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The antibody against LIMD1 was raised in Rabbit using the recombinant fusion protein containing a sequence corresponding to amino acids 1-200 of human LIMD1 (NP_055055.1) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, ELISA.
The antibody against LIMD1 was raised in Rabbit using the recombinant fusion protein containing a sequence corresponding to amino acids 1-200 of human LIMD1 (NP_055055.1) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, ELISA.
| Cat.No | ADA-06951A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | LIMD1 |
| Target Synonyms | LIMD1 | Form | Liquid |
| Species Reactivity | Human, Mouse | Isotype | IgG |
| Storage Buffer | 50% Glycerol, PBS with 0.01% thimerosal, pH7.3. | Purification Method | Affinity purification |
| Positive Samples | HeLa, Mouse heart, HepG2, MCF7, Mouse lung | Application | ELISA, WB |
| Immunogen Description | Recombinant fusion protein containing a sequence corresponding to amino acids 1-200 of human LIMD1 (NP_055055.1). | Target Species | Human |
|---|---|---|---|
| Immunogen Sequence | MDKYDDLGLEASKFIEDLNMYEASKDGLFRVDKGAGNNPEFEETRRVFATKMAKIHLQQQQQQLLQEETLPRGSRGPVNGGGRLGPQARWEVVGSKLTVDGAAKPPLAASTGAPGAVTTLAAGQPPYPPQEQRSRPYLHGTRHGSQDCGSRESLATSEMSAFHQPGPCEDPSCLTHGDYYDNLSLASPKWGDKPGVSPSI | Uniprot ID | Q9UGP4 |
Uniprot Id
Q9UGP4
Target Species
Human
Target Name
LIMD1
Target Full Name
LIM domain-containing protein 1
Target Function
Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, cell-cell adhesion, cell differentiation, proliferation and migration. Positively regulates microRNA (miRNA)-mediated gene silencing and is essential for P-body formation and integrity. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Acts as a transcriptional corepressor for SNAI1- and SNAI2/SLUG-dependent repression of E-cadherin transcription. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1. Inhibits E2F-mediated transcription, and suppresses the expression of the majority of genes with E2F1-responsive elements. Regulates osteoblast development, function, differentiation and stress osteoclastogenesis. Enhances the ability of TRAF6 to activate adapter protein complex 1 (AP-1) and negatively regulates the canonical Wnt receptor signaling pathway in osteoblasts. May act as a tumor suppressor by inhibiting cell proliferation
Target Subcellular Location
Cytoplasm. Nucleus. Cytoplasm, P-body. Cell junction, adherens junction. Cell junction, focal adhesion. Note=Shuttles between cytoplasm and nucleus but is localized predominantly to the cytoplasm. Found in the nucleus but not nucleoli. Colocalizes with VCL in the focal adhesions. Down-regulation and/or elimination of its expression from the nucleus of neoplastic cells correlates strongly with poor patient prognosis and aggressive forms of breast carcinoma. Conversely, strong nuclear localization correlates with low-tumor grade and better patient prognosis.
Target Protein Families
Zyxin/ajuba family
Target Tissue Specificity
Expressed in normal and breast cancer tissues (at protein level). Ubiquitous.
Target Synonyms
AW822033; D9Ertd192e; LIM domain-containing protein 1; LIM domains containing 1; LIMD1; LIMD1_HUMAN; OTTHUMP00000164657; OTTHUMP00000210317; rCG_25194
Target Background
Predicted to enable transcription corepressor activity. Involved in several processes, including negative regulation of hippo signaling; regulation of gene expression; and response to hypoxia. Acts upstream of or within P-body assembly and gene silencing by miRNA. Located in several cellular components, including P-body; adherens junction; and focal adhesion. Part of RISC complex.
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