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HCK Antibody
HCK Antibody
- 中文名称：
- HCK Antibody
- 英文名称：
- HCK Antibody
- 品牌：
- AAA Biotech
- 品牌介绍：
- AAA Biotech专注于为全球生命科学研究提供高品质的蛋白质研究工具，核心产品包括经严格验证的抗体、重组蛋白及ELISA试剂盒。
- 货号：
- AAA326568
- 规格：
- 0.1 mL|0.2 mL|2x0.2 mL|3x0.2 mL|4x0.2 mL
- 保存建议：
- 收到后，可在-20摄氏度储存12个月。
- 货期：
- 6-8周
- 来源宿主：
- Rabbit
- 反应种属：
- Human, Mouse, Rat
- 应用：
- ELISA, IHC (Immunohistochemistry), WB (Western Blot)
- 免责声明：
- *本产品仅供科研实验使用，不得用于临床诊断。*
- 其他：
克隆性:Polyclonal
同型:IgG
克隆号:N/A
特异性:HCK antibody detects endogenous levels of total HCK
纯度:The antiserum was purified by peptide affinity chromatography using SulfoLink Coupling Resin.
形式：Liquid
Phosphate buffered saline, pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
浓度：1mg/ml
- 说明书：
Description: Hck (hemopoietic cell kinase) is a protein tyrosine kinase of the Src family prominently expressed in the lymphoid and myeloid lineages of hemopoiesis (1). It participates in transducing a variety of extracellular signals, which ultimately affect cellular processes including proliferation, differentiation and migration.The well-defined modular structure of Hck comprises a relatively divergent, NH2-terminal unique domain, which is subject to post-translational lipid modifications thereby targeting Hck to the plasma membrane. Src homology 3 (SH3) and 2 (SH2) domains, and a tyrosine kinase catalytic domain follow the unique domain. The catalytic activity of Hck is regulated, both positively and negatively, by tyrosine phosphorylation of highly conserved tyrosine (Y) residues. Phosphorylation of a single conserved Tyr499 residue in the COOH terminus of Hck by the protein kinase Csk renders Hck inactive as a result of an intramolecular interaction between the phosphorylated tyrosine (pY) residue and its own SH2 domain. Disruption of this interaction, either as a result of dephosphorylation, or substitution of the COOH-terminal regulatory Y residue with phenylalanine (F; e.g., HckY499F), or COOH-terminal truncation mutations as observed in the virally transduced v-Src oncoprotein, results in constitutive activation of Hck. In contrast to phosphorylation of the COOH-terminal regulatory tyrosine residue, autophosphorylation of a tyrosine residue (Tyr388) within the kinase domain of Hck acts to positively regulate its catalytic activity. Thus, activation of Hck requires both disruption of the COOH-terminal regulatory tyrosine-SH2 domain interaction and autophosphorylation of the regulatory tyrosine residue within the kinase domain (2, 3). The dysfunction or dysregulation of Hck may contribute to the pathogenesis of some human leukemias (4).
Function: Non-receptor tyrosine-protein kinase found in hematopoietic cells that transmits signals from cell surface receptors and plays an important role in the regulation of innate immune responses, including neutrophil, monocyte, macrophage and mast cell functions, phagocytosis, cell survival and proliferation, cell adhesion and migration. Acts downstream of receptors that bind the Fc region of immunoglobulins, such as FCGR1A and FCGR2A, but also CSF3R, PLAUR, the receptors for IFNG, IL2, IL6 and IL8, and integrins, such as ITGB1 and ITGB2. During the phagocytic process, mediates mobilization of secretory lysosomes, degranulation, and activation of NADPH oxidase to bring about the respiratory burst. Plays a role in the release of inflammatory molecules. Promotes reorganization of the actin cytoskeleton and actin polymerization, formation of podosomes and cell protrusions. Inhibits TP73-mediated transcription activation and TP73-mediated apoptosis. Phosphorylates CBL in response to activation of immunoglobulin gamma Fc region receptors. Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, GAB2, RAPGEF1, STAT5B, TP73, VAV1 and WAS.
Subunit Structure: Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Interacts with VAV1, WAS and RAPGEF1 (By similarity). Interacts (via SH3 domain) with HIV-1 Nef and Vif. This interaction stimulates its tyrosine-kinase activity. Interacts (via SH3 domain) with HEV ORF3 protein. Interacts with ARRB1 and ARRB2. Interacts with ADAM15. Interacts with FASLG. Interacts with CBL. Interacts with FCGR1A; the interaction may be indirect. Interacts with IL6ST. Interacts (via SH3 domain) with ELMO1. Interacts (via SH3 domain) with TP73. Interacts with YAP1. Interacts with ABL1 and ITGB1, and thereby recruits ABL1 to activated ITGB1. Interacts (via SH3 domain) with WDCP.
Post-translational Modifications: Phosphorylated on several tyrosine residues. Autophosphorylated. Becomes rapidly phosphorylated upon activation of the immunoglobulin receptors FCGR1A and FCGR2A. Phosphorylation by the BCR-ABL fusion protein mediates activation of HCK. Phosphorylation at Tyr-411 increases kinase activity. Phosphorylation at Tyr-522 inhibits kinase activity. Kinase activity is not required for phosphorylation at Tyr-522, suggesting that this site is a target of other kinases. Ubiquitinated by CBL, leading to its degradation via the proteasome. Isoform 2 palmitoylation at position 2 requires prior myristoylation. Palmitoylation at position 3 is required for caveolar localization of isoform 2.
Similarity: The SH3 domain mediates binding to HIV-1 Nef. Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.
