protein

Recombinant Fibulin 5 (FBLN5)

MBS2009927

0.01 mg

190 USD

Recombinant Protein

Recombinant Fibulin 5 (FBLN5)

Fibulin 5 (FBLN5)

fibulin-5; Fibulin-5; fibulin-5; urine p50 protein; developmental arteries and neural crest EGF-like protein; fibulin 5; Developmental arteries and neural crest EGF-like protein; Dance; Urine p50 protein

FBLN5

FBLN5; FBLN5; EVEC; UP50; ADCL2; ARMD3; DANCE; ARCL1A; FIBL-5; DANCE; FIBL-5; Dance; UP50

FBLN5_HUMAN

E Coli

Homo sapiens (Human)

448

The sequence of the target protein is listed below. LS APNYPTISRP LICRFGYQMD ESNQCVDVDE CATDSHQCNP TQICINTEGGYTCSCTDGYW LLEGQCLDID ECRYGYCQQL CANVPGSYSC TCNPGFTLNE DGRSC

>95%

Supplied as lyophilized form in 20mM Tris, 150mM NaCl, pH8.0, containing 1mM EDTA, 1mM DTT, 0.01% sarcosyl, 5% trehalose, and preservative.

Avoid repeated freeze/thaw cycles. Store at 2-8 degree C for one month. Aliquot and store at -80 degree C for 12 months. Stability Test: The thermal stability is described by the loss rate of the targetprotein. The loss rate was determined by accelerated thermal degradation test,that is, incubate the protein at 37 degree C for 48h, and no obvious degradation andprecipitation were observed. (Referring from China Biological Products Standard,which was calculated by the Arrhenius equation.) The loss of this protein is lessthan 5% within the expiration date under appropriate storage condition.

SDS-PAGE, Western Blot (WB), ELISA (EIA), Immunoprecipitation (IP)

Expression System: Prokaryotic expression. Residues: Leu99~Cys205. Tags: Two N-terminal Tags, His-tag and T7-tag. Accession: Q9UBX5. Subcellular Location: Secreted. Endotoxin Level: <1.0EU per 1ug (determined by the LAL method).

Predicted isoelectric point: 5.1. Predicted Molecular Mass: 15.7kDa. Accurate Molecular Mass: 20kDa as determined by SDS-PAGE reducing conditions. Reconstitution: Reconstitute in ddH2O.

19743803

NP_006320.2

NM_006329.3

Q9UBX5

Elastic Fibre Formation Pathway (730310); Extracellular Matrix Organization Pathway (576262); Molecules Associated With Elastic Fibres Pathway (730311)

The protein encoded by this gene is a secreted, extracellular matrix protein containing an Arg-Gly-Asp (RGD) motif and calcium-binding EGF-like domains. It promotes adhesion of endothelial cells through interaction of integrins and the RGD motif. It is prominently expressed in developing arteries but less so in adult vessels. However, its expression is reinduced in balloon-injured vessels and atherosclerotic lesions, notably in intimal vascular smooth muscle cells and endothelial cells. Therefore, the protein encoded by this gene may play a role in vascular development and remodeling. Defects in this gene are a cause of autosomal dominant cutis laxa, autosomal recessive cutis laxa type I (CL type I), and age-related macular degeneration type 3 (ARMD3). [provided by RefSeq, Jul 2008]

FBLN5: Promotes adhesion of endothelial cells through interaction of integrins and the RGD motif. Could be a vascular ligand for integrin receptors and may play a role in vascular development and remodeling. Defects in FBLN5 are the cause of cutis laxa, autosomal dominant, type 2 (ADCL2). A connective tissue disorder characterized by loose, hyperextensible skin with decreased resilience and elasticity leading to a premature aged appearance. Face, hands, feet, joints, and torso may be differentially affected. Additional variable clinical features are gastrointestinal diverticula, hernia, and genital prolapse. Rare manifestations are pulmonary artery stenosis, aortic aneurysm, bronchiectasis, and emphysema. Defects in FBLN5 are a cause of cutis laxa, autosomal recessive, type 1A (ARCL1A). A connective tissue disorder characterized by loose, hyperextensible skin with decreased resilience and elasticity leading to a premature aged appearance. Face, hands, feet, joints, and torso may be differentially affected. The clinical spectrum of autosomal recessive cutis laxa is highly heterogeneous with respect to organ involvement and severity. Type I autosomal recessive cutis laxa is a specific, life-threatening disorder with organ involvement, lung atelectasis and emphysema, diverticula of the gastrointestinal and genitourinary systems, and vascular anomalies. Associated cranial anomalies, late closure of the fontanel, joint laxity, hip dislocation, and inguinal hernia have been observed but are uncommon. Defects in FBLN5 are the cause of age-related macular degeneration type 3 (ARMD3). ARMD is a multifactorial disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid (known as drusen) that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane. Belongs to the fibulin family. Protein type: Secreted; Secreted, signal peptide. Chromosomal Location of Human Ortholog: 14q32.1. Cellular Component: extracellular matrix; extracellular space; proteinaceous extracellular matrix; extracellular region. Molecular Function: integrin binding; protein C-terminus binding; protein binding; protein homodimerization activity; calcium ion binding. Biological Process: elastic fiber assembly; secretion; extracellular matrix organization and biogenesis; cell-matrix adhesion; regulation of cell growth. Disease: Cutis Laxa, Autosomal Dominant 2; Macular Degeneration, Age-related, 3; Cutis Laxa, Autosomal Recessive, Type Ia

0.01 mg

190 USD

0.05 mg

395

0.1 mg

610