HCN1 pore, Human (Hyperpolarization-activated Cyclic Nucleotide-gated channel Pore) Control Peptide

Catalogue Number: H1827-31F-USB

Manufacturer:	United States Biological
Shelf Life:	12 months
Physical state:	Supplied as a liquid in PBS, pH 7.2
Type:	Control peptide
Host Cell:	Human synthetic peptide
Shipping Condition:	Blue Ice
Unit(s):	100 ug
Application:	ELISA, WB

Overview
Datasheets

Additional Text

Caution

FOR RESEARCH USE ONLY

Specificity

A 23-aa peptide sequence corresponding to the pore region of human HCN1 Biological rhythms (beating of the heart, circadian sleep cycles, respiration and the release of hormones) are necessary to sustain life. Heart beating is the most reliable and rhythmic biological phenomenon. Cardiac pacemaking is produced by the slow diastolic depolarization phase of the action potential. The hyperpolarization-activated cation current (termed If, Ih, or Iq) plays a key role in the in the initiation and modulation of cardiac and neuronal pacemaker depolarization. The generation of cardiac pacemaker potentials relies on a complex interplay between at least four different types of cation channels: T- and L-type Ca2+ channels, K+ channels and a cation channel termed If (synonymous names are Ih and Iq). The If channel has been designated as "pacemaker" channel because it reveals unique features that are believed to be a prerequisite for pacemaker activity. Recently, the hyperpolarization-activated cyclic nucleotide-gated families of ion channel proteins (HCN1-4) have been identified as the "pacemaker" channel. The amino acid sequences of HCNs predict a structure similar to that of voltage-gated (Kv) channels and cyclic nucleotide-gated (CNG) channels. HCNs proteins (HCN1-4) are characterized by six transmembrane domains (S1-S6), including a including a positively charged voltage-sensing S4 segment and an ion-conducting pore between S5 and S6. In the C terminus the HCNs carry a cyclic nucleotide-binding domain (CNBD), a motif found in several cyclic nucleotide-binding proteins. The core region of HCNs channels (S1 to the C terminus of the CNBD) is highly conserved, whereas the cytoplasmic N and C-termini, vary considerably in their length and share only weak sequence homology. The functional HCN, like other members of the superfamily of voltage-gated cation channels, channels probably assemble into tetrameric complexes. HCN channels pass both Na+ and K+ with relative permeability ratio of ~0.15 to 0.25. The primary sequence of HCN pore region is clearly related to that of highly selective K+ channels. In contrast to nonselective CNG or Na+-channels, both K+ and HCN channels contain a GYG motif in the pore. By affecting the spatial coordination of the GYG sequence in the tetrameric channel complex, other channel domains could control the structural rigidity of the pore and thereby determine whether only K+ or also other monovalent are allowed to permeate.

Purification

Purified

H1827-31F Datasheet

Price

£387.00

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