AFfirm™ Lamin A/C Mouse Monoclonal Antibody - #BF8946
製品説明
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
折りたたみ/展開
70 kDa lamin; Cardiomyopathy dilated 1A (autosomal dominant); CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL; FPLD; FPLD2; HGPS; IDC; Lamin A; Lamin A/C; Lamin A/C like 1; Lamin; Lamin C; Lamin-A/C; LDP1; LFP; LGMD1B; Limb girdle muscular dystrophy 1B (autosomal dominant); LMN 1; LMN A; LMN C; LMN1; LMNA; LMNA_HUMAN; LMNC; LMNL1; Prelamin A/C; PRO1; Renal carcinoma antigen NY REN 32; Renal carcinoma antigen NY-REN-32; Renal carcinoma antigen NYREN32;
免疫原
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.
- P02545 LMNA_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMGNWQIKRQNGDDPLLTYRFPPKFTLKAGQVVTIWAAGAGATHSPPTDLVWKAQNTWGCGNSLRTALINSTGEEVAMRKLVRSVTVVEDDEDEDGDDLLHHHHGSHCSSSGDPAEYNLRSRTVLCGTCGQPADKASASGSGAQVGGPISSGSSASSVTVTRSYRSVGGSGGGSFGDNLVTRSYLLGNSSPRTQSPQNCSIM
PTMs - P02545 基板として
Site | PTM Type | Enzyme | Source |
---|---|---|---|
M1 | Acetylation | Uniprot | |
T3 | Phosphorylation | Uniprot | |
S5 | Phosphorylation | Uniprot | |
T10 | Phosphorylation | Uniprot | |
S12 | Phosphorylation | Uniprot | |
S17 | Phosphorylation | Uniprot | |
S18 | Phosphorylation | Uniprot | |
T19 | Phosphorylation | P06493 (CDK1) | Uniprot |
S22 | Phosphorylation | P28482 (MAPK1) , P06493 (CDK1) | Uniprot |
T24 | Phosphorylation | Uniprot | |
T27 | Phosphorylation | Uniprot | |
K32 | Ubiquitination | Uniprot | |
R41 | Methylation | Uniprot | |
Y45 | Phosphorylation | Uniprot | |
R48 | Methylation | Uniprot | |
S51 | Phosphorylation | Uniprot | |
T64 | Phosphorylation | Uniprot | |
S66 | Phosphorylation | Uniprot | |
S71 | Phosphorylation | Uniprot | |
S75 | Phosphorylation | Uniprot | |
K78 | Ubiquitination | Uniprot | |
Y81 | Phosphorylation | Uniprot | |
K90 | Ubiquitination | Uniprot | |
S94 | Phosphorylation | Uniprot | |
K97 | Acetylation | Uniprot | |
K97 | Sumoylation | Uniprot | |
K97 | Ubiquitination | Uniprot | |
S107 | Phosphorylation | Uniprot | |
K108 | Acetylation | Uniprot | |
K108 | Ubiquitination | Uniprot | |
K114 | Acetylation | Uniprot | |
K114 | Ubiquitination | Uniprot | |
K117 | Ubiquitination | Uniprot | |
K123 | Ubiquitination | Uniprot | |
K135 | Acetylation | Uniprot | |
K135 | Ubiquitination | Uniprot | |
S143 | Phosphorylation | Uniprot | |
K144 | Acetylation | Uniprot | |
K144 | Ubiquitination | Uniprot | |
S149 | Phosphorylation | Uniprot | |
T150 | Phosphorylation | Uniprot | |
S153 | Phosphorylation | Uniprot | |
K155 | Acetylation | Uniprot | |
K155 | Ubiquitination | Uniprot | |
T157 | Phosphorylation | Uniprot | |
R166 | Methylation | Uniprot | |
K171 | Acetylation | Uniprot | |
K171 | Ubiquitination | Uniprot | |
K180 | Acetylation | Uniprot | |
K180 | Ubiquitination | Uniprot | |
K181 | Ubiquitination | Uniprot | |
R189 | Methylation | Uniprot | |
T199 | Phosphorylation | Uniprot | |
K201 | Acetylation | Uniprot | |
K201 | Sumoylation | Uniprot | |
K201 | Ubiquitination | Uniprot | |
K208 | Acetylation | Uniprot | |
K208 | Sumoylation | Uniprot | |
K208 | Ubiquitination | Uniprot | |
Y211 | Phosphorylation | Uniprot | |
S212 | Phosphorylation | Uniprot | |
T218 | Phosphorylation | Uniprot | |
K219 | Sumoylation | Uniprot | |
K219 | Ubiquitination | Uniprot | |
T224 | Phosphorylation | Uniprot | |
K233 | Acetylation | Uniprot | |
