中文 
别名:RAF proto-oncogene serine/threonine-protein kinase, Proto-oncogene c-RAF, cRaf, Raf-1, RAF1, RAF应用:WB
反应种属:Human
规格：50μl/100μl
| Description |
|---|
| Raf-1 is a MAP kinase kinase kinase (MAP3K) which functions downstream of the Ras family of membrane associated GTPases to which it binds directly. Once activated Raf-1 can phosphorylate to activate the dual specificity protein kinases MEK1 and MEK2 which in turn phosphorylate to activate the serine/threonine specific protein kinases ERK1 and ERK2. Activated ERKs are pleiotropic effectors of cell physiology and play an important role in the control of gene expression involved in the cell division cycle, apoptosis, cell differentiation and cell migration. |
| Specification | |
|---|---|
| Aliases | RAF proto-oncogene serine/threonine-protein kinase, Proto-oncogene c-RAF, cRaf, Raf-1, RAF1, RAF |
| Entrez GeneID | 5894 |
| Swissprot | P04049 |
| WB Predicted band size | 73.1kDa |
| Host/Isotype | Rabbit IgG |
| Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| Species Reactivity | Human |
| Immunogen | This RAF1 Antibody is generated from rabbits immunized with a KLH conjugated synthetic phosphopeptide corresponding to amino acid residues surrounding S338 of human RAF1. |
| Formulation | Purified polyclonal antibody supplied in PBS with 0.05% sodium azide. This antibody is first purified by protein A affinity chromatography. Then, the antibody fraction is peptide affinity purified in a 2-step procedure with peptides. The antibody is eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS. |
| Application | |
|---|---|
| WB | 1/500-1/1000 |
 |
Dot blot analysis of anti-RAF1-pS338 Phospho-specific Pab (Cat.#P30192) on nitrocellulose membrane. 50ng of Phospho-peptide or Non Phospho-peptide per dot were adsorbed. Antibody working concentrations are 0.5ug per ml. |
本公司的所有产品仅用于科学研究或者工业应用等非医疗目的，不可用于人类或动物的临床诊断或治疗，非药用，非食用。
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本公司的所有产品仅用于科学研究或者工业应用等非医疗目的，不可用于人类或动物的临床诊断或治疗，非药用，非食用。
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