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Recombinant Mouse V-type proton ATPase subunit S1 (Atp6ap1), partial

Recombinant Mouse V-type proton ATPase subunit S1 (Atp6ap1), partial

Code
MSDS	MSDS Datasheet
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Source
Conjugate
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Target Background

Product Details

Abbreviation

Atp6ap1

Purity

>85% (SDS-PAGE)

Target Names

Atp6ap1

Uniprot NO.

Q9R1Q9

Alternative Names

Atp6ap1; Atp6ip1; Atp6s1; V-type proton ATPase subunit S1; V-ATPase subunit S1; Protein C7-1; V-ATPase Ac45 subunit; V-ATPase S1 accessory protein; Vacuolar proton pump subunit S1

Species

Mus musculus (Mouse)

Source

Yeast

Protein Length

Partial

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage Condition

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

Accessory subunit of the proton-transporting vacuolar (V)-ATPase protein pump, which is required for luminal acidification of secretory vesicles. Guides the V-type ATPase into specialized subcellular compartments, such as neuroendocrine regulated secretory vesicles or the ruffled border of the osteoclast, thereby regulating its activity. Involved in membrane trafficking and Ca(2+)-dependent membrane fusion. May play a role in the assembly of the V-type ATPase complex. In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation.

Gene References into Functions

The mitochondrial H(+)-ATP synthase, by coupling the Warburg effect to anabolic metabolism, enables de-differentiation during the reprogramming of somatic cells to induced pluripotent stem cells. PMID:23287468
The essential role of Ac45 in osteoclast-mediated extracellular acidification and protease exocytosis, as well as the ability of Ac45 to guide lysosomal intracellular trafficking to the ruffled border, is demonstrated. PMID:22467241
propose that, in addition to its canonical function in V-ATPase-mediated acidification, Ac45 plays versatile roles during osteoclast formation and function. PMID:22087256
These results suggest that a3 V-ATPase promotes distant metastasis of B16-F10 cells by creating acidic environments via proton secretion. PMID:21669964
A point mutation within the a3 subunit, R740S, which is dominant negative for proton pumping and bone resorption, also uncouples proton pumping from ATP hydrolysis. PMID:21305608
Disruption of vacuolar H+-ATPase a3-B2 subunit interaction inhibited osteoclast bone resorption. PMID:20837476
Targeted disruption of the gene for the chromaffin granular V-ATPase-associated protein Ac45 in embryonic stem cells affects the normal blastocyst development, suggesting an essential role for the V-ATPase in early embryonic development. [AC45] PMID:11989824
In osteoclasts, the activity-dependent accumulation of acids and Ca(2+) in the closed extracellular compartment might serve as negative feedback signals for regulating the V-ATPase. PMID:16901940
cytoplasmic terminus of Ac45 contains elements necessary for its proper interaction with V(0) domain and efficient osteoclastic bone resorption PMID:18227071
role for furin in regulated secretion, particularly in intragranular acidification most likely due to impaired processing of Ac45 PMID:18713856