2μg（R: reducing conditions）
Human Progranulin Protein, His tag
Human Progranulin Protein, His tag
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Product Details
Product Details
Product Specification
| Species | Human |
| Synonyms | PGRN, Acrogranin, Epithelin precursor, Glycoprotein of 88 Kda (GP88; Glycoprotein 88), Granulin precursor, PC cell-derived growth factor (PCDGF), Proepithelin (PEPI), GRN |
| Accession | P28799 |
| Amino Acid Sequence | Protein sequence (P28799, Thr18-Leu593, with C-His tag) TRCPDGQFCPVACCLDPGGASYSCCRPLLDKWPTTLSRHLGGPCQVDAHCSAGHSCIFTVSGTSSCCPFPEAVACGDGHHCCPRGFHCSADGRSCFQRSGNNSVGAIQCPDSQFECPDFSTCCVMVDGSWGCCPMPQASCCEDRVHCCPHGAFCDLVHTRCITPTGTHPLAKKLPAQRTNRAVALSSSVMCPDARSRCPDGSTCCELPSGKYGCCPMPNATCCSDHLHCCPQDTVCDLIQSKCLSKENATTDLLTKLPAHTVGDVKCDMEVSCPDGYTCCRLQSGAWGCCPFTQAVCCEDHIHCCPAGFTCDTQKGTCEQGPHQVPWMEKAPAHLSLPDPQALKRDVPCDNVSSCPSSDTCCQLTSGEWGCCPIPEAVCCSDHQHCCPQGYTCVAEGQCQRGSEIVAGLEKMPARRASLSHPRDIGCDQHTSCPVGQTCCPSLGGSWACCQLPHAVCCEDRQHCCPAGYTCNVKARSCEKEVVSAQPATFLARSPHVGVKDVECGEGHFCHDNQTCCRDNRQGWACCPYRQGVCCADRRHCCPAGFRCAARGTKCLRREAPRWDAPLRDPALRQLL |
| Expression System | HEK293 |
| Molecular Weight | Predicted MW: 63.5 kDa Observed MW: 90 kDa |
| Purity | ＞95% by SDS-PAGE |
| Endotoxin | <0.1EU/μg |
| Conjugation | Unconjugated |
| Tag | with C-His tag |
| Physical Appearance | Lyophilized Powder |
| Storage Buffer | Lyophilized from a 0.2 μm filtered solution of 0.2M PBS, pH7.4. |
| Reconstitution | Reconstitute no more than 1 mg/mL according to the size in deionized water after rapid centrifugation. |
| Stability & Storage | 12 months from date of receipt, -20 to -70 °C as supplied. |
Background
Granulin is a protein that in humans is encoded by the GRN gene. Each granulin protein is cleaved from the precursor progranulin, a 593 amino-acid-long and 68.5 kDa protein. Both forms of the protein have been implicated in development, inflammation, cell proliferation and protein homeostasis. Cleavage of progranulin produces a variety of active 6 kDa granulin peptides. Cleavage of progranulin into granulin occurs either in the extracellular matrix or the lysosome. Elastase, proteinase 3 and matrix metalloproteinase are proteases capable of cleaving progranulin into individual granulin peptides. While progranulin is associated with anti-inflammation, cleaved granulin peptides have been implicated in pro-inflammatory behavior.
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