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AB278660

FITC Anti-Lamin A + Lamin C (phospho S22) antibody [LaminACS22-CF12]

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(1 Publication)

Rabbit Recombinant Monoclonal Lamin-A/C phospho S22 antibody - conjugated to FITC. Suitable for Flow Cyt and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Synthetic Peptide within Human LMNA phospho S22.

View Alternative Names

LMN1, LMNA, Prelamin-A/C

1 Images
Flow Cytometry - FITC Anti-Lamin A + Lamin C (phospho S22) antibody [LaminACS22-CF12] (AB278660)
  • Flow Cyt

Supplier Data

Flow Cytometry - FITC Anti-Lamin A + Lamin C (phospho S22) antibody [LaminACS22-CF12] (AB278660)

Flow cytometric analysis of Hela cells untreated (red) or treated with nocadozole (green) using ab278660, or concentration-matched Rabbit (G9) mAb IgG Isotype Control (FITC Conjugate) for cells untreated (black) or treated with nocodazole (blue).

Key facts

Host species

Rabbit

Clonality

Monoclonal

Clone number

LaminACS22-CF12

Isotype

IgG

Light chain type

kappa

Conjugation

FITC

Excitation/Emission

Ex: 495nm, Em: 519nm

Carrier free

No

Reacts with

Human

Applications

Flow Cyt

applications

Immunogen

Synthetic Peptide within Human LMNA phospho S22. The exact immunogen used to generate this antibody is proprietary information.

P02545

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "FlowCyt" : {"fullname" : "Flow Cytometry", "shortname":"Flow Cyt"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "FlowCyt-species-checked": "testedAndGuaranteed", "FlowCyt-species-dilution-info": "5 µL for 10^6 Cells", "FlowCyt-species-notes": "<p></p>" } } }

Product details

What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:

  • - High batch-to-batch consistency and reproducibility
  • - Improved sensitivity and specificity
  • - Long-term security of supply
  • - Animal-free batch production

For more information, read more on recombinant antibodies.

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A/G
Storage buffer
Preservative: 0.09% Sodium azide Constituents: PBS, 0.2% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
+4°C
Storage information
Store in the dark

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Lamin A and Lamin C also known as lamin A/C are proteins encoded by the LMNA gene. These proteins are key components of the nuclear envelope where they provide structural support and maintain the shape of the nucleus. The lamin A/C molecule has a molecular weight of approximately 60-70 kDa. Expression of lamin A and lamin C occurs predominantly in differentiated cells where these proteins integrate into the nuclear lamina alongside other lamin molecules like lamin B. Lamin A alone sometimes referred to by designations like 4C11 plays a significant role in mechanical support at a molecular level.
Biological function summary

Lamin A/C proteins play a role in maintaining nuclear stability chromosome organization and gene regulation. They are part of a complex network within the nuclear lamina that includes interactions with proteins and DNA. Lamin A with a molecular weight distinct from other lamins participates in assembling this supportive matrix and contributes to DNA maintenance and repair processes. Their interaction with chromatin and gene expression regulation emphasizes their influence on important cellular functions.

Pathways

Lamin A/C proteins engage in the mechanosensory signaling and DNA damage response pathways. They interact with pathways involving the nuclear envelope structure and have connections to proteins like emerin and nuclear actin. Lamin A's role in these pathways supports its involvement in responding to mechanical stress and preserving genomic integrity highlighting its integration with these cellular processes.

Mutations in lamin A/C are linked to disorders such as Hutchinson-Gilford Progeria Syndrome and Emery-Dreifuss Muscular Dystrophy. These conditions highlight the importance of lamin A/C in cellular stability and nuclear integrity. Proteins such as emerin often relate to lamin A/C in these diseases as disruptions to their interactions can lead to compromised nuclear function and disease phenotypes.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Lamin-A/C. Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed : 10080180, PubMed : 10580070, PubMed : 10587585, PubMed : 10814726, PubMed : 11799477, PubMed : 12075506, PubMed : 12927431, PubMed : 15317753, PubMed : 18551513, PubMed : 18611980, PubMed : 2188730, PubMed : 22431096, PubMed : 2344612, PubMed : 23666920, PubMed : 24741066, PubMed : 31434876, PubMed : 31548606, PubMed : 37788673, PubMed : 37832547). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed : 10080180, PubMed : 10580070, PubMed : 10587585, PubMed : 10814726, PubMed : 11799477, PubMed : 12075506, PubMed : 12927431, PubMed : 15317753, PubMed : 18551513, PubMed : 18611980, PubMed : 22431096, PubMed : 23666920, PubMed : 24741066, PubMed : 31548606, PubMed : 37788673, PubMed : 37832547). Lamin A and C also regulate matrix stiffness by conferring nuclear mechanical properties (PubMed : 23990565, PubMed : 25127216). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed : 2188730, PubMed : 2344612). Lamin A and C are present in equal amounts in the lamina of mammals (PubMed : 10080180, PubMed : 10580070, PubMed : 10587585, PubMed : 10814726, PubMed : 11799477, PubMed : 12075506, PubMed : 12927431, PubMed : 15317753, PubMed : 18551513, PubMed : 18611980, PubMed : 22431096, PubMed : 23666920, PubMed : 31548606). Also invoved in DNA repair : recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (PubMed : 31548606). Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation (PubMed : 10080180, PubMed : 10814726, PubMed : 11799477, PubMed : 18551513, PubMed : 22431096). Required for osteoblastogenesis and bone formation (PubMed : 12075506, PubMed : 15317753, PubMed : 18611980). Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone (PubMed : 10587585). Required for cardiac homeostasis (PubMed : 10580070, PubMed : 12927431, PubMed : 18611980, PubMed : 23666920).. Prelamin-A/C. Prelamin-A/C can accelerate smooth muscle cell senescence (PubMed : 20458013). It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence (PubMed : 20458013).
See full target information LMNA phospho S22

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Experimental neurology 373:114656 PubMed38114054

2023

Intranasal administration of recombinant prosaposin attenuates neuronal apoptosis through GPR37/PI3K/Akt/ASK1 pathway in MCAO rats.

Applications

Unspecified application

Species

Unspecified reactive species

Jing Yu,Jinlan Li,Nathanael Matei,Wenna Wang,Lihui Tang,Jinwei Pang,Xue Li,Lili Fang,Jiping Tang,John H Zhang,Min Yan
View all publications

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