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CLNS1A HumanDescription:
Chloride Channel, Nucleotide-Sensitive, 1A Human Recombinant
CLNS1A, CLCI, ICLN, CLNS1B, Methylosome subunit pICln, Chloride channel, nucleotide sensitive 1A, Chloride conductance regulatory protein ICln, Chloride ion current inducer protein, Reticulocyte pICln.
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PRO-1277Price :
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CLIC4 HumanDescription:
Chloride Intracellular Channel 4 Human Recombinant
Chloride intracellular channel protein 4, Intracellular chloride ion channel protein p64H1, CLIC4, H1, huH1, p64H1, CLIC4L, MTCLIC, FLJ38640, DKFZp566G223.
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PRO-173Price :
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CLIC2 HumanDescription:
Chloride Intracellular Channel 2 Human Recombinant
Chloride intracellular channel protein 2, XAP121, CLIC2, CLIC2b, XAP121.
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PRO-198Price :
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CLIC1 HumanDescription:
Chloride Intracellular Channel 1 Human Recombinant
ACBP, ACBD1, CCK-RP, EP, CLIC1, G6, NCC27, Nuclear chloride ion channel 27, Chloride channel ABP, Regulatory nuclear chloride ion channel protein, hRNCC, Chloride intracellular channel protein 1.
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PRO-833Price :
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About CLIC / Chloride Intracellular Channel:
CLIC1 stands for chloride intracellular channel protein 1, which is a type of protein found within humans.
Chloride channels are a varied collection of proteins that are responsible for regulating critical cellular processes. Some of the processes that these proteins are responsible for include regulating the volume of calls, maintaining intracellular PH, transepithelial transport, and stabilizing the potential of the cell membrane.
CLIC Function
CLIC1 is a member of the protein family p64. This means that the protein principally localizes to the nucleus of the cell, exhibiting both plasma and nuclear membrane chloride ion channel activity.
Chloride Intracellular Channel Interactions
In terms of interaction, this protein has been proven to interact with TRAPPC2. For those whoa re unaware, TRAPPC2 stands for trafficking protein particle complex subunit 2. This protein is believed to be part of a big multisubunit complex that is involved in the fusing and targeting of endoplasmic reticulum-to-Golgi transport vesicles with their acceptor compartment.
CLIC Structure
CLICs have been proven to exist in both integral and soluble membrane forms.
CLIC1 can be interested in membranes, forming channels of chloride ion. The channel activity is dependent on the pH.
Inserting into the membrane appears to be redox-regulated and this may only happen under conditions of oxidation.
CLIC1 in the soluble form is structurally homologous and monomeric to the superfamily of glutathione S-transferase, with a redox-active site that resembles glutaredoxin.