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Key Documents

C3470

Sigma-Aldrich

Anti-Connexin-32 (265-279) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-CMTX, Anti-CMTX1, Anti-CX32

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About This Item

MDL number:
MFCD01633267
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

200

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 27 kDa

species reactivity

mouse, human, rat

technique(s)

immunohistochemistry (frozen sections): 1:600 using rat liver tissue
microarray: suitable
western blot: 1:600 using a rat liver membrane preparation

UniProt accession no.

P08034

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... GJB1(2705)
mouse ... Gjb1(14618)
rat ... Gjb1(29584)

General description

Connexins (Cx) are a multi-gene family of highly related proteins with molecular weights ranging from 26 to 70 kD. 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. Anti-Connexin 32 is developed in rabbit using synthetic peptide Lys- Arg- Ser-Pro- Gly- Thr- Gly- Ala-Gly- Leu- Ala- Glu- Lys-Ser- Asp- Arg conjugated to KLH with glutaraldehyde as immunogen.
Gap junction protein, connexin-32 (Cx32) is encoded by gap junction protein β 1 (GJB1) gene, localized on the human chromosome X. This gene is expressed in the central nervous system (CNS) in oligodendrocytes and other neuronal populations.

Immunogen

synthetic human/rat connexin-32 peptide (amino acids 265-279 with an N-terminally added lysine).

Application

Anti-Connexin-32 (265-279) antibody produced in rabbit has been used in western blot analysis and immunocytochemistry.

Biochem/physiol Actions

Mutations of the gap junction protein β 1 (GJB1) gene results in the X-linked form of Charcot-Marie-tooth disease (CMTX1). Cx32 participates in the liver regeneration after partial hepatectomy.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin with 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Cx32 hemichannel opening by cytosolic Ca2+ is inhibited by the R220X mutation that causes Charcot-Marie-Tooth disease
Carrer A, et al.
Human Molecular Genetics, 27(1), 80-94 (2017)
Epidermal growth factor regulates connexin 43 in the human epididymis: role of gap junctions in azoospermia
Dube E, et al.
Human Reproduction, 27(8), 2285-2296 (2012)
Michael K G Stewart et al.
PloS one, 11(4), e0154162-e0154162 (2016-04-23)
Pannexin1 (Panx1) subunits oligomerize to form large-pore channels between the intracellular and extracellular milieu that have been shown to regulate proliferation, differentiation and cell death mechanisms. These key cellular responses are ultimately necessary for normal tissue development and function but
An 8-generation family with X-linked Charcot-Marie-Tooth: Confirmation Of the pathogenicity Of a 3? untranslated region mutation in GJB1 and its clinical features
Chen DH, et al.
Muscle and Nerve, 57(5), 859-862 (2018)
Six novel connexin32 (GJB1) mutations in X-linked Charcot-Marie-Tooth disease
Lee MJ, et al.
Journal of Neurology, Neurosurgery, and Psychiatry, 73(3), 304-306 (2002)
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