ATP2C1, Polyclonal Antibody

Calcium-transporting ATPase type 2C member 1; ATPase 2C1; ATP-dependent Ca(2+) pump PMR1; ATP2C1; KIAA1347; PMR1L

For Research Use Only. Not for use in diagnostic procedures.

Polyclonal

Rabbit Ig

Rabbit

This ATP2C1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 882-909 amino acids from the C-terminal region of human ATP2C1.

Peptide Affinity Purified Rabbit Polyclonal Antibody (Pab)

Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.

Vial Concentration: 0.5 (lot specific)

Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C in small aliquots to prevent freeze-thaw cycles.

Small volumes of anti-ATP2C1 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

The protein encoded by this gene belongs to the family of
P-type cation transport ATPases. This magnesium-dependent enzyme
catalyzes the hydrolysis of ATP coupled with the transport of the
calcium. Defects in this gene cause Hailey-Hailey disease, an
autosomal dominant disorder. Alternatively spliced transcript
variants encoding different isoforms have been identified.

Metabolism; Signal Transduction

Western Blot (WB), ELISA (EIA)

WB~~1:1000

ATP2C1 Antibody (C-term) western blot analysis in T47D cell line lysates (35ug/lane).This demonstrates the ATP2C1 antibody detected the ATP2C1 protein (arrow).

100577

ATPase, Ca++ transporting, type 2C, member 1

calcium-transporting ATPase type 2C member 1

Calcium-transporting ATPase type 2C member 1

KIAA1347; PMR1L; ATPase 2C1  [Similar Products]

AT2C1_HUMAN

The protein encoded by this gene belongs to the family of P-type cation transport ATPases. This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium ions. Defects in this gene cause Hailey-Hailey disease, an autosomal dominant disorder. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Aug 2011]

ATP2C1: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of the calcium. Defects in ATP2C1 are the cause of Hailey-Hailey disease (HHD); also known as benign familial pemphigus. HHD is an autosomal dominant disorder characterized by persistent blisters and suprabasal cell separation (acantholysis) of the epidermis, due to impaired keratinocyte adhesion. Patients lacking all isoforms except isoform 2 have HHD. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIA subfamily. 6 isoforms of the human protein are produced by alternative splicing.

Protein type: Transporter, ion channel; Hydrolase; Membrane protein, multi-pass; EC 3.6.3.8; Transporter; Membrane protein, integral

Chromosomal Location of Human Ortholog: 3q22.1

Cellular Component: Golgi membrane; Golgi apparatus; membrane; integral to membrane; trans-Golgi network

Molecular Function: manganese-transporting ATPase activity; signal transducer activity; calcium-transporting ATPase activity; manganese ion binding; metal ion binding; calcium ion binding; ATP binding

Biological Process: cellular calcium ion homeostasis; Golgi calcium ion homeostasis; epidermis development; positive regulation of I-kappaB kinase/NF-kappaB cascade; metabolic process; calcium ion transport; calcium-dependent cell-cell adhesion; actin cytoskeleton reorganization; manganese ion transport; cellular manganese ion homeostasis; signal transduction; Golgi calcium ion transport; transmembrane transport

Disease: Benign Chronic Pemphigus

Baron, S., et al. Biochim. Biophys. Acta 1798(8):1512-1521(2010)
Davila, S., et al. Genes Immun. 11(3):232-238(2010)
Tian, H., et al. J. Dermatol. Sci. 58(1):80-82(2010)
Ding, Y.G., et al. Clin. Exp. Dermatol. 34 (8), E968-E971 (2009) :
Nechama, M., et al. BMC Cell Biol. 10, 70 (2009) :

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