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KSR1 Antibody (N-term A7)
Purified Rabbit Polyclonal Antibody (Pab)
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Application 
| IHC-P, E |
|---|---|
| Primary Accession | Q8IVT5 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 102160 Da |
| Antigen Region | 1-30 aa |
| Gene ID | 8844 |
|---|---|
| Other Names | Kinase suppressor of Ras 1, KSR1, KSR |
| Target/Specificity | This KSR1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human KSR1. |
| Dilution | IHC-P~~1:50~100 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | KSR1 Antibody (N-term A7) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | KSR1 |
|---|---|
| Synonyms | KSR |
| Function | Part of a multiprotein signaling complex which promotes phosphorylation of Raf family members and activation of downstream MAP kinases (By similarity). Independently of its kinase activity, acts as MAP2K1/MEK1 and MAP2K2/MEK2-dependent allosteric activator of BRAF; upon binding to MAP2K1/MEK1 or MAP2K2/MEK2, dimerizes with BRAF and promotes BRAF-mediated phosphorylation of MAP2K1/MEK1 and/or MAP2K2/MEK2 (PubMed:29433126). Promotes activation of MAPK1 and/or MAPK3, both in response to EGF and to cAMP (By similarity). Its kinase activity is unsure (By similarity). Some protein kinase activity has been detected in vitro, however the physiological relevance of this activity is unknown (By similarity). |
| Cellular Location | Cytoplasm. Membrane; Peripheral membrane protein. Cell membrane {ECO:0000250|UniProtKB:Q61097}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q61097}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q61097}. Endoplasmic reticulum membrane. Note=In unstimulated cells, where the phosphorylated form is bound to a 14-3-3 protein, sequestration in the cytoplasm occurs. Following growth factor treatment, the protein is free for membrane translocation, and it moves from the cytoplasm to the cell periphery. |
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Provided below are standard protocols that you may find useful for product applications.
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. The STE group (homologs of yeast Sterile 7, 11, 20 kinases) consists of 50 kinases related to the mitogen-activated protein kinase (MAPK) cascade families (Ste7/MAP2K, Ste11/MAP3K, and Ste20/MAP4K). MAP kinase cascades, consisting of a MAPK and one or more upstream regulatory kinases (MAPKKs) have been best characterized in the yeast pheromone response pathway. Pheromones bind to Ste cell surface receptors and activate yeast MAPK pathway.
References
Blume-Jensen P, et al. Nature 2001. 411: 355.
Cantrell D, J. Cell Sci. 2001. 114: 1439.
Jhiang S Oncogene 2000. 19: 5590.
Manning G, et al. Science 2002. 298: 1912.
Moller, D, et al. Am. J. Physiol. 1994. 266: C351-C359.
Robertson, S. et al. Trends Genet. 2000. 16: 368.
Robinson D, et al. Oncogene 2000. 19: 5548.
Van der Ven, P, et al. Hum. Molec. Genet. 1993. 2: 1889.
Vanhaesebroeck, B, et al. Biochem. J. 2000. 346: 561.
Van Weering D, et al. Recent Results Cancer Res. 1998. 154: 271.
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