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NSJ Bioreagents

SKU:RQ8116

CRABP1 Antibody / Cellular retinoic acid-binding protein 1

CRABP1 Antibody / Cellular retinoic acid-binding protein 1

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Cellular retinoic acid-binding protein 1 is a protein that in humans is encoded by the CRABP1 gene. This gene encodes a specific binding protein for a vitamin A family member and is thought to play an important role in retinoic acid-mediated differentiation and proliferation processes. It is structurally similar to the cellular retinol-binding proteins, but binds only retinoic acid at specific sites within the nucleus, which may contribute to vitamin A-directed differentiation in epithelial tissue.

Specifications

Family Primary antibody
Formulation 0.5mg/ml if reconstituted with 0.2ml sterile DI water
Format Antigen affinity purified
Host Animal Rabbit
Clonality Polyclonal (rabbit origin)
Isotype Rabbit IgG
Species Reactivity Human
Application WB, FACS, Direct ELISA
Application Details Western blot: 0.5-1ug/ml,Flow cytometry: 1-3ug/million cells,Direct ELISA: 0.1-0.5ug/ml
Application Note Optimal dilution of the CRABP1 antibody should be determined by the researcher.
Immunogen E. coli-derived recombinant human protein (amino acids R60-E118) was used as the immunogen for the CRABP1 antibody.
Buffer Lyophilized from 1X PBS with 2% Trehalose
Purity Antigen affinity purified
Storage After reconstitution, the CRABP1 antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
Limitation This CRABP1 antibody is available for research use only.
Uniprot # P29762
Status Available
PDF Link https://www.nsjbio.com/tds-pdf/crabp1-antibody-cellular-retinoic-acid-binding-protein-1-rq8116
Title CRABP1 Antibody / Cellular retinoic acid-binding protein 1
Description Cellular retinoic acid-binding protein 1 is a protein that in humans is encoded by the CRABP1 gene. This gene encodes a specific binding protein for a vitamin A family member and is thought to play an important role in retinoic acid-mediated differentiation and proliferation processes. It is structurally similar to the cellular retinol-binding proteins, but binds only retinoic acid at specific sites within the nucleus, which may contribute to vitamin A-directed differentiation in epithelial tissue.
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