ESYT2 Knockout HEK293 Cell Line

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ESYT2 Knockout HEK293 Cell Line
Cat.No.:

EDC07553

Species:

Human

Cell Name:

HEK293

Gene:

ESYT2

Gene ID:

57488

Size:

1×10⁶cells

ESYT2 Knockout Cell Line (HEK293) 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. EDC07553
Product Name ESYT2 Knockout Cell Line (HEK293)
Cell Line HEK293
Cellosaurus ID CVCL_0045
Cell Line Synonyms Hek293, HEK-293, HEK/293, (HEK)293, HEK 293, HEK,293, 293, 293 HEK, 293 Ad5, Graham 293, Graham-293, Human Embryonic Kidney 293
Gene ESYT2
NCBI Gene ID
Gene Synonyms CHR2SYT|E-Syt2|FAM62B
Summary
Enables calcium ion binding activity; identical protein binding activity; and phospholipid binding activity. Predicted to be involved in endocytosis; endoplasmic reticulum-plasma membrane tethering; and lipid transport. Located in several cellular components, including cytoplasmic side of plasma membrane; endoplasmic reticulum membrane; and endoplasmic reticulum-plasma membrane contact site. [provided by Alliance of Genome Resources, Jul 2025]
Associated Diseases Non-tumor
Morphology Adherent
Passage Ratio 1/5，2days
Complete Culture Medium DMEM + 10% FBS
Freezing Medium 95% Complete culture medium+ 5% 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: HEK293		STR Info (Cell bank)
Cell Line: HEK293
Allele1Allele2Allele1Allele2
Amelogenin X X
CSF1P0 12 11 12
D2S1338 19 19
D3S1358 15 17 15 17
D5S818 8 8 9
D7S820 11 12 11 12
D8S1179 12 14 12 14
D13S317 12 14 12 14
D16S539 9 13 9 13
D18S51 17 18 17 18
D19S433 15 18 15 18
D21S11 28 30.2 28 30.2
FGA 23 23
Penta D 9 10 9 10
Penta E 7 15 7 15
TH01 7 9.3 7 9.3
TPOX 11 11
vWA 16 19 16 19
D6S1043 11 11
D12S391 19 21 11 15
D2S441 11 15 11 15
* 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.

FAQ

The choice depends on whether you are studying ESYT2's role as an ER-PM contact site tether or its functions in non-vesicular lipid transfer and calcium-regulated signaling. The Knockout line is the standard tool for asking whether ESYT2 is required for these processes — ESYT2 has been the most-characterized ESYT family member, mediating phospholipid transfer at ER-PM junctions and showing calcium-regulated tethering. Overexpression is useful for studying ESYT2 gain-of-function effects. Important consideration: ESYT1, ESYT3 paralog expression analysis aids interpretation given functional overlap. This product complements the parallel ESYT3 Knockout and the ESYT2 & ESYT3 Double Knockout in HEK293 (both also available) for paralog-specific functional dissection. Rescue with wild-type, SMP-domain-mutant (lipid-transfer-deficient), or C2-domain-mutant (PM-binding-deficient) ESYT2 enables structure-function studies.
Primary applications: • Calcium-regulated ER-PM tethering: ESYT2 calcium-regulated PM binding analysis through C2 domains. • Non-vesicular lipid transfer: glycerophospholipid transport quantification at ER-PM junctions. • PI(4,5)P2 dynamics: PIP2 replenishment at PM following stimulus-induced depletion. • Cross-paralog analysis: combined analysis with ESYT3 KO and ESYT2&ESYT3 Double KO for systematic ESYT family dissection. EDITGENE recommends this model for researchers investigating ESYT2 biology and ER-PM contact site lipid transfer.
Yes. ESYT2 rescue experiments require attention to ER-PM contact site architecture: • Construct design: use a codon-modified ESYT2 sequence with a small C-terminal tag (FLAG, HA). ESYT2 has the canonical ESYT architecture (ER hairpin, SMP domain, multiple C2 domains) — preserve all elements. • Calcium-binding-deficient rescue: C2 domain Ca²⁺-binding aspartate mutations affect calcium-regulated tethering. • Functional readout: rescue should restore ER-PM contact site formation and calcium-regulated lipid transfer. HEK293 transduces efficiently with lentivirus and supports stable rescue line generation.
* Research Use Disclaimer: Content is generated from publicly available research data, bioinformatic resources, and computational analyses for research reference only.

Related Publications

IF=15.7
Nature communications
ANO1 plays a crucial role in determining numerous physiological functions, including epithelial secretion, yet its regulatory mechanisms remain incompletely understood. Here, we describe a fundamental dynamic regulation of ANO1 surface expression and Ca-dependent gating via the cAMP/PKA pathway at the STIM1 ER/PM junctions. At these junctions, STIM1 assembles AC-AKAP-PKA complexes, while E-Syt1 mediates formation of ANO1-VAPA-IRBIT-E-Syt1-AC8-AKAP5-PKA complex, that phosphorylates ANO1 S673, increasing ANO1 Ca affinity. Within these complexes, the Ca and cAMP pathways act synergistically to enhance ANO1 function. By contrast, E-Syt2 dissociates the ANO1-VAPA interaction, forming ANO1-IRBIT-E-Syt2-AC6-AKAP11-PKA complex that phosphorylates ANO1 S221, which markedly reduces ANO1 Ca affinity. The effects of the E-Syts are primarily mediated by their reciprocal regulation of junctional PI(4)P, PI(4,5)P and PtdSer. Accordingly, IRBIT deletion in mice impairs receptor-stimulated activation of ANO1 and fluid secretion. These findings should have broad implications for ANO1 roles and functions across various tissues.
This KO model may be useful for: - Investigating the role of E-Syt2 in organizing cAMP/PKA signaling complexes at ER/PM junctions - Studying the regulation of Ca²⁺-dependent ion channels, specifically ANO1 (TMEM16A), by E-Syt-mediated membrane contact sites - Elucidating the reciprocal gating mechanisms between STIM1, E-Syt proteins, and ion channel activity - Functional dissection of E-Syt1 vs. E-Syt2 specificity in junctional signaling and calcium homeostasis - Exploring the interplay between lipid transfer and ion channel modulation at ER-plasma membrane contact sites

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