IF Human

Intrinsic Factor Human Recombinant
Cat. No.
BT15751
Source
Sf9 Insect Cells.
Synonyms
Gastric intrinsic factor, Intrinsic factor, INF, IF, GIF, IFMH, TCN3, Cobalamin/Vitamin B-12 binding transport protein.
Appearance

Sterile Filtered pink solution.

Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Intrinsic Factor Human Recombinant produced in baculovirus is a glycosylated, polypeptide chain having a molecular mass of 55,000 Dalton.
The Intrinsic Factor is fused to a hexa-histidine at the C-terminus and purified by proprietary chromatographic techniques for removal of bound Vitamin B-12.

Product Specs

Introduction
Intrinsic Factor, a glycoprotein crucial for vitamin B12 absorption, is produced by gastric parietal cells. This protein facilitates the binding of vitamin B12 in the small intestine, allowing its absorption in the ileum. Essential for red blood cell development, mutations in the Intrinsic Factor gene can result in congenital pernicious anemia.
Description

Recombinant Human Intrinsic Factor, a glycosylated polypeptide, is produced using baculovirus expression system. With a molecular weight of 55 kDa, it features a C-terminal hexa-histidine tag. Purification is achieved through proprietary chromatography techniques to eliminate bound Vitamin B-12.

Physical Appearance

Sterile, pink solution.

Formulation

The protein is supplied in a solution containing 20mM HEPES buffer (pH 8.0), 100mM NaCl, and 20% Glycerol.

Stability
For short-term storage (up to 4 weeks), store at 4°C. For extended periods, store frozen at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity exceeds 95% as determined by:
(a) Reverse-phase high-performance liquid chromatography (RP-HPLC).
(b) Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE).
Synonyms
Gastric intrinsic factor, Intrinsic factor, INF, IF, GIF, IFMH, TCN3, Cobalamin/Vitamin B-12 binding transport protein.
Source
Sf9 Insect Cells.

Product Science Overview

Function and Mechanism

Vitamin B12 is essential for various bodily functions, including DNA synthesis and red blood cell formation. However, it cannot be absorbed directly by the body. When vitamin B12 enters the stomach, it binds to a protein called haptocorrin. This complex travels to the duodenum, where pancreatic enzymes digest haptocorrin, freeing vitamin B12. In the less acidic environment of the small intestine, vitamin B12 binds to intrinsic factor. This new complex then travels to the ileum, where specialized epithelial cells endocytose it. Inside the cell, vitamin B12 dissociates from intrinsic factor and binds to another protein, transcobalamin II, which transports it to the liver .

Recombinant Human Intrinsic Factor

Recombinant Human Intrinsic Factor is a laboratory-produced version of the naturally occurring protein. It is created using recombinant DNA technology, which involves inserting the gene responsible for producing intrinsic factor into a host cell, such as HEK293 cells. These cells then produce the protein, which can be harvested and purified for various applications .

Applications

Recombinant Human Intrinsic Factor is used in research and clinical diagnostics. It serves as a high-quality replacement for native porcine intrinsic factor, which has seen a decline in quality in recent years. The recombinant version is highly purified and offers a reliable and economical alternative. It is particularly useful in vitamin B12 assay development and other research applications .

Stability and Storage

Recombinant Human Intrinsic Factor is typically provided as a lyophilized powder, which is stable for up to twelve months when stored at -20°C to -80°C. It is recommended to store the protein under sterile conditions and avoid repeated freeze-thaw cycles to maintain its stability and activity .

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