XBP1 Knockout HeLa Cell Line

XBP1 Knockout HeLa Cell Line
Cat.No.:

EDJ-KQ20056

Species:

Human

Cell Name:

HeLa

Gene:

XBP1

Gene ID:

7494

Size:

1×10⁶cells

XBP1 Knockout Cell Line (Hela) is an exclusive upgraded CRISPR/Cas9 system-mediated gene knockout cell, with the advantages of Optimized Strategy Design, Efficient Cell Transfection, High-Performance Cas9 Protein and Hassle-Free Cell Selection.
Cat.No. EDJ-KQ20056
Product Name XBP1 Knockout Hela Cell Line
Cell Line Hela
Cellosaurus ID CVCL_0030
Cell Line Synonyms HELA, Hela, He La, He-La, HeLa-CCL2, Henrietta Lacks cells, Helacyton gartleri
Gene XBP1
NCBI Gene ID
Gene Synonyms TREB-5|TREB5|XBP-1|XBP2
Summary
This gene encodes a transcription factor that regulates MHC class II genes by binding to a promoter element referred to as an X box. This gene product is a bZIP protein, which was also identified as a cellular transcription factor that binds to an enhancer in the promoter of the T cell leukemia virus type 1 promoter. It may increase expression of viral proteins by acting as the DNA binding partner of a viral transactivator. It has been found that upon accumulation of unfolded proteins in the endoplasmic reticulum (ER), the mRNA of this gene is processed to an active form by an unconventional splicing mechanism that is mediated by the endonuclease inositol-requiring enzyme 1 (IRE1). The resulting loss of 26 nt from the spliced mRNA causes a frame-shift and an isoform XBP1(S), which is the functionally active transcription factor. The isoform encoded by the unspliced mRNA, XBP1(U), is constitutively expressed, and thought to function as a negative feedback regulator of XBP1(S), which shuts off transcription of target genes during the recovery phase of ER stress. A pseudogene of XBP1 has been identified and localized to chromosome 5. [provided by RefSeq, Jul 2008]
Associated Diseases Cervical Carcinoma
Morphology Adherent
Passage Ratio 1/5, 2days
Complete Culture Medium MEM + 10% FBS
Freezing Medium 70%Complete culture medium+ 20% FBS+ 10% DMSO
QC Indels validated by Sanger sequencing; sterility confirmed via microbial testing.
* For research use only. Not intended for use in humans or animals, including clinical, therapeutic, or diagnostic purposes.
LociSTR Info (Sample Cell)
Sample Cell Line: HeLa
STR Info (Cell bank)
Cell Line: HeLa
Allele1Allele2Allele1Allele2
Amelogenin X X
CSF1PO 9 10 9 10
D1S1656 12 15 12 15
D2S1338 17 17
D3S1358 15 18 15 18
D5S818 11 12 11 12
D6S1043 18 18
D7S820 8 12 8 12
D8S1179 12 13 12 13
D12S391 20 25 20 25
D13S317 12 14 12 14
D16S539 9 10 9 10
D18S51 16 16
D19S433 13 14 13 14
D21S11 27 28 27 28
FGA 18 21 18 21
Penta D 8 15 8 15
Penta E 7 17 7 17
TPOX 8 12 8 12
VWA 16 18 16 18
* STR authentication data of this cell line matches with that of cell lines sourced from ATCC, DSMZ, JCRB, and RIKEN databases.
Conclusion: The STR identification of this cell is correct.
* Research Use Disclaimer: Content is generated from publicly available research data, bioinformatic resources, and computational analyses for research reference only.

Related Publications

IF=16.6
Molecular cell
The tRNA ligase complex (tRNA-LC) splices precursor tRNAs (pre-tRNA), and Xbp1-mRNA during the unfolded protein response (UPR). In aerobic conditions, a cysteine residue bound to two metal ions in its ancient, catalytic subunit RTCB could make the tRNA-LC susceptible to oxidative inactivation. Here, we confirm this hypothesis and reveal a co-evolutionary association between the tRNA-LC and PYROXD1, a conserved and essential oxidoreductase. We reveal that PYROXD1 preserves the activity of the mammalian tRNA-LC in pre-tRNA splicing and UPR. PYROXD1 binds the tRNA-LC in the presence of NAD(P)H and converts RTCB-bound NAD(P)H into NAD(P), a typical oxidative co-enzyme. However, NAD(P) here acts as an antioxidant and protects the tRNA-LC from oxidative inactivation, which is dependent on copper ions. Genetic variants of PYROXD1 that cause human myopathies only partially support tRNA-LC activity. Thus, we establish the tRNA-LC as an oxidation-sensitive metalloenzyme, safeguarded by the flavoprotein PYROXD1 through an unexpected redox mechanism.
This KO model may be useful for: - Investigating the role of XBP1 in the unfolded protein response (UPR) and ER stress signaling - Studying the interplay between tRNA splicing, oxidative stress, and NAD(P)-dependent antioxidant mechanisms - Functional validation of PYROXD1-mediated pre-tRNA splicing in the context of XBP1 deficiency - Exploring compensatory pathways in UPR activation when XBP1 is absent - Screening for small molecules or genetic modifiers that modulate UPR or tRNA ligase activity in an XBP1-null background

Required Accessories

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