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ACP5 Human, His

Source: Sf9, Baculovirus cells.Sterile filtered colorless solution.Acid Phosphatase-5, also known as ACP5 is a member of the Purple acid phosphatase family. ACP5 is implicated in osteopontin as well as bone sialoprotein dephosphorylation. ACP5 expression appears to increase in certain pathological states for instance Gaucher & Hodgkin diseases, the hairy cell, the B-cell, as well as the T-cell leukemias.ACP5 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 310 amino acids (22-325 a.a) and having a molecular mass of 35.1kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions) .ACP5 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Product Specifications

Product Name Alternative

Acid Phosphatase 5, Tartrate Resistant, Tartrate-Resistant Acid ATPase, EC 3.1.3.2, TrATPase, SPENCDI, Tartrate-Resistant Acid Phosphatase Type 5, Tartrate-Resistant Acid Phosphatase, Type 5 Acid Phosphatase, TR-AP, TRAP, ACP5.

Applications

Functional Assay

Purification

Greater than 95.0% as determined by SDS-PAGE.

Components

ACP5 protein solution (0.5mg/mL) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Storage Conditions

Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA) .Avoid multiple freeze-thaw cycles.

Applications Notes

Specific activity is > 5,000 units/mg, and is defined as the amount of enzyme that hydrolyze 1.0 nmoles of p-nitrophenyl phosphate (pNPP) per minute at pH 5.0 at 37C.

Amino Acids

ATPALRFVAV GDWGGVPNAP FHTAREMANA KEIARTVQIL GADFILSLGD NFYFTGVQDI NDKRFQETFE DVFSDRSLRK VPWYVLAGNH DHLGNVSAQI AYSKISKRWN FPSPFYRLHF KIPQTNVSVA IFMLDTVTLC GNSDDFLSQQ PERPRDVKLA RTQLSWLKKQ LAAAREDYVL VAGHYPVWSI AEHGPTHCLV KQLRPLLATY GVTAYLCGHD HNLQYLQDEN GVGYVLSGAG NFMDPSKRHQ RKVPNGYLRF HYGTEDSLGG FAYVEISSKE MTVTYIEASG KSLFKTRLPR RARPHHHHHH.
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