Recombinant Human FABP6 Protein

Name: Recombinant Human FABP6 Protein
Brand: Beta LifeScience
SKU: BLPSN-1956
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	N/A
Host Species	Human
Accession	AAH22489.1
Synonym	I-15P, I-BABP, I-BALB, I-BAP, ILBP, ILBP3, ILLBP
Background	Gastrotropin, also known as Fatty acid-binding protein 6, Ileal lipid-binding protein, ILBP, Intestinal 15 kDa protein, Intestinal bile acid-binding protein, I-BABP and FABP6, is a cytoplasm protein which belongs to thecalycin superfamily and Fatty-acid binding protein (FABP) family. Isoform2 of FABP6 is expressed in colorectal adenocarcinomas and their adjacent normal mucosa (at protein level). Isoform1of FABP6 is expressed in the jejunum, ileum, cecum and ascending colon intestine. Isoform2is expressed in the gallbladder, duodenum, jejunum, ileum, cecum, ascending, transverse and descending colon, sigmoid colon and rectum. FABP6 / I-BABP is a cancer-related protein that acts as an intracellular transporter of bile acid in the ileal epithelium. FABP6 / I-BABP may also play an important role in early carcinogenesis.
Description	A DNA sequence encoding the human FABP6 (AAH22489.1) (Met 1-Ala 128) was expressed and purified.
Source	E.coli
Predicted N Terminal	Met 1
AA Sequence	Met 1-Ala 128
Molecular Weight	The recombinant human FABP6 consisting of 128 a.a. and has a calculated molecular mass of 14.4 kDa as estimated in SDS-PAGE under reducing conditions.
Purity	>98% as determined by SDS-PAGE
Endotoxin	Please contact us for more information.
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile PBS, pH 7.5.
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	Binds to bile acids and is involved in enterohepatic bile acid metabolism. Required for efficient apical to basolateral transport of conjugated bile acids in ileal enterocytes. In vitro binds to bile acids in the order: deoxycholic acid > cholic acid > chenodeoxycholic acid and respective BA conjugation modifies affinities in the order taurine-conjugated > glycine-conjugated > unconjugated bile acids. Stimulates gastric acid and pepsinogen secretion.; Essential for the survival of colon cancer cells to bile acid-induced apoptosis.
Subcellular Location	[Isoform 1]: Cytoplasm. Membrane; Peripheral membrane protein; Cytoplasmic side.; [Isoform 2]: Cytoplasm.
Protein Families	Calycin superfamily, Fatty-acid binding protein (FABP) family
Database References	HGNC: 3561 OMIM: 600422 KEGG: hsa:2172 STRING: 9606.ENSP00000377549 UniGene: Hs.519719
Tissue Specificity	Isoform 1 is expressed in the jejunum, ileum, cecum and ascending colon intestine. Isoform 2 is xpressed in the gallbladder, duodenum, jejunum, ileum, cecum, ascending, transverse and descending colon, sigmoid colon and rectum. Isoform 2 is expressed in c

Gene Functions References

Structural determinants of ligand binding in the ternary complex of human ileal bile acid binding protein with glycocholate and glycochenodeoxycholate obtained from solution NMR PMID: 26613247
Analysis of slow and fast motions in I-BABP indicates largely different energy landscapes for the apo and holo states suggesting that optimization of binding interactions might be achieved by altering the dynamic behavior of specific protein segments. PMID: 25073073
show, using electrospray ionization mass spectroscopy, that human ILBP binds bile acids with a 3:1 ratio, even at low protein and ligand concentrations PMID: 23758264
Ursodeoxycholic acid induces unique conformational changes in IBABP. PMID: 22223860
NMR data are in agreement with a conformational selection model we proposed earlier for I-BABP and support the hypothesis of an allosteric mechanism of ligand binding PMID: 22329738
The-putative functional-Thr79Met substitution of FABP6 confers a protective effect on type 2 diabetes in obese individuals. PMID: 19744871
NMR structure of human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures PMID: 12486725
the I-BABP gene may be a novel target for PPAR in humans PMID: 15936983
ASBT and ILBP protein were 48% and 67% lower in normal weight gallstone carriers than in controls (P < 0.05); similar differences were found for mRNA expression levels. PMID: 16237211
The expression of FABP6 was higher in primary colorectal cancers and adenomas than in normal epithelium, but was dramatically decreased in lymph node metastases, suggesting that FABP6 may play an important role in early carcinogenesis. PMID: 16951225
In keeping with its role in the enterohepatic circulation and ileal reabsorption of bile acids, the gene promoter contains consensus elements for CDX2 and FXR. More than one transcription start site has been identified. PMID: 14654244

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.