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>   首页   >   产品   >   一抗   >   信号转导   >   LIMA1 Antibody (N-term)   

LIMA1 Antibody (N-term)

Affinity Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - LIMA1 Antibody (N-term) AP16362a
    LIMA1 Antibody (N-term) (Cat. #AP16362a) western blot analysis in A549 cell line lysates (35ug/lane).This demonstrates the LIMA1 antibody detected the LIMA1 protein (arrow).
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession Q9UHB6
Other Accession NP_001107019.1, NP_001107018.1
Reactivity Human
Host Rabbit
Clonality Polyclonal
Isotype Rabbit IgG
Calculated MW 85226 Da
Antigen Region 135-163 aa
Additional Information
Gene ID 51474
Other Names LIM domain and actin-binding protein 1, Epithelial protein lost in neoplasm, LIMA1, EPLIN, SREBP3
Target/Specificity This LIMA1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 135-163 amino acids from the N-terminal region of human LIMA1.
Dilution WB~~1:1000
E~~Use at an assay dependent concentration.
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsLIMA1 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name LIMA1 (HGNC:24636)
Function Actin-binding protein involved in actin cytoskeleton regulation and dynamics. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments (PubMed:12566430, PubMed:33999101). Acts as a negative regulator of primary cilium formation (PubMed:32496561). Plays a role in cholesterol homeostasis. Influences plasma cholesterol levels through regulation of intestinal cholesterol absorption. May act as a scaffold protein by regulating NPC1L1 transportation, an essential protein for cholesterol absorption, to the plasma membrane by recruiting MYO5B to NPC1L1, and thus facilitates cholesterol uptake (By similarity).
Cellular Location Cytoplasm. Cell junction, focal adhesion. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, stress fiber. Cell membrane {ECO:0000250|UniProtKB:Q9ERG0}. Cell projection, ruffle. Cell projection, lamellipodium. Note=Expressed in the brush border membrane of the small intestine and colocalizes with NPC1L1 and MYO5B (PubMed:29880681). Colocalizes with PXN at focal adhesions in mesangial cells (PubMed:24694988). Colocalizes with actin stress fibers in quiescent cells. PDGF stimulation induced disassembly of stress fibers and formation of peripheral and dorsal ruffles, where LIMA1 is relocalized (By similarity). Localized at the lamellipodia, just behind lamellipodia actin ruffles (PubMed:33999101) {ECO:0000250|UniProtKB:Q9ERG0, ECO:0000269|PubMed:24694988, ECO:0000269|PubMed:29880681, ECO:0000269|PubMed:33999101}
Tissue Location Highly expressed in placenta, kidney, pancreas, prostate, ovary, spleen and heart. Also detected in lung, liver, brain, skeletal muscle, thymus, testis and intestine. Not detected in leukocytes. Isoform Beta expressed generally at very low levels Isoform Alpha abundant in epithelial cells from mammary gland, prostate and in normal oral keratinocytes. Low levels in aortic endothelial cells and dermal fibroblasts. Not detectable in myocardium
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

EPLIN is a cytoskeleton-associated protein that inhibits actin filament depolymerization and cross-links filaments in bundles (Maul et al., 2003 [PubMed 12566430]).

REFERENCES

Chircop, M., et al. Cell Cycle 8(5):757-764(2009)
Abe, K., et al. Proc. Natl. Acad. Sci. U.S.A. 105(1):13-19(2008)
Jiang, W.G., et al. Mol. Cancer 7, 71 (2008) :
Sugiyama, N., et al. Mol. Cell Proteomics 6(6):1103-1109(2007)
Olsen, J.V., et al. Cell 127(3):635-648(2006)

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