antibody

Vitamin A transporter N-epitope

MBS540119

0.1-0.15 ml WB Contr

290 USD

polyclonal

rabbit

nonconjugated

western blot, immunoprecipitation

Antibody

Vitamin A transporter N-epitope

Vitamin A transporter

Anti-RBP4 Receptor Stra6 (Stimulated by Retinoic Acid) antibodies. ; Affinity purified Stra6 antibody (rat/mouse)

retinoic acid-responsive protein; Stimulated by retinoic acid gene 6 protein; stimulated by retinoic acid gene 6 protein; retinoic acid-responsive protein; stimulated by retinoic acid gene 6; Retinoic acid-responsive protein

Stra6; Stra6; AI891933

STRA6_MOUSE

Polyclonal

Rabbit

Affinity purifed

The antiserum is supplied in antibody stabilization buffer. Store at -20 degree C for long-term storage. MyBioSource does not recommend storage of very dilute antibody solutions unless they are prepared in specially formulated multi use antibody dilution

~0.5mg/ml (Concentrations are in the range of 0.69-1.00 mg/ml of antibody stabilization buffer)

Shipped at 4 degree C. Working solutions of antibodies in DiluOBuffer should be filtered through 0.45um filter after every use for long-term storage.

Western Blot (WB), Immunoprecipitation (IP)

Are tested for WB application at 1:500 dilution. Other applications for this antibody is not tested. WB: > 1:500; Immunoprecipitation & i.p pull-down assays: n.d; IHC n.d (Antibody dilutions for this antibody is for reference only, investigators are expected to determine the optimal conditions). Cross reactivity among various species was no determined.

Immunogen: peptide . Reactivity Note: Cross reactivity Rabbit Affinity purified Stra6 antibody (rat/mouse)

Preservatives: 0.02% Na3N. Buffer: PO4-buffer/Tris/Glycine, pH 7.4-7.8. PO4-buffer/Tris/Glycine, pH 7.4-7.8. Product Note: Now MyBioSource antibody blots now can be stripped and recycle using our specially formulated StripObuffer . This stripping buffer does not requ2ire heating or have any pungent smell.

Antibodies to Retinol Binding Protein Receptors

Stra6 gene encodes a membrane bound retinoic acid sensitive protein that facilitates the transport of vitamin A thru its soluble retinol binding protein complex. The transcription of Stra6 is directly regulated by the cellular levels of retinoic acid, which is a strong teratogen when exposed at elevated concentrations during early embryogenesis. The Stra 6 gene was studies in two human fetuses from consanguineous families with Matthew-Wood syndrome. These subjects exhibited severe microphthalmia, pulmonary agenesis, bilateral diaphragmatic eventration, duodenal stenosis, pancreatic malformations, and intrauterine growth retardation (1). In view of the increasing evidence that retinoic acid (RA) is a crucial signaling molecule during vertebrate development, several studies were initiated to systematically isolate the genes whose expression is induced by retinoic acid treatment at various exposure times. Several genes are induced in Pluripotent mouse P19 embryonal carcinoma cells (P19EC) RA treatment. At least 50 different cDNA fragments corresponding to RA-induced genes were isolated, 6 of them are known proteins, 4 of which are described as RA inducible, while the remaining 40 are unknown and novel genes. Two of these unknown novel genes are Stra1 and Stra6. Stra1 corresponds to the mouse ligand for Cek5 receptor protein tyrosine kinase and Stra6 is a vitamin A transporter (1). Stra6 is a membrane bound protein containing 10 TMD characteristic of solute carrier proteins. Stra6 protein is expressed in various tissues including fibroblasts and eye, a detailed analysis of distinct parts of an adult eye revealed expression in sclera, retina, retinal pigment epithelium and trabecular mashwork but not in choroid and iris (2). A number of mutations in the Stra6 (chromosome 15) gene have been studied. A homozygous deletion generating a premature stop codon that led to absence of the immunoreactive protein in patient fibroblasts culture and three miss-sense mutations (P90L, P293L and T321P) caused significant alteration in the geometry of the loops connecting the transmembrane helices of Stra6. Two other mutations in the C-terminal region caused aberration in the SH2 binding motifs and in the phosphorylation of the Stra67 protein (2). Patients with these mutations show anophthalmia and distinct eyebrows as common signs along with alveolar dysplasia or a common congenital heart defect and diaphragmatic hernia. Stra6 is a 99 kDa membrane bound protein with 10 TMD as commonly seen in all membrane transporter proteins. The Stra6 selective-antibodies were generated against conserved sequences from the mouse and human Stra6 protein that are unique to either mouse or human stra6 protein. MyBioSource employs cyclic peptide methodology for generating antibodies, which results in higher titer and specificity. The Str6-selective antibodies are affinity purified against immobilized antigen based affinity chromatography which yielded epitope-specific antibodies. The Str6 antibodies label a 99kDa protein in Western blot using Western blot positive control for Stra6 (PC-Str6). Anti-Stra6-selective antibodies are most suitable for immunoprecipitation and immunohistochemical localization of Str6 protein. MyBioSource will conjugate antibodies with various fluorescent probes upon request at nominal charge. Limited quantities of antigens are also available for blocking studies. Please enquire for their availability before ordering. MyBioSource also provides antibodies to various eye related proteins and other targets, for a complete listings visit our website at www.mybiosource.com. MyBioSource will also provide Western blot positive controls for most of these an tibodies in ready-to-use buffer for easy identification of respective proteins.

