ATP6AP2 Human
ATPase Transporting Lysosomal Accessory Protein 2 Human Recombinant
Cat. No.
BT22244
Source
Escherichia Coli.
Synonyms
Renin receptor, ATPase H(+)-transporting lysosomal accessory protein 2, ATPase H(+)-transporting lysosomal-interacting protein 2, ER-localized type I transmembrane adaptor, Embryonic liver differentiation factor 10, N14F, Renin/prorenin receptor, Vacuolar ATP synthase membrane sector-associated protein M8-9, ATP6M8-9, V-ATPase M8.9 subunit, ATP6AP2, ATP6IP2, CAPER, ELDF10, M8-9, MRXE, XMRE, XPDS, HT028, MRXSH, MSTP009, APT6M8-9.
Appearance
Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description
ATP6AP2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 296 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 33kDa (calculated).
Product Specs
Introduction
ATPase Transporting Lysosomal Accessory Protein 2 (ATP6AP2) plays a crucial role in the function of proton-translocating ATPases, which are essential for energy production, transport, and pH regulation within cells. This protein is a component of V-type ATPases, specifically interacting with their transmembrane proton-conducting region. Beyond its role in ATPase function, ATP6AP2 acts as a receptor for renin and prorenin, influencing cellular responses through the activation of ERK1 and ERK2 signaling pathways. Its presence is observed in various organs including the brain, heart, placenta, liver, kidney, and pancreas, while being minimally detectable in the lungs and skeletal muscles. Notably, ATP6AP2 is also found in vascular structures and syncytiotrophoblast cells of the placenta during pregnancy.
Description
Recombinant human ATP6AP2, expressed in E. coli, is available as a single, non-glycosylated polypeptide chain. This protein consists of 296 amino acids, including a 10 amino acid N-terminal His-tag, resulting in a calculated molecular mass of 33 kDa.
Physical Appearance
White, lyophilized powder after filtration.
Formulation
The ATP6AP2 protein has been filtered through a 0.4 μm filter and lyophilized from a solution containing 0.5 mg/ml protein in 20 mM Tris buffer with 50 mM NaCl at pH 7.5.
Solubility
To create a working stock solution, add deionized water to the lyophilized powder to achieve a concentration of approximately 0.5 mg/ml. Allow the pellet to dissolve completely. It is essential to note that this product is not sterile. Before use in cell culture, ensure to filter the solution through an appropriate sterile filter.
Stability
The lyophilized protein should be stored at -20°C. After reconstitution, aliquot the product to prevent repeated freeze-thaw cycles. The reconstituted protein is stable at 4°C for a limited time and has been observed to remain stable for up to two weeks when stored at 4°C.
Purity
The purity of this product is greater than 90.0% as determined by SDS-PAGE analysis.
Synonyms
Renin receptor, ATPase H(+)-transporting lysosomal accessory protein 2, ATPase H(+)-transporting lysosomal-interacting protein 2, ER-localized type I transmembrane adaptor, Embryonic liver differentiation factor 10, N14F, Renin/prorenin receptor, Vacuolar ATP synthase membrane sector-associated protein M8-9, ATP6M8-9, V-ATPase M8.9 subunit, ATP6AP2, ATP6IP2, CAPER, ELDF10, M8-9, MRXE, XMRE, XPDS, HT028, MRXSH, MSTP009, APT6M8-9.
Source
Escherichia Coli.
Amino Acid Sequence
MKHHHHHHAS NEFSILKSPG SVVFRNGNWP IPGERIPDVA ALSMGFSVKE DLSWPGLAVG NLFHRPRATV MVMVKGVNKL ALPPGSVISY PLENAVPFSL DSVANSIHSL FSEETPVVLQ LAPSEERVYM VGKANSVFED LSVTLRQLRN RLFQENSVLS SLPLNSLSRN NEVDLLFLSE LQVLHDISSL LSRHKHLAKD HSPDLYSLEL AGLDEIGKRY GEDSEQFRDA SKILVDALQK FADDMYSLYG GNAVVELVTV KSFDTSLIRK TRTILEAKQA KNPASPYNLA YKYNFE.
Product Science Overview
Structure and Function
ATP6AP2 is a transmembrane protein that plays a crucial role as an accessory component of the vacuolar ATPase (V-ATPase). V-ATPases are essential for the acidification of intracellular compartments, which is vital for various cellular processes, including protein degradation, receptor-mediated endocytosis, and autophagy . The protein has a calculated molecular mass of approximately 39 kDa and contains an N-terminal hydrophobic signal sequence, a C-terminal transmembrane region, and several putative phosphorylation sites .
Biological Roles
- Lysosomal Degradation and Autophagy: ATP6AP2 is essential for the proper functioning of lysosomal degradative processes and autophagy. It helps maintain intracellular pH homeostasis by facilitating proton transport across lysosomal membranes .
- Renin-Angiotensin System: ATP6AP2 acts as a receptor for renin and prorenin, playing a role in the renin-angiotensin system, which regulates blood pressure and fluid balance .
- WNT Signaling: The protein is also involved in WNT signaling, a pathway crucial for cell proliferation, differentiation, and migration .
Expression Patterns
ATP6AP2 is expressed in various tissues, with the highest levels observed in the brain, heart, and placenta. Intermediate expression levels are found in the kidney and pancreas, while lower levels are present in the lung and skeletal muscle . In the kidney, ATP6AP2 localizes to glomeruli and vascular structures, whereas in the heart, it is found in coronary arteries .
Clinical Significance
Mutations or dysregulation of the ATP6AP2 gene have been associated with several disorders, including:
- Parkinsonism with Spasticity, X-Linked: A neurodegenerative disorder characterized by parkinsonian features and spasticity .
- Congenital Disorder of Glycosylation, Type IIr: A metabolic disorder affecting glycosylation processes .
- Intellectual Developmental Disorder, X-Linked Syndromic, Hedera Type: A condition involving intellectual disability and other syndromic features .
Research and Therapeutic Potential
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