Shc-Transforming Protein 1 (SHC1) Protein (MBP&His-Avi)

Name: Biotinylated Recombinant Human Shc-Transforming Protein 1 (SHC1) Protein (MBP&His-Avi)
Brand: Beta LifeScience
SKU: BLC-06742P
Price: 735.2 USD
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Avi-tagged proteins, Biotinylated proteins, Featured biotinylated protein molecules, Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Biotinylated Recombinant Human Shc-Transforming Protein 1 (SHC1) Protein (MBP&His-Avi) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P29353
Target Symbol	SHC1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-MBP&C-6His-Avi
Target Protein Sequence	HPNDKVMGPGVSYLVRYMGCVEVLQSMRALDFNTRTQVTREAISLVCEAVPGAKGATRRRKPCSRPLSSILGRSNLKFAGMPITLTVSTSSLNLMAADCKQIIANHHMQSISFASGGDPDTAEYVAYVAKDPVNQRACHILECPEGLAQDVISTIGQAFELRFKQYLRNPP
Expression Range	150-320aa
Protein Length	Partial
Mol. Weight	66.4 kDa
Research Area	Neuroscience
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	Signaling adapter that couples activated growth factor receptors to signaling pathways. Participates in a signaling cascade initiated by activated KIT and KITLG/SCF. Isoform p46Shc and isoform p52Shc, once phosphorylated, couple activated receptor tyrosine kinases to Ras via the recruitment of the GRB2/SOS complex and are implicated in the cytoplasmic propagation of mitogenic signals. Isoform p46Shc and isoform p52Shc may thus function as initiators of the Ras signaling cascade in various non-neuronal systems. Isoform p66Shc does not mediate Ras activation, but is involved in signal transduction pathways that regulate the cellular response to oxidative stress and life span. Isoform p66Shc acts as a downstream target of the tumor suppressor p53 and is indispensable for the ability of stress-activated p53 to induce elevation of intracellular oxidants, cytochrome c release and apoptosis. The expression of isoform p66Shc has been correlated with life span. Participates in signaling downstream of the angiopoietin receptor TEK/TIE2, and plays a role in the regulation of endothelial cell migration and sprouting angiogenesis.
Subcellular Location	Cytoplasm.; [Isoform p46Shc]: Mitochondrion matrix.
Database References	HGNC: 10840 OMIM: 600560 KEGG: hsa:6464 STRING: 9606.ENSP00000401303 UniGene: Hs.433795
Tissue Specificity	Widely expressed. Expressed in neural stem cells but absent in mature neurons.