K233 | Sumoylation | Uniprot | |
K233 | Ubiquitination | Uniprot | |
K260 | Acetylation | Uniprot | |
K260 | Sumoylation | Uniprot | |
K260 | Ubiquitination | Uniprot | |
K261 | Acetylation | Uniprot | |
K261 | Ubiquitination | Uniprot | |
K265 | Acetylation | Uniprot | |
K265 | Sumoylation | Uniprot | |
K265 | Ubiquitination | Uniprot | |
K270 | Acetylation | Uniprot | |
K270 | Sumoylation | Uniprot | |
K270 | Ubiquitination | Uniprot | |
S277 | Phosphorylation | Uniprot | |
S282 | Phosphorylation | Uniprot | |
S295 | Phosphorylation | Uniprot | |
S301 | Phosphorylation | P31749 (AKT1) | Uniprot |
S303 | Phosphorylation | Uniprot | |
S307 | Phosphorylation | O14757 (CHEK1) | Uniprot |
K311 | Acetylation | Uniprot | |
K311 | Sumoylation | Uniprot | |
K311 | Ubiquitination | Uniprot | |
K316 | Ubiquitination | Uniprot | |
K319 | Ubiquitination | Uniprot | |
S326 | Phosphorylation | Uniprot | |
Y359 | Phosphorylation | Uniprot | |
Y376 | Phosphorylation | Uniprot | |
K378 | Acetylation | Uniprot | |
K378 | Sumoylation | Uniprot | |
K378 | Ubiquitination | Uniprot | |
R386 | Methylation | Uniprot | |
S390 | Phosphorylation | P06493 (CDK1) | Uniprot |
S392 | Phosphorylation | P06493 (CDK1) | Uniprot |
T394 | Phosphorylation | Uniprot | |
S395 | Phosphorylation | Uniprot | |
S398 | Phosphorylation | Uniprot | |
S403 | Phosphorylation | Uniprot | |
S404 | Phosphorylation | P31749 (AKT1) | Uniprot |
S406 | Phosphorylation | Uniprot | |
S407 | Phosphorylation | Uniprot | |
T409 | Phosphorylation | Uniprot | |
S414 | Phosphorylation | Uniprot | |
T416 | Phosphorylation | Uniprot | |
K417 | Acetylation | Uniprot | |
K417 | Sumoylation | Uniprot | |
K417 | Ubiquitination | Uniprot | |
K418 | Acetylation | Uniprot | |
K418 | Ubiquitination | Uniprot | |
K420 | Sumoylation | Uniprot | |
K420 | Ubiquitination | Uniprot | |
S423 | Phosphorylation | Uniprot | |
T424 | Phosphorylation | Uniprot | |
S426 | Phosphorylation | Uniprot | |
S429 | Phosphorylation | Uniprot | |
S431 | Phosphorylation | Uniprot | |
S437 | Phosphorylation | Uniprot | |
K450 | Acetylation | Uniprot | |
K450 | Sumoylation | Uniprot | |
K450 | Ubiquitination | Uniprot | |
K457 | Acetylation | Uniprot | |
K457 | Ubiquitination | Uniprot | |
S458 | Phosphorylation | Uniprot | |
S463 | Phosphorylation | Uniprot | |
K470 | Acetylation | Uniprot | |
K470 | Methylation | Uniprot | |
K470 | Ubiquitination | Uniprot | |
T480 | Phosphorylation | Uniprot | |
Y481 | Phosphorylation | Uniprot | |
K486 | Sumoylation | Uniprot | |
K486 | Ubiquitination | Uniprot | |
T488 | Phosphorylation | Uniprot | |
T505 | Phosphorylation | Uniprot | |
S507 | Phosphorylation | Uniprot | |
T510 | Phosphorylation | Uniprot | |
K515 | Acetylation | Uniprot | |
C522 | S-Nitrosylation | Uniprot | |
S525 | Phosphorylation | Uniprot | |
T528 | Phosphorylation | Uniprot | |
S533 | Phosphorylation | Uniprot | |
T534 | Phosphorylation | Uniprot | |
S546 | Phosphorylation | Uniprot | |
T548 | Phosphorylation | Uniprot | |
S568 | Phosphorylation | Uniprot | |
S583 | Phosphorylation | Uniprot | |
T585 | Phosphorylation | Uniprot | |
T590 | Phosphorylation | Uniprot | |
K597 | Acetylation | Uniprot | |
K597 | Sumoylation | Uniprot | |
K597 | Ubiquitination | Uniprot | |
S599 | Phosphorylation | Uniprot | |
S601 | Phosphorylation | Uniprot | |
S603 | Phosphorylation | Uniprot | |
