Recombinant Human Retinaldehyde-binding protein 1 (RLBP1)

Code CSB-YP019743HU
MSDS
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Source Yeast
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Code CSB-EP019743HU
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Source E.coli
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Code CSB-EP019743HU-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP019743HU
MSDS
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Source Baculovirus
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Code CSB-MP019743HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
RLBP1
Uniprot No.
Alternative Names
Cellular retinaldehyde binding protein 1; Cellular retinaldehyde binding protein; Cellular retinaldehyde-binding protein; MGC3663; Retinaldehyde binding protein 1; Retinaldehyde-binding protein 1; RLBP 1; RLBP1; RLBP1_HUMAN
Species
Homo sapiens (Human)
Expression Region
2-317
Target Protein Sequence
SEGVGTFRM VPEEEQELRA QLEQLTTKDH GPVFGPCSQL PRHTLQKAKD ELNEREETRE EAVRELQEMV QAQAASGEEL AVAVAERVQE KDSGFFLRFI RARKFNVGRA YELLRGYVNF RLQYPELFDS LSPEAVRCTI EAGYPGVLSS RDKYGRVVML FNIENWQSQE ITFDEILQAY CFILEKLLEN EETQINGFCI IENFKGFTMQ QAASLRTSDL RKMVDMLQDS FPARFKAIHF IHQPWYFTTT YNVVKPFLKS KLLERVFVHG DDLSGFYQEI DENILPSDFG GTLPKYDGKA VAEQLFGPQA QAENTAF
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Soluble retinoid carrier essential the proper function of both rod and cone photoreceptors. Participates in the regeneration of active 11-cis-retinol and 11-cis-retinaldehyde, from the inactive 11-trans products of the rhodopsin photocycle and in the de novo synthesis of these retinoids from 11-trans metabolic precursors. The cycling of retinoids between photoreceptor and adjacent pigment epithelium cells is known as the 'visual cycle'.
Gene References into Functions
  1. RLBP1 gene geographical area-related mutation is associated with retinitis punctata albescens. PMID: 28764803
  2. we provide evidence for an allosteric modulation of the enzymatic activity by 11-cis retinoids. This regulation is independent from cellular retinaldehyde-binding protein (CRALBP), the major cis-retinoid binding protein. PMID: 28096191
  3. These results show that joint tests of main effects and gene-gene interaction reveal associations at some novel loci that were missed when considering main effects alone. PMID: 28813576
  4. Different mutations in RLBP1 are correlated with quite different morphological and functional characteristics outlines the complexity of the protein. PMID: 25429852
  5. RLBP1 gene is upregulated in patients with reactive retinal astrocytic tumors. PMID: 24921169
  6. Patients with retinitis punctata albescens (RPA) show variable degrees of foveal cone death, even at an early stage. This finding has implications for future treatment. PMID: 23929416
  7. The two RLBP1 genotypes presented a phenotypical and electrophysiological expression of progressive retinal disease similar to that previously described in homozygotes for the c.700C>T (p.R234W) RLBP1 mutation. PMID: 22551409
  8. The clinical characteristics of a Japanese patient with a homozygous R234W mutation in RLBP1 are very similar to that of Swedish patients with Bothnia dystrophy. PMID: 22171637
  9. Identification of autoantibodies specific for two retinal antigens (CRALBP and S-Ag) supports the concept of an autoimmunological origin of the disease. PMID: 21904838
  10. The R234W mutation reveals impaired 11-cis-retinal release through stabilization of the ligand complex. PMID: 22183382
  11. mutations in RLBP1 are responsible for fundus albipunctatus in the affected individuals of these consanguineous Pakistani families. PMID: 21447491
  12. In the RLBP1-Bothnia dystrophy phenotype, a loss of function and thinning of the central macula are found, indicating early damage of the cone photoreceptors in this disease of the visual cycle. PMID: 20696998
  13. Newfoundland rod-cone dystrophy, an early-onset retinal dystrophy, is caused by splice-junction mutations in RLBP1 PMID: 11868161
  14. the M225K mutation abolishes and the R233W mutation tightens retinoid binding and both impair CRALBP function in the visual cycle as an 11-cis-retinol acceptor and as a substrate carrier. PMID: 12536144
  15. Trp-165, Met-208, Met-222, Met-225, and Trp-244 are components of the CRALBP ligand binding cavity. PMID: 12536149
  16. Patients with a clinical presentation of RPA (retinitis punctata albescens) can have genetically different mutations. PMID: 14718298
  17. Only eight RLBP1 mutations have been reported to date, and here we describe two novel mutations. PMID: 15234312
  18. Cellular retinaldehyde binding protein 1 (CRALBP) inhibits the reduction of 11-cis-retinal stronger than the oxidation of 11-cis-retinol, in accord with its higher affinity for 11-cis-retinal. PMID: 15865448
  19. A novel mutation in RLBP1 gene was found in a Japanese patient with retinitis punctata albescens. Degenerative changes of the outer retina were detected by optical coherence tomography PMID: 15953459
  20. Because of the high density of Alu elements in RLBP1, a systematic search should be made for deletions in this gene when one or both alleles lack point mutations, in the case of RPA or flecked retinal dystrophy. PMID: 17065479
  21. analysis of CRALBP ligand and protein interactions PMID: 17249612
  22. CRALBP transcripts in retinal pigment epithelium cells contain a noncoding exon in addition to a newly described promoter and, by definition, an additional intron PMID: 17652763
  23. The presence of CRALBP autoantibodies in 54% of tested uveitis patients supports CRALBP as a possible autoantigen in human autoimmune uveitis PMID: 18317528
  24. Bothnia dystrophy is caused by the loss of CRALBP function due to changed physical features and impaired activity of retinoid binding. PMID: 18344446
  25. These results reveal an unanticipated domino-like structural transition causing Bothnia-type retinal dystrophy by the impaired release of 11-cis-retinal from R234W. PMID: 19846785
  26. Using shotgun mass spectrometry, we found this protein differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia PMID: 19165527

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Involvement in disease
Bothnia retinal dystrophy (BRD); Rod-cone dystrophy Newfoundland (NFRCD); Retinitis punctata albescens (RPA)
Subcellular Location
Cytoplasm.
Tissue Specificity
Retina and pineal gland. Not present in photoreceptor cells but is expressed abundantly in the adjacent retinal pigment epithelium (RPE) and in the Mueller glial cells of the retina.
Database Links

HGNC: 10024

OMIM: 136880

KEGG: hsa:6017

STRING: 9606.ENSP00000268125

UniGene: Hs.1933

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