深圳欣博盛生物科技有限公司

Connexin 43 antibody

gap junction protein alpha 1 , AVSD3 , CMDR , CX43 , EKVP , EKVP3 , GJAL , HLHS1 , HSS , ODDD , PPKCA

Chicken, Hamster, Human, Mouse, Rat

Rabbit

ICC/IF, IHC-Fr, IHC-P, WB

Anti-Connexin 43 reacts specifically with connexin 43. By immunoblotting, the antibody detects a single band or 2-3 bands at 43 kDa region. Staining of connexin 43 band(s) by immunoblotting is specifically inhibited with the connexin 43 peptide (amino acid residues 363-382). Reactivity has been observed with human, bovine, rat, mouse, hamster and chicken connexin 43.

IgG

synthetic peptide corresponding to the C-terminal segment of the cytoplasmic domain (amino acids 363-382 with N-terminally added lysine) of human/rat connexin-43.

Polyclonal

Purified by affinity chromatography

Unconjugated

Batch dependent (Please refer to the vial label for the specific concentration.)

Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.

4°C

43

Liquid

PBS, 1% BSA, 15mM Sodium azide.

GeneTex

Gap junctions are aggregations of intercellular channels, which directly connect the cytoplasm of adjacent cells. Gap junctions coordinate cellular and organ function in tissues and are involved in metabolic cooperation between cells, synchronization of cellular physiological activities, growth control, and developmental regulation. The gap junction channels allow intercellular exchange of ions, nucleotides, and small molecules between adjacent cells. Unlike other membrane channels, intercellular channels span two plasma membranes and require the contribution of hemi-channels, called connexons, from both participating cells. These channels accommodate molecules as large as 1 kDa. They have been detected in virtually every cell type in mammals, except mature skeletal muscle, spermatozoa, and erythrocytes. Two connexons interact in the extracellular space to form the complete intercellular channel. Each connexon is composed of six similar or identical proteins, which have been termed connexins. Connexins (Cx) are a multi-gene family of highly related proteins with molecular weights between 26 and 70 kDa. At least a dozen distinct connexin genes have been identified; many of them expressed in a tissue-specific manner. Two distinct lineages have been identified in mammals. One termed class I or beta group consists of Cx26, Cx30, Cx31, Cx31.1, and Cx32. The other, termed class II or alpha group, is represented by Cx33, Cx37, Cx40, Cx43 and Cx46. All of the connexins share a common membrane topology but differ in their conductance and channel gating properties. The structure of connexin molecules includes a cytoplasmic N-terminal region, four transmembrane domains, two extracellular loops, and a C-terminal cytoplasmic tail of varying length. The various connexins are highly conserved in the transmembrane and extracellular regions, but they differ in their cytoplasmic domain. The 43 kDa connexin protein (connexin 43, Cx43) belongs to the alpha type (group II) subfamily of connexin proteins. It is expressed in most tissues, even though the pattern of expression may differ in various cell types. For example, in the brain it is found in astrocytes, ependyma and leptomeninges but not in neurons, oligodendrocytes and pinealocytes; in the liver it is present in Ito cells but not hepatocytes. Gap junction protein levels change in response to disruption of tissue architecture. For instance, an increased expression of Cx43 was found in early stages of atherosclerosis. Changes in the levels or types of connexin expressed in a given cell type have been found to correlate with tumor progression and metastasis. However, glioma cells transfected with the oncogene neu (c-erb-B2) have been shown to exhibit a major reduction in intercellular communication with no decrease in overall expression of Cx43. Monoclonal antibodies reacting specifically with Cx43 may be applied in diverse cellular and molecular approaches to study gap junctions and their properties. They can also be used to correlate their expression pattern with physiological functions or pathological conditions.