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Human IGF-I, Fc Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 98%.

Immobilized Human IGF-I, Fc Tag (Cat. No. IG1-H4269) at 5 μg/mL (100 μL/well) can bind Human IGFBP-3, His Tag (Cat. No. IG3-H52H9) with a linear range of 0.125-1 μg/mL (QC tested).

Immobilized Human IGF-I R, His Tag (Cat. No. IGR-H5229) at 5 μg/mL (100 μL/well) can bind Human IGF-I, Fc Tag (Cat. No. IG1-H4269) with a linear range of 0.039-0.313 μg/mL (Routinely tested).

IG1-H4269 | Human IGF-I Protein, Fc Tag | ACRObiosystems available at Bio-Connect

Human IGF-I Protein, Fc Tag | IG1-H4269 | ACRObiosystems

Human IGF-I Protein, Fc Tag

Characteristics: This protein carries a human IgG1 Fc tag at the N-terminus. The protein has a calculated MW of 34.6 kDa. The protein migrates as 40 kDa under reducing (R) condition (SDS-PAGE). Description: Insulin-like growth factor 1 (IGF-1 or IGF-I), also known as somatomedin C, is the dominant effector of growth hormone and is structurally homologous to proinsulin. Human IGF-1 is synthesized as two precursor isoforms with N- and alternate C‑terminal propeptides (1). These isoforms are differentially expressed by various tissues (1). The 7.6 kDa mature IGF‑1 is identical between isoforms and is generated by proteolytic removal of the N- and C‑terminal regions. Mature human IGF-1 shares 94% and 96% aa sequence identity with mouse and rat IGF-1, respectively (2), and exhibits cross-species activity. It shares 64% aa sequence identity with mature human IGF2. Circulating IGF-1 is produced by hepatocytes, while local IGF-1 is produced by many other tissues in which it has paracrine effects (1). IGF-1 induces the proliferation, migration, and differentiation of a wide variety of cell types during development and postnatally (3). IGF-1 regulates glucose and fatty acid metabolism, steroid hormone activity, and cartilage and bone metabolism (4‑7). It plays an important role in muscle regeneration and tumor progression (1, 8). IGF-1 binds IGF1R, IGF2R, and the insulin receptor, although its effects are mediated primarily by IGF1R (9). IGF-1 association with IGF binding proteins increases its plasma half‑life and modulates its interactions with receptors (10).

Human VEGF-C, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.

Immobilized Human VEGF R3, Fc Tag (Cat. No. FL4-H5251) at 5 μg/mL (100 μL/well) can bind Human VEGF-C, His Tag (Cat. No. VEC-H4225) with a linear range of 2-20 ng/mL (QC tested).

Human VEGF-C / Flt4-L Protein, His Tag (MALS verified) | VEC-H4225 | ACRObiosystems available at Bio-Connect

Human VEGF-C / Flt4-L Protein, His Tag... | VEC-H4225 | ACRObiosystems

Human VEGF-C / Flt4-L Protein, His Tag (MALS verified)

Characteristics: This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 14.9 kDa. The protein migrates as 19-25 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation. Description: Vascular endothelial growth factor C is also known as VEGFC, Flt4-L and VRP, it contains the C-terminal propeptide which has an unusual structure with tandemly repeated cysteine-rich motifs. Upon biosynthesis, VEGFC is secreted as a non-covalent momodimer in an anti-parellel fashion. VEGFC is a member of the platelet-derived growth factor/vascular endothelial growth factor (PDGF/VEGF) family, is active in angiogenesis, lymphangiogenesis and endothelial cell growth and survival, and can also affect the permeability of blood vessels. This secreted protein undergoes a complex proteolytic maturation, generating multiple processed forms that bind and activate VEGFR-3 receptors. Only the fully processed form can bind and activate VEGFR-2 receptors. The structure and function of this protein is similar to those of vascular endothelial growth factor D (VEGF-D). VEGFC may function in angiogenesis of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Overexpression of VEGF-C causes lymphatics to enlarge possibly facilitates metastasis.

Human Transferrin, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.

Immobilized Human Transferrin, His Tag (Cat. No. TRN-H4229) at 2 μg/mL (100 μL/well) can bind Biotinylated Human Transferrin R, His Tag, primary amine labeling (Cat. No. TFR-H8243) with a linear range of 5-78 ng/mL (QC tested).

Human Transferrin Protein, His Tag (MALS verified) | TRN-H4229 | ACRObiosystems available at Bio-Connect

Human Transferrin Protein, His Tag (MA... | TRN-H4229 | ACRObiosystems

Human Transferrin Protein, His Tag (MALS verified)

Characteristics: This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 76.0 kDa. The protein migrates as 70-90 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation. Description: Transferrin is also known as Serotransferrin, Beta-1 metal-binding globulin, TF, and is iron-binding blood plasma glycoproteins that control the level of free iron in biological fluids. Although iron bound to transferrin is less than 0.1% (4 mg) of the total body iron, it is the most important iron pool, with the highest rate of turnover (25 mg/24 h). The affinity of transferrin for Fe(III) is extremely high (1023 M−1 at pH 7.4) but decreases progressively with decreasing pH below neutrality.When not bound to iron, it is known as "apo-transferrin”. In humans, transferrin consists of a polypeptide chain containing 679 amino acids. It is a complex composed of alpha helices and beta sheets to form two domains (the first situated in the N-terminus and the second in the C-terminus). The N- and C- terminal sequences are represented by globular lobes and between the two lobes is an iron-binding site. The liver is the main source of manufacturing transferrin, but other sources such as the brain also produce this molecule . Transferrin is also associated with the innate immune system. Transferrin is found in the mucosa and binds iron, thus creating an environment low in free iron that impedes bacteria survival in a process called iron withholding. The level of transferrin decreases in inflammation. The metal binding properties of transferrin have a great influence on the biochemistry of plutonium in humans. Transferrin has a bacteriocidal effect on bacteria, in that it makes Fe3+ unavailable to the bacteria.Carbohydrate deficient transferrin increases in the blood with heavy ethanol consumption and can be monitored via laboratory testing.

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