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Western blot analysis of pICIn on A431 lysate. Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000 dilution of pICIn.

HCT-8


BD Transduction Laboratories™ Purified Mouse Anti-pICIn

BD Transduction Laboratories™ Purified Mouse Anti-pICIn

Regulatory Status Legend
Any use of products other than the permitted use without the express written authorization of Becton, Dickinson and Company is strictly prohibited.
Preparation And Storage
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
pICln (I = current, Cl = chloride, n = nucleotide-sensitive) was initially described as an integral component of a nucleotide-sensitive chloride channel. However, it lacks homology to known channel proteins and exhibits cytoplasmic and nuclear localization. Thus, pICln is thought to be a cytosolic regulator of a swelling-induced chloride channel, rather than a component of a channel itself. In support of this hypothesis, pICln interacts with several cytosolic proteins. It binds to several Sm proteins, which are common spliceosomal core proteins whose assembly is necessary for the biogenesis of small nuclear ribonucleoproteins (snRNPs). Sm protein association with pICln inhibits their assembly. pICln also interacts with the 72 kDa human homolog of Skb1, a yeast protein that binds a homolog of p21[Cdc42/Rac]-activated protein kinases. In addition, pICln interacts with, and is phosphorylated by, a constitutively active cytosolic protein kinase. Therefore, pICln is thought to be a component of signaling pathways that function in transcriptional or translational regulation, cytoskeletal reorganization, or a number of other biological processes.
Development References (3)
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Krapivinsky G, Pu W, Wickman K, Krapivinsky L, Clapham DE. pICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology. J Biol Chem. 1998; 273(18):10811-10814. (Biology). View Reference
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Pu WT, Krapivinsky GB, Krapivinsky L, Clapham DE. pICln inhibits snRNP biogenesis by binding core spliceosomal proteins. Mol Cell Biol. 1999; 19(6):4113-4120. (Biology). View Reference
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Sanchez-Olea R, Emma F, Coghlan M, Strange K. Characterization of pICln phosphorylation state and a pICln-associated protein kinase. Biochim Biophys Acta. 1998; 1381(1):49-60. (Biology). View Reference
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For Research Use Only. Not for use in diagnostic or therapeutic procedures.