H_Products

Histamine dihydrochloride is a hydrophilic amine compound derived through the decarboxylation of histidine by L-histidine decarboxylase. It is a substrate used to assay histamine-N-methyltransferase ion-pair extraction of histamine using HPLC. Additionally, histamine dihydrochloride activates nitric oxide synthase and inhibits formation of reactive oxygen species.

Horseradish peroxidase (HRP) is the most commonly used antibody-conjugated enzyme. Substrates for HRP are luminol and benzidine substrates. Tetramethylbenzidine (TMB) and similar substrates are oxidized by HRP in the presence of hydrogen peroxide, or nontoxic substitutes, to yield a chinoid structure of intense blue color.

Hydrocortisone is a glucocorticoid primarily produced by the adrenal cortex. It is used as an anti-inflammatory and is researched for its immunosuppressive and for glucose metabolism regulation. Hydrocortisone completes its action on a wide scale by binding glucocorticoid receptors which upregulates anti-inflammatory protein synthesis.

Hygro99 is the purest form of Hygromycin B available. It is over 99% pure and should be used for the most sensitive applications and on the most sensitive cell lines. All impurities that might cause inhibition of resistant cell lines have been removed. In general, our Molecular Grade Hygromycin B (which is still ≥92 % pure and less expensive) will not adversely affect your cells and is suitable for most experiments.

Hygromycin B is an aminoglycoside antibiotic isolated from Streptomyces hygroscopicus. It is commonly used to study protein synthesis. Aside from its efficacy against bacteria, fungi, and higher eukaryotic cells, hygromycin B is also an antiviral agent inhibiting translation upon selectively entering cells made permeable due to viral infection. It works as a standard selection antibiotic in gene experiments, especially for selection of hygromycin resistance gene transformed cells.

The Hygromycin B EZ Pak™ is the fastest and easiest way to make a set amount of sterile hygromycin B solution. The kit includes pre-weighed hygromycin B powder, a sterile filter and a sterile container for the filtered solution. No need to calculate, simply add the stated amount of deionized H₂O, filter, and pour into the labeled bottle for easy usage. The EZ Pak™ includes high quality GoldBio hygromycin B and the sterile solution is ready for tissue culture, bacterial media or any other appropriate use.

Interferon alpha1 belongs to the type I interferon family and is encoded by the IFNA1 gene in humans. It is expressed in peripheral blood leukocytes and lymphoblastoid cells. It plays an important role in inducing non-specific resistance against a broad range of viral infections, and also affects cell proliferation and modulates immune responses. Interferon alpha proteins represent a group of related but distinct proteins that share over 95 % amino acid sequence homology. IFNA1 contains four highly conserved cysteine residues which form two disulfide bonds, one of which is necessary for biological activity. IFNalpha1A differs from IFNalpha1B by having one alanine residue in a position where IFNalpha1B has a valine.

Interferon alpha1 belongs to the type I interferon family and is encoded by the IFNA1 gene in humans. It is expressed in peripheral blood leukocytes and lymphoblastoid cells. It plays an important role in inducing non-specific resistance against a broad range of viral infections. It also affects cell proliferation and modulates immune responses. Interferon alpha proteins represent a group of related but distinct proteins that share over 95 % amino acid sequence homology. IFNA1 contains four highly conserved cysteine residues which form two disulfide bonds, one of which is necessary for biological activity. IFNalpha1B differs from IFNalpha1A by having one valine residue in a position where IFNalpha1A has an alanine.

Interferon alpha2 belongs to the type I interferon family and is encoded by the IFNA2 gene in humans. Like the other IFN-alpha proteins, it is expressed in leukocytes and plays an important role in inducing non-specific resistance against a broad range of viral infections. Recombinant IFN-alpha2A has been used to induce regression of corticosteroid-resistant hemangiomas in infancy. IFNA2 is one of 13 subtypes of interferon alpha found in humans, clustered on chromosome 9. It contains four highly conserved cysteine residues forming two disulfide bonds, one of which is necessary for biological activity.

Interferon alpha2 belongs to the type I interferon family and is encoded by the IFNA2 gene in humans. Like the other IFN-alpha proteins, it is expressed in leukocytes and plays an important role in inducing non-specific resistance against a broad range of viral infections. Studies have shown the ability of recombinant IFN-alpha2B to decrease hepatic metastases from intraocular melanoma. It used to treat high-risk cutaneous melanomas, but is associated with many contraindications. IFNA2 is one of 13 subtypes of interferon alpha found in humans, clustered on chromosome 9. It contains four highly conserved cysteine residues forming two disulfide bonds, one of which is necessary for biological activity.

