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E_B4 (C-term)Purified Rabbit Polyclonal Antibody (Pab)
| Country | United States
Ordering Information
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| Catalog # | Size | Availability | Price | |
| AP7631b | 0.1 mg 400 ul | In Stock | $ 255.00 | DISCONTINED INQUIRE CLICK INQUIRE Add to cart |
- Specification
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E_B4 (C-term) - Product info | |
| Application | WB
|
| Primary Accession | Q15303 |
| Reactivity | Human |
| Concentration | 0.25 mg/ml |
| Isotype | Rabbit Ig |
| Calculated MW | 146808 Da |
E_B4 (C-term) - Additional info | |
| Gene ID 2066 | |
| Other Names ERBB4; HER4; Receptor tyrosine-protein kinase erbB-4; Proto-oncogene-like protein c-ErbB-4; Tyrosine kinase-type cell surface receptor HER4; p180erbB4; ERBB4 intracellular domain; s80HER4 | |
| Target/Specificity This ErbB4 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1279~1308 amino acids from the C-terminal region of human ErbB4. | |
| Dilution WB~~1:100~500WB~~1:1000 | |
| Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS. | |
| Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. | |
| Precautions E_B4 (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. | |
E_B4 (C-term) - Protein Information | |
| Name ERBB4 | |
| Synonyms HER4 | |
| Function Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins and EGF family members and regulates development of the heart, the central nervous system and the mammary gland, gene transcription, cell proliferation, differentiation, migration and apoptosis. Required for normal cardiac muscle differentiation during embryonic development, and for postnatal cardiomyocyte proliferation. Required for normal development of the embryonic central nervous system, especially for normal neural crest cell migration and normal axon guidance Required for mammary gland differentiation, induction of milk proteins and lactation. Acts as cell-surface receptor for the neuregulins NRG1, NRG2, NRG3 and NRG4 and the EGF family members BTC, EREG and HBEGF. Ligand binding triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors. Ligand specificity and signaling is modulated by alternative splicing, proteolytic processing, and by the formation of heterodimers with other ERBB family members, thereby creating multiple combinations of intracellular phosphotyrosines that trigger ligand- and context-specific cellular responses. Mediates phosphorylation of SHC1 and activation of the MAP kinases MAPK1/ERK2 and MAPK3/ERK1 Isoform JM-A CYT-1 and isoform JM-B CYT-1 phosphorylate PIK3R1, leading to the activation of phosphatidylinositol 3-kinase and AKT1 and protect cells against apoptosis. Isoform JM-A CYT-1 and isoform JM-B CYT-1 mediate reorganization of the actin cytoskeleton and promote cell migration in response to NRG1 Isoform JM-A CYT-2 and isoform JM-B CYT-2 lack the phosphotyrosine that mediates interaction with PIK3R1, and hence do not phosphorylate PIK3R1, do not protect cells against apoptosis, and do not promote reorganization of the actin cytoskeleton and cell migration. Proteolytic processing of isoform JM-A CYT-1 and isoform JM-A CYT-2 gives rise to the corresponding soluble intracellular domains (4ICD) that translocate to the nucleus, promote nuclear import of STAT5A, activation of STAT5A, mammary epithelium differentiation, cell proliferation and activation of gene expression. The ERBB4 soluble intracellular domains (4ICD) colocalize with STAT5A at the CSN2 promoter to regulate transcription of milk proteins during lactation. The ERBB4 soluble intracellular domains can also translocate to mitochondria and promote apoptosis | |
| Cellular Location Cell membrane; Single-pass type I membrane protein. Note=In response to NRG1 treatment, the activated receptor is internalized | |
| Tissue Location Expressed at highest levels in brain, heart, kidney, in addition to skeletal muscle, parathyroid, cerebellum, pituitary, spleen, testis and breast. Lower levels in thymus, lung, salivary gland, and pancreas. Isoform JM-A CYT-1 and isoform JM-B CYT-1 are expressed in cerebellum, but only the isoform JM-B is expressed in the heart | |
E_B4 (C-term) - Related products
AP3122a: Phospho-HER4-Y1162 Antibody
AP3124a: Phospho-HER4-Y1188 Antibody
RI11826: ERBB4 predesign siRNA
BP3122a: Phospho-HER4-Y1162 Antibody Blocking Peptide
BP3124a: Phospho-HER4-Y1188 Antibody Blocking Peptide
BP7631a: ErbB4 Antibody (N-term) Blocking Peptide
BP7631b: ErbB4 Antibody (C-term) Blocking Peptide
AJ1342a: HER4 (ErbB4) Antibody
AJ1342b: HER4 (ErbB4) Antibody (C-term)
AJ1342c: HER4 (ErbB4) Antibody Phospho (pY1162)
AJ1342d: HER4 (ErbB4) Antibody Phospho (pY1188)
E_B4 (C-term) - Application data
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Western blot analysis of anti-ErbB4 Pab (Cat. #AP7631b) in T-47D cell lysate. ErbB4 (arrow) was detected using purified Pab. Secondary HRP-anti-rabbit was used for signal visualization with chemiluminescence.
E_B4 (C-term) - Research Areas
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BACKGROUND
Protein kinases are enzymes that transfer a phosphate group from a phosphate donor, generally the g phosphate of ATP, onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. With more than 500 gene products, the protein kinase family is one of the largest families of proteins in eukaryotes. The family has been classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/threonine (STK) kinase catalytic domains.
REFERENCES
Cheng, Q.C., et al., J. Biol. Chem. 278(40):38421-38427 (2003). Komuro, A., et al., J. Biol. Chem. 278(35):33334-33341 (2003). Williams, E.E., et al., Cancer Lett. 192(1):67-74 (2003). Thomas, C.Y., et al., Int. J. Cancer 104(1):19-27 (2003). Ni, C.Y., et al., J. Biol. Chem. 278(7):4561-4565 (2003).
