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Phospho-PKD2(Ser812) Antibody
Phospho-PKD2(Ser812) Antibody
- 中文名称：
- Phospho-PKD2(Ser812) Antibody
- 英文名称：
- Phospho-PKD2(Ser812) 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：
- AAA321297
- 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：
- 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:Phospho-PKD2(Ser812) antibody detects endogenous levels of PKD2.
纯度:From purified rabbit serum by affinity purification via sequential chromatography on phospho-and non-phospho-peptide affinity columns.
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：
Function: Functions as a cation channel involved in fluid-flow mechanosensation by the primary cilium in renal epithelium (PubMed:18695040). Functions as outward-rectifying K+ channel, but is also permeable to Ca2+, and to a much lesser degree also to Na+ (PubMed:11854751, PubMed:15692563, PubMed:27071085, PubMed:27991905). May contribute to the release of Ca2+ stores from the endoplasmic reticulum (PubMed:11854751, PubMed:20881056). Together with TRPV4, forms mechano-and thermosensitive channels in cilium (PubMed:18695040). PKD1 and PKD2 may function through a common signaling pathway that is necessary to maintain the normal, differentiated state of renal tubule cells. Acts as a regulator of cilium length, together with PKD1. The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling. The cilium length response creates a negative feedback loop whereby fluid shear-mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling. Also involved in left-right axis specification via its role in sensing nodal flow; forms a complex with PKD1L1 in cilia to facilitate flow detection in left-right patterning. Detection of asymmetric nodal flow gives rise to a Ca2+ signal that is required for normal, asymmetric expression of genes involved in the specification of body left-right laterality (By similarity).
Subunit Structure: Homotetramer (PubMed:20881056, PubMed:27768895, PubMed:27991905, PubMed:28092368). Interacts with PKD1, giving rise to a complex formed by one PKD1 chain and a PKD2 homooligomer (PubMed:20881056, PubMed:19556541). In vitro results suggest assembly of a complex composed of one PKD1 chain and a PKD2 trimer; the physiological significance of this is uncertain (PubMed:19556541). Isoform 1 interacts with PKD1 while isoform 3 does not (By similarity). Interacts with PKD1L1. PKD1 requires the presence of PKD2 for stable expression (By similarity). Interacts with CD2AP (PubMed:10913159). Interacts with HAX1 (PubMed:10760273). Interacts with NEK8 (By similarity). Part of a complex containing AKAP5, ADCY5, ADCY6 and PDE4C (By similarity). Interacts (via C-terminus) with TRPV4 (via C-terminus) (PubMed:18695040). Interacts (via C-terminal acidic region) with PACS1 and PACS2; these interactions retain the protein in the endoplasmic reticulum and prevent trafficking to the cell membrane (PubMed:15692563).
Post-translational Modifications: Phosphorylated. Phosphorylation is important for protein function; a mutant that lacks the N-terminal phosphorylation sites cannot complement a zebrafish pkd2-deficient mutant (PubMed:16551655). PKD-mediated phosphorylation at the C-terminus regulates its function in the release of Ca2+ stores from the endoplasmic reticulum (PubMed:20881056). PKA-mediated phosphorylation at a C-terminal site strongly increases the open probability of the channel, but does not increase single channel conductance (PubMed:26269590). N-glycosylated. The four subunits in a tetramer probably differ in the extent of glycosylation; simultaneous glycosylation of all experimentally validated sites would probably create steric hindrance. Thus, glycosylation at Asn-305 is not compatible with glycosylation at Asn-328; only one of these two residues is glycosylated at a given time.
Similarity: The C-terminal coiled-coil domain is involved in oligomerization and the interaction with PKD1 (PubMed:18694932, PubMed:19556541). The isolated coiled-coil domain forms a homotrimer in vitro; the homotrimer interacts with a single PKD1 chain (PubMed:19556541). The coiled-coil domain binds calcium and undergoes a calcium-induced conformation change (in vitro) (PubMed:18694932). Belongs to the polycystin family.
