Anti-SVIL polyclonal antibody (DPAB-DC2999)

Mouse anti-Human SVIL (aa 1679-1786) polyclonal antibody for WB, ELISA

Specifications


Host Species
Mouse
Species Reactivity
Human
Immunogen
SVIL (NP_003165, 1679 a.a. ~ 1786 a.a) partial recombinant protein with GST tag. The sequence is LIHAGLEPLTFTNMFPSWEHREDIAEITEMDTEVSNQITLVEDVLAKLCKTIYPLADLLARPLPEGVDPLKLEIYLTDEDFEFALDMTRDEYNALPAWKQVNLKKAKG
Conjugate
Unconjugated

Target


Alternative Names
SVIL; supervillin; p205/p250; archvillin; membrane-associated F-actin binding protein p205
Entrez Gene ID
UniProt ID

Product Background


Gene summary
SVIL (Supervillin) is a Protein Coding gene. Diseases associated with SVIL include androgenic alopecia. Among its related pathways are Coregulation of Androgen receptor activity. GO annotations related to this gene include actin binding and actin filament binding. An important paralog of this gene is VIL1. This gene encodes a bipartite protein with distinct amino- and carboxy-terminal domains. The amino-terminus contains nuclear localization signals and the carboxy-terminus contains numerous consecutive sequences with extensive similarity to proteins in the gelsolin family of actin-binding proteins, which cap, nucleate, and/or sever actin filaments. The gene product is tightly associated with both actin filaments and plasma membranes, suggesting a role as a high-affinity link between the actin cytoskeleton and the membrane. The encoded protein appears to aid in both myosin II assembly during cell spreading and disassembly of focal adhesions. Several transcript variants encoding different isoforms of supervillin have been described.
Antigen Description
This gene encodes a bipartite protein with distinct amino- and carboxy-terminal domains. The amino-terminus contains nuclear localization signals and the carboxy-terminus contains numerous consecutive sequences with extensive similarity to proteins in the gelsolin family of actin-binding proteins, which cap, nucleate, and/or sever actin filaments. The gene product is tightly associated with both actin filaments and plasma membranes, suggesting a role as a high-affinity link between the actin cytoskeleton and the membrane. The encoded protein appears to aid in both myosin II assembly during cell spreading and disassembly of focal adhesions. Two transcript variants encoding different isoforms of supervillin have been described. Forms a high-affinity link between the actin cytoskeleton and the membrane. Isoform 1 (archvillin) is among the first costameric proteins to assemble during myogenesis and it contributes to myogenic membrane structure and differentiation. Appears to be involved in myosin II assembly. May modulate myosin II regulation through MLCK during cell spreading, an initial step in cell migration. May play a role in invadopodial function. Isoform 2 may be involved in modulation of focal adhesions. Supervillin-mediated down-regulation of focal adhesions involves binding to TRIP6. Plays a role in cytokinesis through KIF14 interaction (By similarity). Supervillin is a protein that in humans is encoded by the SVIL gene. Its function may include recruitment of actin and other cytoskeletal proteins into specialized structures at the plasma membrane and in the nuclei of growing cells. The function about SVIL antigen include actin filament binding; protein binding.
Pathway
Coregulation of Androgen receptor activity.

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References


Pestonjamasp, KN; Pope, RK; et al. Supervillin (p205): A novel membrane-associated, F-actin-binding protein in the Villin/Gelsolin superfamily. JOURNAL OF CELL BIOLOGY 139:1255-1269(1997).
Asano, Y; Kishida, S; et al. DRR1 is expressed in the developing nervous system and downregulated during neuroblastoma carcinogenesis. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 394:829-835(2010).

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