Recombinant Human Morc Family Cw-Type Zinc Finger Protein 3 (MORC3) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-02545P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) MORC3.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) MORC3.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) MORC3.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) MORC3.

Recombinant Human Morc Family Cw-Type Zinc Finger Protein 3 (MORC3) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-02545P
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Product Overview

Description Recombinant Human Morc Family Cw-Type Zinc Finger Protein 3 (MORC3) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb Q14149
Target Symbol MORC3
Synonyms KIAA0136; Microrchidia 3; MORC family CW type zinc finger 3; MORC family CW type zinc finger protein 3; MORC family CW-type zinc finger protein 3; MORC3; MORC3_HUMAN; Nuclear matrix protein 2; Nuclear matrix protein NXP2; NXP2; ZCW5; ZCWCC3; Zinc finger CW type coiled coil domain 3; Zinc finger CW type coiled coil domain protein 3; Zinc finger CW type with coiled coil domain 3; Zinc finger CW-type coiled-coil domain protein 3
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence MAAQPPRGIRLSALCPKFLHTNSTSHTWPFSAVAELIDNAYDPDVNAKQIWIDKTVINDHICLTFTDNGNGMTSDKLHKMLSFGFSDKVTMNGHVPVGLYGNGFKSGSMRLGKDAIVFTKNGESMSVGLLSQTYLEVIKAEHVVVPIVAFNKHRQMINLAESKASLAAILEHSLFSTEQKLLAELDAIIGKKGTRIIIWNLRSYKNATEFDFEKDKYDIRIPEDLDEITGKKGYKKQERMDQIAPESDYSLRAYCSILYLKPRMQIILRGQKVKTQLVSKSLAYIERDVY
Expression Range 1-290aa
Protein Length Partial
Mol. Weight 48.7kDa
Research Area Others
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Nuclear factor which forms MORC3-NBs (nuclear bodies) via an ATP-dependent mechanism. Sumoylated MORC3-NBs can also associate with PML-NBs. Recruits TP53 and SP100 to PML-NBs, thus regulating TP53 activity. Binds RNA in vitro. May be required for influenza A transcription during viral infection. Histone methylation reader which binds to non-methylated (H3K4me0), monomethylated (H3K4me1), dimethylated (H3K4me2) and trimethylated (H3K4me3) 'Lys-4' on histone H3. The order of binding preference is H3K4me3 > H3K4me2 > H3K4me1 > H3K4me0.
Subcellular Location Nucleus, nucleoplasm. Nucleus matrix. Nucleus, PML body.
Database References

HGNC: 23572

OMIM: 610078

KEGG: hsa:23515

STRING: 9606.ENSP00000383333

UniGene: PMID: 27653685

  • Dermatomyositis patients with anti-NXP-2 antibodies have a distinct and often severe systemic phenotype that includes myalgia, peripheral edema, and significant dysphagia, despite having milder inflammatory skin disease. PMID: 28129490
  • MORC3 has antiviral activity during herpes simplex virus 1 and human cytomegalovirus infections. PMID: 27440897
  • Case Report: manifestations of interstitial lung disease in adult dermatomyositis patient with anti-NPX2 autoantibodies. PMID: 26028648
  • Downregulation of NXP2/MORC3 by use of two independent short hairpin RNAs reduced virus titers in low-multiplicity infections. Analysis of viral RNA in high-multiplicity infections showed a reduction of viral RNA and mRNA after NXP2/MORC3 downregulation. PMID: 26202233
  • Case Report: Pemphigus foliaceus associated with anti-NXP2 autoantibody-positive amyopathic dermatomyositis. PMID: 24217940
  • These studies demonstrate that anti-NXP-2 and anti-TIF-1gamma antibodies are frequent DM specificities (found in 55% of patients) and are present in most patients with cancer-associated dermatomhyositis. PMID: 24037894
  • An anti-MJ antibody that recognizes NXP-2 was found to be a useful biomarker in dermatomyositis-polymyositis patients. PMID: 22546500
  • Anti-NXP2 Ab may be associated with adult idiopathic inflammatory myopathies with malignancy. PMID: 22258483
  • MORC3 colocalizes with PML by a two-step molecular mechanism. PMID: 20501696
  • determination of nuclear matrix-binding, RNA-binding, and coiled-coil domans PMID: 11927593
  • When tethered to a promoter by fusion to Gal4, NXP-2 repressed transcription, consistent with a role for NXP-2 in SUMO-mediated repression PMID: 16567619
  • MORC3 (microrchidia3)-ATPase activated p53 and induced cellular senescence in normal fibroblasts but not p53-/- fibroblasts PMID: 17332504
  • FAQs

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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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