• Various whole cell lysates were separated by 10% SDS-PAGE, and the membrane was blotted with anti-Lamin A/C (Phospho-Ser392) (PTR1133) antibody. The HRP-conjugated Goat anti- mouse IgG (H + L) antibody was used to detect the antibody. Lane 1: A431 Lane 2: Hela Lane 3: HEK293Predicted band size: 63, 74kDaObserved band size: 63, 74kDa
  • Various whole cell lysates were separated by 10% SDS-PAGE, and the membrane was blotted with anti-Lamin A/C (Phospho-Ser392) (PTR1133) antibody. The HRP-conjugated Goat anti- mouse IgG (H + L) antibody was used to detect the antibody. Lane 1: A549 Lane 2: LN18Predicted band size: 63, 74kDaObserved band size: 63, 74kDa
  • Various whole cell lysates were separated by 10% SDS-PAGE, and the membrane was blotted with anti-Lamin A/C (Phospho-Ser392) (PTR1133) antibody. The HRP-conjugated Goat anti- mouse IgG (H + L) antibody was used to detect the antibody. Lane 1: HepG2 Lane 2: NIH-3T3Predicted band size: 63, 74kDaObserved band size: 63, 74kDa

Anti-Phospho-LMNA-Ser392 antibody (350-450) [PTR1133] (STJA0006224)

SKU:
STJA0006224

Current Stock:
Host: Mouse
Applications: WB/ELISA
Reactivity: Human/Mouse/Rat
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Mouse monoclonal antibody anti-Phospho-Prelamin-A/C-Ser392 (350-450) is suitable for use in Western Blot and ELISA research applications.
Clonality: Monoclonal
Clone ID: PTR1133
Conjugation: Unconjugated
Isotype: IgG1k
Formulation: Liquid in PBS containing 50% Glycerol and 0.05% Proclin 300.
Purification: The antibody was purified using affinity-chromatography using specific immunogen.
Concentration: 1 mg/mL
Dilution Range: WB 1:500-2000
Storage Instruction: Store at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles.
Gene Symbol: LMNA
Gene ID: 4000
Uniprot ID: LMNA_HUMAN
Immunogen Region: 350-450
Specificity: This antibody detects endogenous levels of Lamin A/C (phospho Ser392) at Human, mouse, rat
Immunogen: Synthesized peptide derived from human protein. AA range: 350-450
Tissue Specificity In the arteries, prelamin-A/C accumulation is not observed in young healthy vessels but is prevalent in medial vascular smooth muscle cells (VSMCs) from aged individuals and in atherosclerotic lesions, where it often colocalizes with senescent and degenerate VSMCs. Prelamin-A/C expression increases with age and disease. In normal aging, the accumulation of prelamin-A/C is caused in part by the down-regulation of ZMPSTE24/FACE1 in response to oxidative stress.
Post Translational Modifications Proteolytic cleavage of the C-terminal of 18 residues of prelamin-A/C results in the production of lamin-A/C. The prelamin-A/C maturation pathway includes farnesylation of CAAX motif by protein farnesyltransferase (FNTA and FNTB), removal of the last three amino acids (-AAX) by RCE1/FACE2 and/or ZMPSTE24, methylation of the C-terminal cysteine by ICMT and endoproteolytic removal of the last 15 C-terminal amino acids by ZMPSTE24. Proteolytic cleavage requires prior farnesylation and methylation, and absence of these blocks cleavage. Farnesylation of prelamin-A/C facilitates nuclear envelope targeting. Increased phosphorylation of the lamins occurs before envelope disintegration and probably plays a role in regulating lamin associations. Phosphorylation status of S-22 determines its localization between double-strand break (DSB) sites and the nuclear matrix. Sumoylation is necessary for the localization to the nuclear envelope.
Function Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. Lamin A and C are present in equal amounts in the lamina of mammals. Recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends. Plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics. Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation. Required for osteoblastogenesis and bone formation. Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone. Required for cardiac homeostasis. Prelamin-A/C can accelerate smooth muscle cell senescence. It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence.
Protein Name Prelamin-A/C Cleaved Into - Lamin-A/C
70 Kda Lamin
Renal Carcinoma Antigen Ny-Ren-32
Database Links Reactome: R-HSA-1221632 P02545-2
Reactome: R-HSA-2980766
Reactome: R-HSA-2995383
Reactome: R-HSA-352238 P02545-1
Reactome: R-HSA-381038
Reactome: R-HSA-4419969
Reactome: R-HSA-6802952
Reactome: R-HSA-8862803 P02545-1
Cellular Localisation Nucleus
Nucleus Envelope
Nucleus Lamina
Nucleoplasm
Nucleus Matrix
Farnesylation Of Prelamin-A/C Facilitates Nuclear Envelope Targeting And Subsequent Cleavage By Zmpste24/Face1 To Remove The Farnesyl Group Produces Mature Lamin-A/C
Which Can Then Be Inserted Into The Nuclear Lamina
Emd Is Required For Proper Localization Of Non-Farnesylated Prelamin-A/C
Isoform C: Nucleus Speckle
Alternative Antibody Names Anti-Prelamin-A/C Cleaved Into - Lamin-A/C antibody
Anti-70 Kda Lamin antibody
Anti-Renal Carcinoma Antigen Ny-Ren-32 antibody
Anti-LMNA antibody
Anti-LMN1 antibody

Information sourced from Uniprot.org

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