anti-Lipoma Preferred Partner pAb (IG-817)
| Code | Size | Price |
|---|
| AG-25T-0106-C050 | 50 ug | £300.00 |
Quantity:
Prices exclude any Taxes / VAT
Overview
Antibody Clonality: Polyclonal
Regulatory Status: RUO
Target Species:
- Bovine (Cattle)
- Human
- Porcine (pig)
Applications:
- Immunocytochemistry (ICC)
- Immunoprecipitation (IP)
- Western Blot (WB)
Shipping:
-20°C
Storage:
-20°C
Documents
Further Information
Alternate Names/Synonyms:
LPP; LIM Domain-containing Preferred Translocation Partner in Lipoma
Concentration:
500µg/ml
EClass:
32160000
Form (Short):
liquid
Formulation:
Liquid. In PBS containing 0.01% sodium azide.
Handling Advice:
Do not freeze/thaw.
Immunogen:
Recombinant human lipoma preferred partner (LPP) (aa 1-109).
Long Description:
Polyclonal Antibody. Recognizes human, rat and pig LPP. Source: Rabbit. Applications: ICC, IP, WB. Liquid. In PBS containing 0.01% sodium azide. Lipoma preferred partner (LPP) is encoded by the preferred fusion partner gene of the high mobility group protein HMGI-C. LPP is frequently affected by chromosomal translocations in a major group of soft tissue lipomas, as well as in a parosteal lipoma and in pulmonary chondroid hamartomas. The resulting fusion proteins comprise three DNA binding domains of HMGI-C fused to two or three C-terminal LIM domains of LPP and a reciprocal product, respectively. Expression of a HMGI-C/LPP fusion protein causes malignant transformation of fibroblasts. Similar to its relatives zyxin and TRIP (thyroid receptor interacting protein 6) / ZRP-1 (zyxin-related protein 1), LPP consists of a N-terminal proline-rich domain followed by three C-terminal LIM domains (double zinc finger structures that are involved in protein-protein interactions). Like the cytoskeletal protein zyxin, LPP localizes to focal adhesions and cell-cell adherens junctions. LPP harbors a nuclear export signal and displays transcriptional activation capacity.
NCBI, Uniprot Number:
Q93052
Package Type:
Plastic Vial
Product Description:
Lipoma preferred partner (LPP) is encoded by the preferred fusion partner gene of the high mobility group protein HMGI-C. LPP is frequently affected by chromosomal translocations in a major group of soft tissue lipomas, as well as in a parosteal lipoma and in pulmonary chondroid hamartomas. The resulting fusion proteins comprise three DNA binding domains of HMGI-C fused to two or three C-terminal LIM domains of LPP and a reciprocal product, respectively. Expression of a HMGI-C/LPP fusion protein causes malignant transformation of fibroblasts. Similar to its relatives zyxin and TRIP (thyroid receptor interacting protein 6) / ZRP-1 (zyxin-related protein 1), LPP consists of a N-terminal proline-rich domain followed by three C-terminal LIM domains (double zinc finger structures that are involved in protein-protein interactions). Like the cytoskeletal protein zyxin, LPP localizes to focal adhesions and cell-cell adherens junctions. LPP harbors a nuclear export signal and displays transcriptional activation capacity.
Purity:
Antigen affinity purified.
Source / Host:
Rabbit
Specificity:
Recognizes human, rat and pig LPP.
Transportation:
Non-hazardous
UNSPSC Category:
Primary Antibodies
UNSPSC Number:
12352203
Use & Stability:
Stable for at least 1 year after receipt when stored at -20°C.
References
LPP, a LIM protein highly expressed in smooth muscle: I. Gorenne, et al.; Am. J. Physiol. Cell Physiol. 285, 674 (2003) | Angiotensin II, focal adhesion kinase, and PRX1 enhance smooth muscle expression of lipoma preferred partner and its newly identified binding partner palladin to promote cell migration: L. Jin, et al.; Circ Res. 100, 817 (2007) | The Actin-associated Protein Palladin Is Required for Development of Normal Contractile Properties of Smooth Muscle Cells Derived from Embryoid Bodies: L. Jin, et al.; J. Biol. Chem. 284, 2121 (2009) | Mechanical properties of the extracellular matrix alter expression of smooth muscle protein LPP and its partner palladin; relationship to early atherosclerosis and vascular injury: L. Jin, et al.; J. Muscle Res. Cell. Motil. 30, 41 (2009) | ETV5 cooperates with LPP as a sensor of extracellular signals and promotes EMT in endometrial carcinomas: E. Colas, et al.; Oncogene 31, 4778 (2012) | Cells lacking beta-actin are genetically reprogrammed and maintain conditional migratory capacity: D. Tondeleir, et al.; Mol. Cell Proteom. 11, 255 (2012) | Nuclear import of LASP-1 is regulated by phosphorylation and dynamic protein?protein interactions: S. Mihlan, et al.; Oncogene 32, 2107 (2013)