PPP1R14A pThr38 Rabbit Polyclonal Antibody
CAT#: AP20858PU-N
PPP1R14A pThr38 rabbit polyclonal antibody, Aff - Purified
Need it in bulk or conjugated?
Get a free quote
CNY 1,999.00
CNY 4,437.00
货期*
2周
规格
Specifications
Product Data | |
Applications | IHC, WB |
Recommend Dilution | Western blot: 1/500 - 1/1000. Immunohistochemistry on paraffin sections: 1/50 - 1/200. |
Reactivity | Human, Mouse, Rat |
Host | Rabbit |
Clonality | Polyclonal |
Specificity | This antibody detects endogenous levels of CPI-17 protein only when phosphorylated at Thr38. |
Formulation | Phosphate buffered saline (PBS), pH 7.2 State: Aff - Purified State: Liquid purified Ig fraction Preservative: 0.05% sodium azide |
Concentration | 1.0 mg/ml |
Purification | Affinity chromatography (> 95% (by SDS-PAGE) |
Conjugation | Unconjugated |
Storage Condition | Store undiluted at 2-8°C for one month or (in aliquots) at -20°C for longer. Avoid repeated freezing and thawing. |
Predicted Protein Size | ~ 22 kDa |
Gene Name | protein phosphatase 1 regulatory inhibitor subunit 14A |
Database Link | |
Background | CPI-17 is a phosphorylation-dependent inhibitory protein for smooth muscle Myosin phosphate. CPI-17 was originally identified as a 17 kDa PKC-potentiated inhibitory protein of protein phosphatase-1, which is dominantly expressed in smooth muscle. Phosphorylation at Threonin 38, in vitro, by PKC or Rho-kinase enhances the inhibitory potency toward myosin phosphatase. CPI-17 is also phosphorylated at Threonine 38 by protein kinase N and might be involved in the calcium sensitization of smooth muscle cont-raction as a downstream effector of Rho and/or arachidonic acid. CPI-17 is dually phosphorylated at Serine 12 and Threonine 38 by a MYPT-associated kinase, M110 kinase. |
Synonyms | Protein phosphatase 1 regulatory subunit 14A, CPI-17, CPI17, PPP1INL |
Reference Data | |
Protein Families | Druggable Genome |
Protein Pathways | Vascular smooth muscle contraction |
Documents
Product Manuals |
FAQs |
SDS |
Resources
抗体相关资料 |
其它PPP1R14A产品
Customer
Reviews
Loading...