Recombinant Human CRABP1 Protein

Beta LifeScience SKU/CAT #: BLPSN-1412

Recombinant Human CRABP1 Protein

Beta LifeScience SKU/CAT #: BLPSN-1412
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Product Overview

Tag N/A
Host Species Human
Accession AAH22069.1
Background CRABP1 is a specific binding protein for a vitamin A family member. It is thought that CRABP1 plays an important role in retinoic acid-mediated differentiation and proliferation processes. CRABP1 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. It forms a beta-barrel structure which accommodates hydrophobic ligands in its interior.
Description A DNA sequence encoding human CRABP1 (AAH22069.1)(Met1-Glu137) was expressed.
Source E.coli
Predicted N Terminal Met
AA Sequence Met1-Glu137
Molecular Weight The recombinant human CRABP1 consists of 137 a.a. and predicts a molecular mass of 15.5 KDa. It migrates as an approximately 14 KDa band in SDS-PAGE under reducing conditions.
Purity >95% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile 20mM tris , 10% glycerol, pH 8.0..
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Cytosolic CRABPs may regulate the access of retinoic acid to the nuclear retinoic acid receptors.
Subcellular Location Cytoplasm.
Protein Families Calycin superfamily, Fatty-acid binding protein (FABP) family
Database References

Gene Functions References

  1. We conclude that the underexpression of CRABP1 and the overexpression of LCN2 may be useful diagnostic biomarkers in thyroid tumours with questionable malignity, and the overexpression of LCN2 and C1QL1 may be useful for prognostic purposes. PMID: 29321030
  2. Holo-CRABPs had higher affinity for CYP26B1 than free atRA, but both apo-CRABPs(CRABP-I and CRABP-II ) inhibited the formation of 4-OH-RA by CYP26B1. PMID: 27416800
  3. p75NTR and CRABP1 modulate the effect of fenretinide on neuroblastoma cells PMID: 26843908
  4. miR-93/miR-106b/miR-375-CIC-CRABP1 is a novel key regulatory axis in prostate cancer progression PMID: 26124181
  5. CRABP1 expression is maintained in ER- and triple-negative breast tumors, and that elevated levels of CRABP1 is a significant indicator of high tumor grade, Ki67 immunoreactivity, and poor prognosis. PMID: 26142905
  6. the first evidence of pro-tumorigenic and pro-metastatic activity of CRABP1 in mesenchymal and neuroendocrine tumors. PMID: 24626200
  7. we demonstrated significant changes in CRABP1 and CRABP2 expression in non-small cell lung cancer samples PMID: 25034531
  8. Factors involved in the retinoid pathway, in particular upregulation of CRBP, CRABP1 and CRABP2, also showed differential expression in tumors with different histological subtypes PMID: 24269351
  9. Results describe the mRNA expression of CRABP1, RERG, and GRP in pituitary adenomas. PMID: 21270509
  10. reduced expression of CRABP1 has a potential as a prognostic marker for serous adenocarcinoma which is the most frequent histological ovarian tumor type and also for clear cell carcinoma that often exhibits chemo-resistance. PMID: 20571827
  11. Loss of cellular retinoic acid binding protein 1 function due to hypermethylation of its promoter leads to pathogenesis of papillary thyroid carcinoma PMID: 12640681
  12. CSF of Moyamoya Disease [MMD] patients reveals high CRABP-I expression suggesting that the elevation of CRABP-I in CSF may be a candidate for pathogenesis of MMD PMID: 14605320
  13. CRABP I plays an important role not only in mediating the retinoid effects, but also in modulating the radiation sensitivity of tumour cells after combined retinoic acid radiation treatment. PMID: 14713576
  14. increased CYP26-mediated catabolism of retinoic by CRABP-I transfection might decrease the amount of retinoic acid that is accessible to the nuclear receptors PMID: 15281009
  15. Decreases in the CRABP1 (cellular retinoic acid binding protein 1) and TFF3 (trefoil factor 3) expression levels identified these as candidate molecular biomarkers for papillary thyroid carcinoma. PMID: 15515157
  16. Real-time RT-PCR analysis disclosed a significant lack of CRABP-I expression in four renal cell carcinoma cell lines PMID: 16254461
  17. Hypermethylation was subsequently identified for three of four analyzed genes, ADAMTS1 (85%), CRABP1 (90%), and NR3C1 (35%). PMID: 17167179
  18. Frequent methylation-associated silencing of CRABP1 is associated with esophageal squamous-cell carcinoma PMID: 17438526
  19. DNA hypermethylation of tumour suppressor genes seems to play an important role in ovarian carcinogenesis and HOXA9, HOXB5, SCGB3A1, and CRABP1 are identified as novel hypermethylated target genes in this tumour type PMID: 17623056
  20. As epidermal basal keratinocyte proliferation is stimulated by paracrine growth factors secreted by ATRA activated suprabasal keratinocytes, our results indicate that CRABPI overexpression in suprabasal keratinocytes enhances ATRA. PMID: 17727842
  21. supports an active role for PLZF and RARalpha-PLZF in leukemogenesis, identifies up-regulation of CRABPI PMID: 18000064
  22. The authors identified several dysregulated genes and proteins, but only the cellular retinoic acid binding protein 1 (CRABP1) was up-regulated exclusively in cells expressing an increased Abeta42/Abeta40 ratio. PMID: 19087254


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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