Human SHC protein fragment (ab109851)
- Product nameHuman SHC protein fragment
- DescriptionRecombinant, His tag
- SourceE. coli
- Amino Acid Sequence
- SequenceMGSSHHHHHHSSGLVPRGSHFNTRTQVTREAISLVCEAVP GAKGATRRRKPCSRPLSSILGRSNLKFAGMPITLTVSTSS LNLMAADCKQIIANHHMQSISFASGGDPDTMNKLSGGGGR RTRVEGGQLGGEEWTRHGSFVNKPTRGWLHPNDKVMGPGV SYLVRYMGCVEVLQSMRALDAEYVAYVAKDPVNQRACHIL ECPEGLAQDVISTIGQAFELRFKQYLRNPPKLVTPHDRMA GFDGSAWDEEEEEPPDHQYYNDFPGKEPPLGGVVDMRLRE GAAPGAARPTAPNAQTPSHLGATLPVGQPVGGDPEVRKQM PPPPPCPAGRELFDDPSYVNVQNLDKARQAVGGAGPPNPA INGSAPRDLFDMKPFEDALRVPPPPQSVSMAEQLRGEPWF HGKLSRREAEALLQLNGDFLVRESTTTPGQYVLTGLQSGQ PKHLLLVDPEGVVRTKDHRFESVSHLISYHMDNHLPIISA GSELCLQQPVERKL
- Molecular weight54 kDa including tags
- Amino acids1 to 474
- TagsHis tag N-Terminus
Our Abpromise guarantee covers the use of ab109851 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
- Purity> 90
% by SDS-PAGE.
- Concentration information loading...
Preparation and Storage
- Stability and Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Constituents: 20% Glycerol, 200mM Sodium chloride, 20mM Tris HCl, 2mM DTT, 0.1mM PMSF, pH 8.0
- SH2 domain protein C1
- SHC (Src homology 2 domain containing) transforming protein 1
- SHC 1
- SHC A
- SHC transforming protein 1
- SHC-transforming protein 1
- SHC-transforming protein 3
- SHC-transforming protein A
- Src homology 2 domain-containing-transforming protein C1
- FunctionSignaling adapter that couples activated growth factor receptors to signaling pathway. 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.
- Tissue specificityWidely expressed. Expressed in neural stem cells but absent in mature neurons.
- Sequence similaritiesContains 1 PID domain.
Contains 1 SH2 domain.
- DomainIn response to a variety of growth factors, isoform p46Shc and isoform p52Shc bind to phosphorylated Trk receptors through their phosphotyrosine binding (PID) and/or SH2 domains. The PID and SH2 domains bind to specific phosphorylated tyrosine residues in the Asn-Pro-Xaa-Tyr(P) motif of the Trk receptors. Isoform p46Shc and isoform p52Shc are in turn phosphorylated on three tyrosine residues within the extended proline-rich domain. These phosphotyrosines act as docking site for GRB2 and thereby are involved in Ras activation.
modificationsPhosphorylated by activated epidermal growth factor receptor. Isoform p46Shc and isoform p52Shc are phosphorylated on tyrosine residues of the Pro-rich domain. Isoform p66Shc is phosphorylated on Ser-36 by PRKCBB upon treatment with insulin, hydrogen peroxide or irradiation with ultraviolet light.
- Cellular localizationCytoplasm; Mitochondrion matrix. Localized to the mitochondria matrix. Targeting of isoform p46Shc to mitochondria is mediated by its first 32 amino acids, which behave as a bona fide mitochondrial targeting sequence. Isoform p52Shc and isoform p66Shc, that contain the same sequence but more internally located, display a different subcellular localization and Mitochondrion. In case of oxidative conditions, phosphorylation at 'Ser-36' of isoform p66Shc, leads to mitochondrial accumulation.
References for Human SHC protein fragment (ab109851)
ab109851 has not yet been referenced specifically in any publications.