FBLIM1 Human

Filamin Binding LIM Protein 1 Human Recombinant
Cat. No.
BT8295
Source
Escherichia Coli.
Synonyms
Filamin binding LIM protein 1, CAL, FBLP-1, FBLP1, RP11-169K16.5, Migfilin, Mitogen-inducible 2-interacting protein, MIG2-interacting protein.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

FBLIM1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 396 amino acids (1-373) and having a molecular mass of 43.1 kDa. FBLIM1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Filamin binding LIM protein 1 (FBLIM1) serves as an anchor for proteins involved in cell-extracellular matrix (ECM) adhesion and for actin filaments that contain filamin. It plays a role in cell shape changes, movement, and the regulation of actin filament cross-linking and stabilization mediated by filamin. Additionally, FBLIM1 enhances integrin activity and modulates cell-cell adhesion mediated by integrins.
Description
Recombinant human FBLIM1, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 396 amino acids (residues 1-373) with a molecular weight of 43.1 kDa. It includes a 23-amino acid His-tag at the N-terminus and is purified using proprietary chromatographic methods.
Physical Appearance
A clear, sterile solution without any color.
Formulation
The FBLIM1 solution is provided at a concentration of 0.25 mg/ml in a buffer consisting of 20 mM Tris-HCl (pH 8.0), 0.15 M NaCl, 10% glycerol, and 1 mM DTT.
Stability
For short-term storage (up to 2-4 weeks), the product can be kept at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. Adding a carrier protein (0.1% HSA or BSA) is advised for long-term storage. Repeated freezing and thawing should be avoided.
Purity
The purity of the protein is greater than 85.0% as assessed by SDS-PAGE.
Synonyms
Filamin binding LIM protein 1, CAL, FBLP-1, FBLP1, RP11-169K16.5, Migfilin, Mitogen-inducible 2-interacting protein, MIG2-interacting protein.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMASKPEK RVASSVFITL APPRRDVAVA EEVRQAVCEA RRGRPWEAPA PMKTPEAGLA GRPSPWTTPG RAAATVPAAP MQLFNGGCPP PPPVLDGEDV LPDLDLLPPP PPPPPVLLPS EEEAPAPMGA SLIADLEQLH LSPPPPPPQA PAEGPSVQPG PLRPMEEELP PPPAEPVEKG ASTDICAFCH KTVSPRELAV EAMKRQYHAQ CFTCRTCRRQ LAGQSFYQKD GRPLCEPCYQ DTLERCGKCG EVVRDHIIRA LGQAFHPSCF TCVTCARCIG DESFALGSQN EVYCLDDFYR KFAPVCSICE NPIIPRDGKD AFKIECMGRN FHENCYRCED CRILLSVEPT DQGCYPLNNH LFCKPCHVKR SAAGCC.

Product Science Overview

Structure and Localization

FBLIM1 is composed of several distinct domains:

  • N-terminal filamin-binding domain: This domain allows FBLIM1 to interact with filamin, a protein that cross-links actin filaments in the cytoskeleton.
  • Central proline-rich domain: This domain is involved in protein-protein interactions.
  • C-terminal LIM domains: These domains are involved in protein-protein interactions and are crucial for the protein’s function in cell adhesion and signaling .

FBLIM1 localizes at cell junctions, where it plays a critical role in linking cell adhesion structures to the actin cytoskeleton. This localization is essential for the assembly and stabilization of actin filaments, which are crucial for maintaining cell shape, motility, and adhesion .

Function

FBLIM1 serves several important functions in the cell:

  • Cell Adhesion: It acts as an anchoring site for cell-extracellular matrix (ECM) adhesion proteins and filamin-containing actin filaments. This anchoring is vital for the stability and integrity of cell junctions .
  • Cell Shape and Motility: FBLIM1 is implicated in modulating cell shape and motility by regulating the cross-linking and stabilization of actin filaments. It also participates in the assembly of filamin-containing signaling complexes that control actin assembly .
  • Integrin Activation: FBLIM1 promotes the activation of integrins, which are transmembrane receptors that facilitate cell-ECM adhesion. It regulates integrin-mediated cell-cell adhesion and promotes the dissociation of filamin A (FLNA) from integrins ITGB3 and ITGB7 .
Clinical Significance

Mutations or dysregulation of the FBLIM1 gene have been associated with several diseases, including:

  • Nivelon-Nivelon-Mabille Syndrome: A rare genetic disorder characterized by developmental anomalies .
  • Valproate Embryopathy: A condition resulting from prenatal exposure to the antiepileptic drug valproate, leading to congenital malformations .
Research and Applications

Recombinant FBLIM1 is used in various research applications to study its role in cell adhesion, motility, and signaling. Understanding the function and regulation of FBLIM1 can provide insights into the mechanisms underlying cell adhesion and motility, which are critical for many physiological processes and disease states .

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