ATPase, H+ Transporting, Lysosomal 42kDa, V1 Subunit C1 (ATP6V1C1) antibody

Antigen: ATPase, H+ Transporting, Lysosomal 42kDa, V1 Subunit C1 (ATP6V1C1)

Synonyms: VATC, Vma5, ATP6C, ATP6D, FLJ20057, U13839, 1700025B18Rik, MGC109315, vatC, MGC140015, MGC75601, DKFZp459P047

Clonality: Polyclonal

Host: Rabbit

Reactivity: Cow (Bovine), Human, Mouse (Murine), Rat (Rattus), Dog (Canine), Zebrafish, Xenopus laevis

Application: Western Blotting (WB)

Catalog no.: ABIN406715

Additional Information

Alternative name: ATP6V1C1

Gene ID: ATP6V1C1

UniProt: P21283

Immunogen: The immunogen for anti-ATP6V1C1 antibody: synthetic peptide directed towards the N terminal of human ATP6V1C1

Sequence: ldafvegvvkkvaqymadvledskdkvqenllangvdlvt yitrfqwdma

Cross-Reactivity: Cow (Bovine), Dog (Canine), Human, Mouse (Murine), Rat (Rattus)

Format: Lyophilized

Reconstitution: Add 50 µl of distilled water. Final anti-ATP6V1C1 antibody concentration is 1 mg/ml.

Description: ATP6V1C1 is a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of intracellular compartments of eukaryotic cells. V-ATPase dependent acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c'', and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This gene is one of two genes that encode the V1 domain C subunit proteins and is found ubiquitously. This C subunit is analogous but not homologous to gamma subunit of F-ATPases. Previously, this gene was designated ATP6D.This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of intracellular compartments of eukaryotic cells. V-ATPase dependent acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c'', and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This gene is one of two genes that encode the V1 domain C subunit proteins and is found ubiquitously. This C subunit is analogous but not homologous to gamma subunit of F-ATPases. Previously, this gene was designated ATP6D. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Characteristics: Antigen Size: 382 amino acids

Molecular Weight: 42kDa

Application Details

Application Notes: WB Suggested Anti-ATP6V1C1 Antibody Titration: 0.2-1 ug/ml
ELISA Titer: 1:312500
Positive Control: HepG2 cell lysate.

Purification: Affinity Purified

Buffer: PBS

Storage (Long Term): For longer periods of storage, store at -20°C. Avoid repeat freeze-thaw cycles.

Storage (Short Term): Any unfrozen and/or unused material can be stored at 4°C for short term use (< 1 week), and should not be re-frozen.

Research Area: Signaling, Metabolism

Restrictions: For Research Use only

Images

WB Suggested Anti-ATP6V1C1 Antibody Titration: 0.2-1 ug/ml
ELISA Titer: 1:312500
Positive Control: HepG2 cell lysate

Publications

Product: Hurtado-Lorenzo, Skinner, El Annan et al.: "V-ATPase interacts with ARNO and Arf6 in early endosomes and regulates the protein degradative pathway." in: Nature cell biology, Vol. 8, Issue 2, pp. 124-36, 2006 (PubMed).