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SAB4200172

Sigma-Aldrich

Anti-NEZHA (N-terminal) antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody

Synonym(s):

Anti-3 calmodulin-regulated spectrin-associated protein 3, Anti-KIAA154

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~150 kDa

species reactivity

human

concentration

~1.0 mg/mL

technique(s)

immunoprecipitation (IP): 2.5-5.0 μg using lysates of HEK-293T cells overexpressing human NEZHA.
western blot: 1-2 μg/mL using lysates of HEK-293T cells overexpressing human NEZHA.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... KIAA1543(57662)
mouse ... 2310057J16Rik(69697)
rat ... Camsap3(689074)

General description

Nezha (a deity in Chinese mythology), also known as KIAA1543 and calmodulin-regulated spectrin associated protein 3 (CAMSAP3) contains one calponin homology (CH) and two coiled coil (CC1 and 2) domains, as well as one DUF1781 (DUF) domain of unknown function. Nezha exists in the cells in two pools: junctional and cytoplasmic. This protein is known to be localized in the noncentrosomal microtubules. The NEZHA gene is mapped to human chromosome 19p13.2.

Specificity

Anti-NEZHA (N-terminal) recognizes human NEZHA.

Immunogen

synthetic peptide corresponding to the N- terminal region of human NEZHA, conjugated to KLH. The corresponding sequence is identical in mouse and rat.

Application

Anti-NEZHA (N-terminal) antibody produced in rabbit is suitable for immunoblotting and immunoprecipitation.

Biochem/physiol Actions

Nezha and its binding partner Pleckstrin homology domain containing A7 (PLEKHA7) are discovered as new proteins which are part of the cadherin-based protein complex in mammalian epithelial cells. This complex can anchor microtubule minus ends to the zonula adherens (ZA) and is necessary for the biogenesis of this specialized junction. The junctional Nezha is recruited to this site via its interaction with PLEKHA7. Reduction of Nezha is shown to disrupt the ZA, in vitro.

Physical form

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

Storage and Stability

For continuous use, store at 2-8 °C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing, orstorage in “frost-free” freezers,is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilutions should be discarded if not used within 12 hours.

Disclaimer

Unless otherwise stated in our catalog, 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

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
100M4864

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Jennifer B Permuth et al.
Human molecular genetics, 25(16), 3600-3612 (2016-07-06)
Rare and low frequency variants are not well covered in most germline genotyping arrays and are understudied in relation to epithelial ovarian cancer (EOC) risk. To address this gap, we used genotyping arrays targeting rarer protein-coding variation in 8,165 EOC
Anna Akhmanova et al.
Cell, 135(5), 791-793 (2008-12-02)
The zonula adherens (ZA) is a specialized cadherin-based structure found at the contacts between epithelial cells. Meng et al. (2008) now identify a protein complex containing the microtubule minus-end-binding protein Nezha, which provides a critical link between microtubules and cadherins
Wenxiang Meng et al.
Cell, 135(5), 948-959 (2008-12-02)
Epithelial cells contain noncentrosomal microtubules (MTs), whose minus ends are oriented apically. In contrast with the well-known interactions of the minus ends with the centrosome, little is known about the termination site of the noncentrosomal minus ends. Here we show

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