Recombinant Human CRABP1 Protein

Name: Recombinant Human CRABP1 Protein
Brand: Beta LifeScience
SKU: BLPSN-1412
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	N/A
Host Species	Human
Accession	AAH22069.1
Synonym	CRABP, CRABP-I, CRABPI, RBP5
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	HGNC: 2338 OMIM: 180230 KEGG: hsa:1381 STRING: 9606.ENSP00000299529 UniGene: Hs.346950

Gene Functions References

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
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
p75NTR and CRABP1 modulate the effect of fenretinide on neuroblastoma cells PMID: 26843908
miR-93/miR-106b/miR-375-CIC-CRABP1 is a novel key regulatory axis in prostate cancer progression PMID: 26124181
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
the first evidence of pro-tumorigenic and pro-metastatic activity of CRABP1 in mesenchymal and neuroendocrine tumors. PMID: 24626200
we demonstrated significant changes in CRABP1 and CRABP2 expression in non-small cell lung cancer samples PMID: 25034531
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
Results describe the mRNA expression of CRABP1, RERG, and GRP in pituitary adenomas. PMID: 21270509
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
Loss of cellular retinoic acid binding protein 1 function due to hypermethylation of its promoter leads to pathogenesis of papillary thyroid carcinoma PMID: 12640681
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
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
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
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
Real-time RT-PCR analysis disclosed a significant lack of CRABP-I expression in four renal cell carcinoma cell lines PMID: 16254461
Hypermethylation was subsequently identified for three of four analyzed genes, ADAMTS1 (85%), CRABP1 (90%), and NR3C1 (35%). PMID: 17167179
Frequent methylation-associated silencing of CRABP1 is associated with esophageal squamous-cell carcinoma PMID: 17438526
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
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
supports an active role for PLZF and RARalpha-PLZF in leukemogenesis, identifies up-regulation of CRABPI PMID: 18000064
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

FAQs

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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.