Recombinant Human Intrinsic Factor Protein (His Tag)

Name: Recombinant Human Intrinsic Factor Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-3011
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	P27352
Synonym	IF, IFMH, INF, TCN3
Background	Gastric intrinsic factor, also known as GIF, belongs to the of the cobalamin transport protein family. It is a glycoprotein produced by the parietal cells of the stomach. Gastric intrinsic factor plays a key role in the absorption of vitamin B12 on in the small intestine. Vitamin B12 bounds to haptocorrin after entry into the stomach. The resulting complex enters the duodenum, where pancreatic enzymes digest haptocorrin. In the less acidic environment of the small intestine, B12 can then bind to gastric intrinsic factor. This new complex travels to the ileum, where special epithelial cells endocytose them. Inside the cell, B12 dissociates once again and binds to another protein, transcobalamin II. The new complex can exit the epithelial cells to enter the liver.
Description	A DNA sequence encoding the human GIF (P27352-1) (Met1-Tyr417) was expressed with a His tag at the C-terminus.
Source	HEK293
Predicted N Terminal	Ser 19
AA Sequence	Met1-Tyr417
Molecular Weight	The recombinant human GIF consists of 410 a.a. and predicts a molecular mass of 44.8 KDa. It migrates as an approximately 49 KDa band in SDS-PAGE under reducing conditions.
Purity	>95% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile PBS, pH 7.4.
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	Promotes absorption of the essential vitamin cobalamin (Cbl) in the ileum. After interaction with CUBN, the CBLIF-cobalamin complex is internalized via receptor-mediated endocytosis.
Subcellular Location	Secreted.
Protein Families	Eukaryotic cobalamin transport proteins family
Database References	HGNC: 4268 OMIM: 261000 KEGG: hsa:2694 STRING: 9606.ENSP00000257248 UniGene: Hs.110014
Associated Diseases	Hereditary intrinsic factor deficiency (IFD)
Tissue Specificity	Gastric mucosa.

Gene Functions References

the present findings reveal that High-altitude polycythemia -induced gastric mucosal lesion inspires the protection responses by up-regulating APOA4 and APOC3, and down-regulating GIF. PMID: 26485402
Our genetic screening of 154 families of patients with inherited cobalamin malabsorption revealed population-specific mutations, mutational hotspots, and functionally distinct regions in the three causal genes: CUBN, AMN, and GIF. PMID: 22929189
Acute lymphoblastic leukemia and vitamin B12 deficiency secondary to a gastric intrinsic factor gene mutation PMID: 22556038
crystal structure of the complex between IF-Cbl and the cubilin IF-Cbl-binding-region (CUB(5-8)) determined at 3.3 A resolution PMID: 20237569
A polymorphism in the gastric intrinsic factor gene is associated with congenital intrinsic factor deficiency. PMID: 14695536
The parameters obtained for ligand and receptor binding in this study indicate that both full-length 50-kDA intrinsic factor and its 30-kDa and 20-kDa fragments may be involved in assimilation of cobalamin. PMID: 15736970
possible basis for the lack of interchangeability of human and rat IF receptors is presented PMID: 17954916
The Q5R mutation of the intrinsic factor gene predisposes to adult-onset pernicious anemia & other causes of low vitamin B12. In this mutation, intrinsic factor secretion is preserved but B12 absorption may be impaired. PMID: 18338170
a specific GIF mutation to be responsible for all Juvenile cobalamin deficiency cases of West-African origin so far was identified PMID: 19036097

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.