Mouse Anti-MORC3 Recombinant Antibody (CBFYM-2473) (CBMAB-M2660-FY)

Name: Mouse Anti-MORC3 Recombinant Antibody (CBFYM-2473)
SKU: CBMAB-M2660-FY
Rating: 5 (1 reviews)

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Datasheet

SDS

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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Mouse

Clone

CBFYM-2473

Application

IF, WB

Immunogen

Recombinant human MORC3

Specificity

Human, Mouse, Rat

Antibody Isotype

IgG1

Clonality

Monoclonal

Application Notes

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format

Liquid

Concentration

1 mg/mL

Storage

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

More Infomation

Target

Full Name

MORC FAMILY CW-TYPE ZINC FINGER 3

Introduction

This gene encodes a protein that localizes to the nuclear matrix and forms nuclear bodies via an ATP-dependent mechanism. The protein is predicted to have coiled-coil and zinc finger domains and has RNA binding activity. Alternative splicing produces multiple transcript variants encoding distinct isoforms.

Entrez Gene ID

Human	23515
Mouse	338467
Rat	304074

UniProt ID

Human	Q14149
Mouse	F7BJB9
Rat	D4A552

Alternative Names

MORC Family CW-Type Zinc Finger 3; Zinc Finger CW-Type Coiled-Coil Domain Protein 3; Zinc Finger, CW Type With Coiled-Coil Domain 3; Nuclear Matrix Protein 2; ZCWCC3; NXP2

Function

Nuclear matrix protein which forms MORC3-NBs (nuclear bodies) via an ATP-dependent mechanism and plays a role in innate immunity by restricting different viruses through modulation of the IFN response (PubMed:27440897, PubMed:34759314).

Mechanistically, possesses a primary antiviral function through a MORC3-regulated element that activates IFNB1, and this function is guarded by a secondary IFN-repressing function (PubMed:34759314).

Sumoylated MORC3-NBs associates with PML-NBs and recruits TP53 and SP100, thus regulating TP53 activity (PubMed:17332504, PubMed:20501696).

Binds RNA in vitro (PubMed:11927593).

Histone methylation reader which binds to non-methylated (H3K4me0), monomethylated (H3K4me1), dimethylated (H3K4me2) and trimethylated (H3K4me3) 'Lys-4' on histone H3 (PubMed:26933034).

The order of binding preference is H3K4me3> H3K4me2> H3K4me1> H3K4me0 (PubMed:26933034).

(Microbial infection) May be required for influenza A transcription during viral infection (PubMed:26202233).

Biological Process

Cell aging Source: MGI
Maintenance of protein location in nucleus Source: MGI
Negative regulation of fibroblast proliferation Source: MGI
Peptidyl-serine phosphorylation Source: MGI
Post-embryonic development Source: Ensembl
Protein phosphorylation Source: MGI
Protein stabilization Source: MGI

Cellular Location

Nucleus
Nucleoplasm
Nucleus matrix
PML body
Other locations
Chromosome
Note: Also found in PML-independent nuclear bodies. Localization to nuclear bodies is ATP-dependent.

PTM

Sumoylation is involved in interaction with PML and localization to PML nuclear bodies.

Wang, L., Zheng, W., Lv, X., Song, Y., & Xu, T. (2023). circMORC3-encoded novel protein negatively regulates antiviral immunity through synergizing with host gene MORC3. Plos Pathogens, 19(12), e1011894.

Xue, Y., Wang, H., Tian, B., Wang, S., & Gao, X. J. (2023). Selenium deficiency promotes the expression of lncRNA-MORC3, activating NLRP3-caspase-1/IL-1β signaling to induce inflammatory damage and disrupt tight junctions in piglets. Biological Trace Element Research, 201(5), 2365-2376.

Ma, X. H., Yao, Y. X., Wang, X. Z., Zhou, Y. P., Huang, S. N., Li, D., ... & Yang, B. (2022). MORC3 restricts human cytomegalovirus infection by suppressing the major immediate‐early promoter activity. Journal of Medical Virology, 94(11), 5492-5506.

Gaidt, M. M., Morrow, A., Fairgrieve, M. R., Karr, J. P., Yosef, N., & Vance, R. E. (2021). Self-guarding of MORC3 enables virulence factor-triggered immunity. Nature, 600(7887), 138-142.

Groh, S., Milton, A. V., Marinelli, L. K., Sickinger, C. V., Russo, A., Bollig, H., ... & Schotta, G. (2021). Morc3 silences endogenous retroviruses by enabling Daxx-mediated histone H3. 3 incorporation. Nature communications, 12(1), 5996.

Desai, V. P., Chouaref, J., Wu, H., Pastor, W. A., Kan, R. L., Oey, H. M., ... & Daxinger, L. (2021). The role of MORC3 in silencing transposable elements in mouse embryonic stem cells. Epigenetics & chromatin, 14(1), 1-14.

Zhang, Y., Ahn, J., Green, K. J., Vann, K. R., Black, J., Brooke, C. B., & Kutateladze, T. G. (2019). MORC3 is a target of the influenza A viral protein NS1. Structure, 27(6), 1029-1033.

Zhang, Y., Klein, B. J., Cox, K. L., Bertulat, B., Tencer, A. H., Holden, M. R., ... & Kutateladze, T. G. (2019). Mechanism for autoinhibition and activation of the MORC3 ATPase. Proceedings of the National Academy of Sciences, 116(13), 6111-6119.

Zhang, Y., Bertulat, B., Tencer, A. H., Ren, X., Wright, G. M., Black, J., ... & Kutateladze, T. G. (2019). MORC3 forms nuclear condensates through phase separation. IScience, 17, 182-189.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

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