腺病毒IgM

Specificity: The antibody detects endogenous level of total IGF-1R protein

Immunogen: Peptide sequence around aa 1163~1167/1164~1168 (T-D-Y-Y-R-K) derived from Human IGF-1R

Binding Site: around Tyr1165/Tyr1166

WB Dilution: 500~1000

Antibodies were produced by immunizing rabbits with synthetic peptide and KLH conjugates. Antibodies were purified by affinity-chromatography using epitope-specific peptide.This receptor binds insulin-like growth factor 1 (IGF1) with a high affinity and IGD2 with a lower affinity. It has a tyrosine-protein kinase activity which is necessary for the activation of the IGF-1 stimulated downstream signaling cascade. When present in a hybrid receptor with INSR, binds IGF1

Function: This receptor binds insulin-like growth factor 1 (IGF1) with a high affinity and IGF2 with a lower affinity. It has a tyrosine-protein kinase activity, which is necessary for the activation of the IGF1-stimulated downstream signaling cascade.

Catalytic Activity: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Enzyme Regulation: Autophosphorylation activates the kinase activity.

Subunit: Tetramer of 2 alpha and 2 beta chains linked by disulfide bonds. The alpha chains contribute to the formation of the ligand-binding domain, while the beta chain carries the kinase domain. Interacts with PIK3R1 and with the PTB/PID domains of IRS1 and SHC1 in vitro when autophosphorylated on tyrosine residues.

Subcellular Location: Membrane; Single-pass type I membrane protein.

Tissue Specificity: Expressed in a variety of tissues.

Ptm: The cytoplasmic domain of the beta subunit is autophosphorylated on tyrosine residues in response to insulin-like growth factor I (IGF I).

Ptm: Phosphorylation of Tyr-980 is required for IRS1- and SHC1-binding.

Similarity: Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.

Similarity: Contains 3 fibronectin type-III domains.

Similarity: Contains 1 protein kinase domain. [1] Ullrich A., Gray A., Tam A.W., Yang-Feng T., Tsubokawa M., Collins C., Henzel W., Bon T.L., Kathuria S., Chen E., et al.
Insulin-like growth factor I receptor primary structure: comparison with insulin receptor suggests structural determinants that define functional specificity.
[2] Abbot A.M., Bueno R., Pedrini M.T., Murray J.M., Smith R.J.
Insulin-like growth factor I receptor gene structure.
[3] Rieder M.J., Livingston R.J., Daniels M.R., Montoya M.A., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., et al.
NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).
[4] Cooke D.W., Bankert L.A., Roberts C.T. Jr., Leroith D., Casella S.J.
Analysis of the human type I insulin-like growth factor receptor promoter region.
[5] Lee S.-T., Strunk K.M., Spritz R.A.
A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes.
[6] Tollefsen S.E., Stoszek R.M., Thompson K.
Interaction of the alpha beta dimers of the insulin-like growth factor I receptor is required for receptor autophosphorylation.
[7] Kato H., Faria T.N., Stannard B., Roberts C.T. Jr., LeRoith D.
Role of tyrosine kinase activity in signal transduction by the insulin-like growth factor-I (IGF-I) receptor. Characterization of kinase-deficient IGF-I receptors and the action of an IGF-I-mimetic antibody (alpha IR-3).
[8] Craparo A., O'Neill T.J., Gustafson T.A.
Non-SH2 domains within insulin receptor substrate-1 and SHC mediate their phosphotyrosine-dependent interaction with the NPEY motif of the insulin-like growth factor I receptor.
[9] Lopaczynski W., Terry C., Nissley P.
Autophosphorylation of the insulin-like growth factor I receptor cytoplasmic domain.