Gene Functions References

Data suggest that up-regulation of SHC threonine phosphorylation is responsible for elevated Akt-signaling and Erk-signaling in triple-negative breast cancer cell lines. PMID: 29208567
Characterization of bioenergetic parameters and reactive oxygen species production showed that the cellular model of Leigh syndrome is described by increased intracellular oxidative stress and oxidative damage to DNA and proteins, which correlate with increased p66Shc phosphorylation at Ser36. PMID: 28739512
A positive relationship between the p66Shc expression and oxidative stress was found. p66Shc and oxidative stress were significant predictors of the degree of tubular damage. PMID: 27377870
Adeno-X Adenoviral System 3 can be used to efficiently construct recombinant adenovirus containing p66Shc gene, and the Adeno-X can inhibit the proliferation of MCF-7 cells by inducing cell cycle arrest at the G2/M phase PMID: 27530145
STAT4 is a novel transcriptional regulator of p66Shc in normal and chronic lymphocytic leukemia B cells PMID: 27494881
Isoform b of DDR1 is responsible for collagen I-induced up-regulation of N-cadherin and tyrosine 513 of DDR1b is necessary. PMID: 27605668
NIC exacerbated AZA-dependent injury via augmenting p66shc transcription. While RES suppressed NIC+AZA-mediated injury, -surprisingly-it further enhanced activity of the p66shc promoter. RES protected cells via the cytoplasmic p66shc/Nrf2/heme oxygenase-1 (HO-1) axis PMID: 28739690
The results show that the interaction between STS-1 and ShcA is regulated in response to EGF receptor activation. PMID: 28690151
Nox4-derived H2O2 in part activates Nox2 to increase mitochondrial ROS via pSer36-p66Shc, thereby enhancing VEGFR2 signaling and angiogenesis in endothelial cells. PMID: 28424170
Data identify, for the first time, a novel non-canonical dynamic mode of interaction between Met and the p66 protein isoform of Shc and its effects on rewiring binding effector complexes according to the activation state of the receptor. PMID: 27048591
regulates the alternative splicing of XAF1 in extracellular matrix-detachment induced autophagy to coordinate with the anoikic cell death PMID: 26643258
The silence of p66(Shc) in HCT8 cells reduced the proliferation and accelerated the apoptosis, in addition, the expression of pro-apoptotic proteins caspase-3, caspase-9, Bax was enhanced and the expression of anti-apoptotic protein Bcl-2 was declined. PMID: 26464652
In mice and humans, reduced p66Shc levels protect from obesity, but not from ectopic fat accumulation, glucose intolerance and insulin resistance. PMID: 26122877
Data suggest SHC1 (SH2 domain protein C1) expression down-regulates epithelial-mesenchymal transition by repressing TGFB-induced SMAD2/3 activation through differential partitioning of receptors at cell surface of mammocytes/keratinocytes. PMID: 26680585
p66shc expression in coronary heart disease patients was significantly higher compared with the control group PMID: 24676406
Finally, a crystal structure of EGFR in complex with a primed Shc1 peptide reveals the structural basis for EGFR substrate specificity. PMID: 26551075
p53-dependent augmentation of p66(Shc) expression and function represents a key signalling response contributing to beta cell apoptosis under conditions of lipotoxicity PMID: 25810038
Results show elevated level of p66Shc protein reveal in ovarian cancer cells (OCa) indicating a functional role of the protein in regulating the proliferation of OCa cells. PMID: 24395385
p66ShcA was upregulated in hearts of patients with ischemic heart disease without heart failure PMID: 25680868
These data demonstrate that the p52Shc phosphorylation level is altered by the solution environment without affecting the fraction of active c-Src. PMID: 25961473
Although H2S failed to affect the activities of these two proteins, it disrupted their association. Cysteine-59 resides in proximity to serine-36, the phosphorylation site of p66Shc. PMID: 24766279
demonstrate that ShcA-dependent activation of AKT, but not the RAS/MAPK pathway, induces VEGF production by bolstering VEGF mRNA translation PMID: 24837366
the p66shc-dependant ROS production during oxidative stress has mitochondrial origin in human normal and cancer cells. PMID: 24618848
p66Shc is a bifunctional protein involved in cellular oxidative stress response and differentiation. PMID: 24807908
High p66Shc expression is associated with malignant gastrointestinal lesions. PMID: 24599562
CRIF1 knockdown partially induces endothelial activation via increased ROS production and phosphorylation of p66shc PMID: 24906005
p66(Shc) plays a vital part in canonical Wnt signaling in the endothelium and mediates Wnt3a-stimulated endothelial oxidative stress and dysfunction. PMID: 25147340
these results identify Grb2 and Shc as central signaling effectors of Met-driven progression of intestinal epithelial-derived cancers. Notably, they suggest that Grb2 may represent a promising target for the design of novel colorectal cancer therapies. PMID: 24708867
repression of Shc expression by let-7a delays senescence of human diploid fibroblasts. PMID: 24165399
Study identifies p66ShcA as one of the first prognostic biomarkers for the identification of more aggressive tumors with mesenchymal properties, regardless of molecular subtype. PMID: 25071152
Serine phosphorylation of p66shc is carried out by active MKK6.beta-Amyloid-induced ROS production and apoptosis increased in the presence of MKK6 and p66shc, which directly associate. PMID: 24085465
unlike the other isoforms of Shc1, p66Shc appears to antagonize insulin and mTOR signaling, which limits glucose uptake and metabolism. PMID: 24550542
Exposure of human aortic endothelial cells to stretch led to stretch- and time-dependent p66(Shc) phosphorylation downstream of integrin alpha5beta1 and JNK kinase. In parallel, NADP oxidase and reactive oxygen species increased, and NO bioavailability decreased PMID: 24842918
study concludes hypercholesterolemia stimulates p66Shc expression in platelets, promoting platelet oxidative stress, hyperreactivity and hyperaggregation via p66Shc PMID: 24845561
In lung cancer tissues and single cells, p66(Shc) expression inversely correlates with that of Aiolos. PMID: 24823637
Arg-II promotes mitochondrial dysfunction leading to VSMC senescence/apoptosis through complex positive crosstalk among S6K1-JNK, ERK, p66Shc, and p53, contributing to atherosclerotic vulnerability phenotype. PMID: 23832324
a central role for adaptor proteins p66Shc and Grb2 in the regulation of ARF1 and ARF6 activation in invasive breast cancer cells. PMID: 24407288
different domains in SOCS5 contribute to two distinct mechanisms for regulation of cytokine and growth factor signaling with JAK1 and SHC-1 PMID: 23990909
Salvianolic acid A induced SIRT1 plays an anti-apoptotic role in concanavalin A induced hepatitis by inhibiting p66Shc expression. PMID: 23993977
p66(Shc) is a good candidate molecule to address the mechanisms underlying healthy aging and to be targeted for the development of novel pharmacological tools for the prevention or cure of age-related pathologies. PMID: 23524280
DNA methylation of the p66Shc promoter was significantly decreased in the intrauterine growth restricted compared with the appropriate for gestational age infants groups. PMID: 23529764
Shc plays a pivotal role in coordinately regulating autophagy process and apoptotic resistance in lung adenocarcinoma cells under nutrient-limited conditions. PMID: 23815759
Knock-down of p66(Shc) leads to a positive feedback upregulation of Nrf2 expression and accordingly, Nrf2 is found to be highly expressed in tumors with low p66(Shc) expression PMID: 23689140
The p66Shc protein (SHC1 protein) is very important for the regulation of the intracellular redox balance and oxidative stress levels. PMID: 23606925
Distinct phosphotyrosine-dependent functions of the ShcA adaptor protein are required for transforming growth factor beta (TGFbeta)-induced breast cancer cell migration, invasion, and metastasis PMID: 23277357
our analysis of human samples demonstrated that enhanced p53/p66Shc signaling plays an important role in the progression of human non-alcoholic fatty liver disease. PMID: 22641095
Expression of SHC1 mutant protects PC-3 cells against Diallyl trisulfide induced death. PMID: 22020565
S1P1 expression is controlled by the pro-oxidant activity of p66Shc and is impaired in B-CLL patients with unfavorable prognosis. PMID: 23033271
Elevated p66Shc expression enhances prostate cancer tumorigenicity. PMID: 22561705
These findings indicate that LDL cholesterol upregulates human endothelial p66shc expression via hypomethylation of CpG dinucleotides in the p66shc promoter. PMID: 22661506

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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.

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