1. Bouillet P, Oulad-Abdelghani M, Vicaire S, Garnier JM, Schuhbaur B, Dollé P, Chambon P. Efficient cloning of cDNAs of retinoic acid-responsive genes in P19 embryonal carcinoma cells and characterization of a novel mouse gene, Stra1 (mouse LERK-2/Eplg2). Dev Biol. 1995 Aug;170(2):420-33. 2. Golzio C, Martinovic-Bouriel J, Thomas S, Mougou-Zrelli S, Grattagliano-Bessieres B, Bonniere M, Delahaye S, Munnich A, Encha-Razavi F, Lyonnet S, Vekemans M, Attie-Bitach T, Etchevers HC. Matthew-Wood syndrome is caused by truncating mutations in the retinol-binding protein receptor gene STRA6. Am J Hum Genet. 2007 Jun;80(6):1179-87. Epub 2007 Apr 11. Links

3126975

AAC16016

O70491

73,775 Da

Disease Pathway 819462!!Diseases Associated With Visual Transduction Pathway 819540!!Retinoid Cycle Disease Events Pathway 819541!!Signal Transduction Pathway 819739!!The Canonical Retinoid Cycle In Rods (twilight Vision) Pathway 819545!!Visual Phototransduction Pathway 819543

Function: May act as a high-affinity cell-surface receptor for the complex retinol-retinol binding protein (RBP/RBP4). Acts by removing retinol from RBP/RBP4 and transports it across the plasma membrane, where it can be metabolized. This mechanism does not depend on endocytosis. Binds to RBP/RBP4 with high affinity. Increases cellular retinol uptake from the retinol-RBP complex . By similarity. Subcellular location: Cell membrane; Multi-pass membrane protein. Note: Plasma membrane of the basal pole of Sertoli cells, absent in plasma membrane of neighboring spermatogonia. Ref.1. Tissue specificity: Widely expressed in the embryo. In the adult, is highly expressed in cells that compose blood-organ barriers in the brain (choroid plexus and the brain microvascular), in the eye (retinal pigment epithelium), in testis (the basal layer of the seminiferous epithelium), in the yolk sac, and in the chorioallantoic placenta (at protein level). Also detected in kidney, spleen, and female genital tract; and at lower levels in heart and lung. Not detected in liver. Ref.1. Developmental stage: During embryogenesis, strongly expressed in the periocular mesenchyme, in the developing eyes, in respiratory mesenchymes, and in respiratory and bronchial epithelium, as well as in the developing central nervous system and in different embryonic gut derivatives (the epithelium of the pharyngeal pouches, mesenchyme of the esophagus, stomach, intestine, and rectum). In Sertoli cells expression depends on the stage of the spermatogenic cycle. During early placentation, is expressed in the yolk sac membrane and the chorionic plate. Expression was no longer detected in the yolk sac membrane during mid-late gestation, but was found in the labyrinthine zone of the chorioallantoic placenta. Expressed during early dorsoventral limb patterning and during endochondral ossification. Ref.1 Ref.4 Ref.5. Induction: By retinoic acid. Synergistically up-regulated by Wnt1 and retinoids in mammary epithelial cells. Ref.1 Ref.3 Ref.6 Ref.7. Miscellaneous: The retinoic acid-induced activation is impaired in retinoic acid receptor gamma-null F9 cells.

0.1-0.15 ml WB Control

290 USD