Retinol-binding protein 4 Recombinant Protein | RBP4 recombinant protein

Recombinant human Retinol-binding protein 4 protein

Cat. Num. AAA717379

• Gene Names: RBP4; RDCCAS
• Applications: SDS-Page, ELISA
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Retinol-binding protein 4; Recombinant human Retinol-binding protein 4 protein; Plasma retinol-binding protein; RBP4 recombinant protein

• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence: MKWVWALLLLAALGSGRAERDCRVSSFRVKENFDKARFSGTWYAMAKKDPEGLFLQDNIVAEFSVDETGQMSATAKGRVRLLNNWDVCADMVGTFTDTEDPAKFKMKYWGVASFLQKGNDDHWIVDTDYDTYAVQYSCRLLNLDGTCADSYSFVFSRDPNGLPPEAQKIVRQRQEELCLARQYRLIVHNGYCDGRSERNLL

• Applicable Applications for RBP4 recombinant protein: SDS-PAGE, ELISA
• Preparation and Storage: Store working aliquots at 4 degree C for up to one week. For extended storage, conserve at -20 degree C or -80 degree C. Repeated freezing and thawing is not recommended.

Related Product Information for RBP4 recombinant protein

Delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin, this prevents its loss by filtration through the kidney glomeruli.

References

[1] "Cloning and sequencing of a full length cDNA coding for human retinol-binding protein." Colantuoni V., Romano V., Bensi G., Santoro C., Costanzo F., Raugei G., Cortese R. Nucleic Acids Res. 11:7769-7776(1983) [PubMed: 6316270] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2] "The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3] Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4] "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[5] "Structure and cell-specific expression of a cloned human retinol binding protein gene: the 5'-flanking region contains hepatoma specific transcriptional signals." D'Onofrio C., Colantuoni V., Cortese R. EMBO J. 4:1981-1989(1985) [PubMed: 2998779] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-189.

NCBI and Uniprot Product Information

• NCBI GI #: 55743122
• NCBI GeneID: 5950
• NCBI Accession #: NP_006735.2
• NCBI GenBank Nucleotide #: NM_006744.3
• UniProt Accession #: P02753; O43478; O43479; Q5VY24; Q8WWA3; Q9P178; D3DR38
• Molecular Weight: 29 kDa
• NCBI Official Full Name: retinol-binding protein 4
• NCBI Official Synonym Full Names: retinol binding protein 4, plasma
• NCBI Official Symbol: RBP4
• NCBI Official Synonym Symbols: RDCCAS
• NCBI Protein Information: retinol-binding protein 4; RBP; PRBP; plasma retinol-binding protein; retinol-binding protein 4, interstitial
• UniProt Protein Name: Retinol-binding protein 4
• Protein Family: Retinol-binding protein
• UniProt Gene Name: RBP4
• UniProt Synonym Gene Names: PRBP; RBP
• UniProt Entry Name: RET4_HUMAN

NCBI Description

This protein belongs to the lipocalin family and is the specific carrier for retinol (vitamin A alcohol) in the blood. It delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin which prevents its loss by filtration through the kidney glomeruli. A deficiency of vitamin A blocks secretion of the binding protein posttranslationally and results in defective delivery and supply to the epidermal cells. [provided by RefSeq, Jul 2008]

Uniprot Description

Function: Delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin, this prevents its loss by filtration through the kidney glomeruli.

Subcellular location: Secreted.

Involvement in disease: Retinal dystrophy, iris coloboma, and comedogenic acne syndrome (RDCCAS) [MIM:615147]: A disease characterized by retinal degeneration, ocular colobomas involving both the anterior and posterior segment, impaired night vision and loss of visual acuity. Additional characteristic features include developmental abnormalities and severe acne.Note: The disease is caused by mutations affecting the gene represented in this entry. Loss of functional RBP4 protein results in serum retinol deficiency. Lack of normal levels of retinol impairs the visual cycle leading to night blindness at early stages; prolonged deficiency may lead to retinal degeneration. Additionally, retinol deficiency may result in dry skin, increased susceptibility to infection and acne (Ref.14).

Sequence similarities: Belongs to the calycin superfamily. Lipocalin family.

Mass spectrometry: Molecular mass is 21063.46±1.88 Da from positions 17 - 199. Determined by ESI. Ref.10Molecular mass is 20534 Da from positions 19 - 197. Determined by MALDI. Ref.12Molecular mass is 20162 Da from positions 19 - 194. Determined by MALDI. Ref.12

Sequence caution: The sequence AAF69622.1 differs from that shown. Reason: Erroneous initiation.