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Product
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Cathepsin D, Human
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Cat#
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101-32-135A
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Sequence
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LVRIPLHKFT SIRRTMSEVG GSVEDLIAKG PVSKYSQAVP
AVTEGPIPEV LKNYMDAQYY
GEIGIGTPPQ CFTVVFDTGS SNLWVPSIHC
KLLDIACWIH HKYNSDKSST YVKNGTSFDI
HYGSGSLSGY LSQDTVSVPC
QSASSASALG GVKVERQVFG EATKQPGITF IAAKFDGILG
MAYPRISVNN
VLPVFDNLMQ QKLVDQNIFS FYLSRDPDAQ PGGELMLGGT
DSKYYKGSLS
YLNVTRKAYW QVHLDQVEVA SGLTLCKEGC EAIVDTGTSL
MVGPVDEVRE LQKAIGAVPL
IQGEYMIPCE KVSTLPAITL KLGGKGYKLS
PEDYTLKVSQ AGKTLCLSGF MGMDIPPPSG
PLWILGDVFI GRYYTVFDRD
NNRVGFAEAA RLHHHHHHHH HH
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Unit/Weight
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10 μg
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Unit Price
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$138.00
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Description
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Cathepsin D, also known as CTSD and CPSD, belongs to the peptidase A1 family. Cathepsin D is an aspartic protease that becomes activated at a pH of 5 in hepatocyte endosomes where it degrades insulin. In addition to low pH, activation of cathepsin D depends critically on protonation of its Asp active site residue. .Asp-protonation and low pH leads to a conformational switch in cathepsin-D where the N terminal segment of the protease moves out of the active site. Cathepsin D can be cleaved into the following 2 chains: cathepsin D light chain and cathepsin D heavy chain, which is expressed in the aorta extracellular space. Cathepsin D plays a role in antigen processing, cell proliferation and tissue renewal, and prohormone activation.
Recombinant Human Cathepsin D produced in CHO cells is a polypeptide chain containing 402 amino acids. A fully biologically active molecule, rh Cathepsin D has a molecular mass of 44 kDa analyzed by reducing SDS-PAGE and is obtained by chromatographic techniques at Pepmic.
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Molecular Weight
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44 kDa, observed by reducing SDS-PAGE.
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Purity
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> 95% as analyzed by SDS-PAGE.
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Storage
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Recombinant Human Cathepsin D remains stable up to 6 months at -20°C to -80°C from date of receipt under sterile conditions. Up to 3 months at -20°C to -80°C under sterile conditions after opening. Avoid repeated freeze-thaw cycles.
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