S612 | O-Glycosylation | Uniprot | |
S612 | Phosphorylation | Uniprot | |
S613 | Phosphorylation | Uniprot | |
S615 | Phosphorylation | Uniprot | |
S616 | Phosphorylation | Uniprot | |
S618 | Phosphorylation | Uniprot | |
S619 | Phosphorylation | Uniprot | |
T621 | Phosphorylation | Uniprot | |
T623 | Phosphorylation | Uniprot | |
S625 | Phosphorylation | Uniprot | |
S628 | Phosphorylation | Uniprot | |
S632 | Phosphorylation | Uniprot | |
S636 | Phosphorylation | Uniprot | |
T643 | O-Glycosylation | Uniprot | |
T643 | Phosphorylation | Uniprot | |
R644 | Methylation | Uniprot | |
S651 | Phosphorylation | Uniprot | |
S652 | Phosphorylation | Uniprot | |
T655 | Phosphorylation | Uniprot | |
S657 | Phosphorylation | Uniprot |
研究背景
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. 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.
Increased phosphorylation of the lamins occurs before envelope disintegration and probably plays a role in regulating lamin associations.
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, ZMPSTE24/FACE1 mediated cleavage of the last three amino acids, methylation of the C-terminal cysteine and endoproteolytic removal of the last 15 C-terminal amino acids. Proteolytic cleavage requires prior farnesylation and methylation, and absence of these blocks cleavage.
Sumoylation is necessary for the localization to the nuclear envelope.
Farnesylation of prelamin-A/C facilitates nuclear envelope targeting.
Nucleus. Nucleus envelope. Nucleus lamina. Nucleus>Nucleoplasm.
Note: 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.
Nucleus speckle.
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.
Homodimer of lamin A and lamin C. Interacts with lamin-associated polypeptides IA, IB and TMPO-alpha, RB1 and with emerin. Interacts with SREBF1, SREBF2, SUN2 and TMEM43. Interacts with TMEM201 (By similarity). Proteolytically processed isoform A interacts with NARF. Interacts with SUN1. Prelamin-A/C interacts with EMD. Interacts with MLIP. Interacts with DMPK; may regulate nuclear envelope stability. Interacts with SUV39H1; the interaction increases stability of SUV39H1. Interacts with SYNE2. Interacts with ITSN1 isoform 2.
Belongs to the intermediate filament family.
研究領域
· Cellular Processes > Cell growth and death > Apoptosis. (View pathway)
· Human Diseases > Cardiovascular diseases > Hypertrophic cardiomyopathy (HCM).
· Human Diseases > Cardiovascular diseases > Arrhythmogenic right ventricular cardiomyopathy (ARVC).
· Human Diseases > Cardiovascular diseases > Dilated cardiomyopathy (DCM).
Restrictive clause
Affinity Biosciences tests all products strictly. Citations are provided as a resource for additional applications that have not been validated by Affinity Biosciences. Please choose the appropriate format for each application and consult Materials and Methods sections for additional details about the use of any product in these publications.
For Research Use Only.
Not for use in diagnostic or therapeutic procedures. Not for resale. Not for distribution without written consent. Affinity Biosciences will not be held responsible for patent infringement or other violations that may occur with the use of our products. Affinity Biosciences, Affinity Biosciences Logo and all other trademarks are the property of Affinity Biosciences LTD.