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XBP1, Recombinant, Human, aa2-160, His-tag (X-box-binding Protein 1, XBP-1, Tax-responsive Element-binding Protein 5, TREB5, XBP2)

XBP1, Recombinant, Human, aa2-160, His-tag (X-box-binding Protein 1, XBP-1, Tax-responsive Element-binding Protein 5, TREB5, XBP2)

Cat no: 149772

Supplier: United States Biological
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X box binding protein 1 (XBP-1) is a key protein in the mammalian unfolded protein response (UPR) that protects the cell against the stress of malfolded proteins in the endoplasmic reticulum (ER). Upon sensing unfolded proteins, an ER transmembrane endonuclease and kinase termed IRE1p is activated and excises an intron from XBP-1 mRNA. The spliced XBP-1 mRNA results in a 371aa protein (XBP-1s) which is then translocated to the nucleus where it binds to the regulatory elements of downstream genes. Together with other UPR transcription factors such as ATF6, XBP-1 stimulates the production of ER stress proteins including the ER resident protein chaperones glucose regulated protein (GRP) 78 and GRP94. Source: Recombinant protein corresponding to human XBP1, fused to His-tag at N-terminal expressed in E.coli. Molecular Weight: ~25kD Applications: Suitable for use in ELISA and Western Blot. Other applications not tested. Recommended Dilution: Optimal dilutions to be determined by the researcher. Storage and Stability: Aliquot to avoid repeated freezing and thawing and store at -70 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Catalogue number: 149772
Size: 50ug
Form: Supplied as a liquid in 1X PBS, 0.1% SDS.
Purity: ~95%
References: 1. Yoshida H, Matsui T, Yamamoto T, et al. XBP1 mRNA is induced by ATF6 and spliced by IRE1p in response to ER stress to produce a highly active transcription factor. Cell 2001; 107:881-91. 2. Calfon M, Zeng H, Urano F, et al. IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 2002; 415:92-6. 3. Haze K, Yoshida H, Yanagi H, et al. Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic stress. Mol. Cell. Biol. 1999; 10:3787-99. 4.Little E, Ramakrishnan M, Roy B, et al. The glucose-regulated proteins (GRP78 and GRP94): functions, gene regulation, and applications. Crit. Rev. Eukaryot. Gene Expr. 1994; 4:1-18.

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