Interferon alpha2 belongs to the type I interferon family and is encoded by the IFNA2 gene in humans. Like the other IFN-alpha proteins, it is expressed in leukocytes and plays an important role in inducing non-specific resistance against a broad range of viral infections. Studies have shown the ability of recombinant IFN-alpha2B to decrease hepatic metastases from intraocular melanoma. It used to treat high-risk cutaneous melanomas, but is associated with many contraindications. IFNA2 is one of 13 subtypes of interferon alpha found in humans, clustered on chromosome 9. It contains four highly conserved cysteine residues forming two disulfide bonds, one of which is necessary for biological activity.

Interferon gamma is the only type II interferon found in humans and binds to the heterodimeric IFNGR that consists of two chains, IFNGR1 and IFNGR2. This interaction activates the JAK-STAT pathway. IFNG is produced primarily by T-lymphocytes and natural killer (NK) cells. It is critical for innate and adaptive immunity against viral and intracellular bacterial infections. This is partly due to its ability to inhibit viral replication directly, but also due to its immunostimulatory and immunomodulatory effects. IFNG induces the production of cytokines and upregulates the expression of class I and II MHC antigens, Fc receptors, and leukocyte adhesion molecules. It modulates macrophage effector functions, influences isotype switching, and potentiates the secretion of immunoglobulins by B cells. Additionally, IFNG augments TH1 cell expansion and may be required for TH1 cell differentiation.

Interferon lambda 1, also known as interleukin 29, belongs to the newly classified type III interferon family. Expression of IFNL1 is seen in a variety of cell types in response to viral infection or treatment with double-stranded RNA. IFNL1 exerts antiviral activity and upregulation of MHC class I antigen expression. It signals through a heterodimeric receptor complex composed of IL10RB and IFNLR1 which activates the JAK-STAT pathway, phosphorylating STAT1, STAT2, and STAT3.

Interferon omega 1 is a member of the type I family of interferons. It is the only functional interferon omega gene in humans; many pseudogenes of interferon omega exist in humans, some of which are functional in non-primate placental mammals. Expression of IFNW1 is seen in leukocytes in response to viral infection or treatment with double-stranded RNA. It stimulates NK cell activity, enhances expression of major histocompatibility complex class I antigens, and inhibits proliferation of lymphocytes stimulated with mitogens or allogeneic cells. It also inhibits proliferation of a variety of tumor cell lines in vitro.

IGF1 belongs to the insulin gene family. It is a mitogenic polypeptide growth factor that stimulates the proliferation and survival of various cell types including muscle, bone, and cartilage tissue in vitro. IGF1 DES is a truncated variant of human IGF1 with the tripeptide Gly-Pro-Glu absent from the N-terminus. It has been isolated from bovine colostrum, human brain, and porcine uterus. The IGF1 DES is believed to result from post-translational cleavage of IGF1 via protease activity. It is about 10-fold more potent than IGF1 at stimulating hypertrophy and proliferation of cultured cells, a consequence of much reduced binding to IGF-binding proteins, which is in turn caused by the absence of the glutamate at position 3. Clinical opportunities for IGF1-DES have not yet been evaluated, but could apply in catabolic states as well as for the treatment of inflammatory bowel diseases.

The Insulin-like growth factors (IGFs) are mitogenic polypeptide growth factors, predominantly produced in the liver, that stimulate the proliferation and survival of various cell types, including muscle, bone and cartilage tissue in vitro. IGFs belong to the Insulin gene family and are similar by structure and function to insulin, but have a much higher growth-promoting activity. IGF1 expression is regulated by growth hormone, while IGF2 expression is influenced by placenta lactogen. Both IGF1 and IGF2 signal through the tyrosine kinase type I receptor (IGFIR). Mature IGFs are generated through proteolytic processing of inactive precursor proteins. Recombinant human IGF1 is a globular protein containing 70 amino acids and 3 intra-molecular disulfide bonds. This particular product has been labeled with the stable 15N isotope to help track its activity.

The Insulin-like growth factors (IGFs) are mitogenic polypeptide growth factors that stimulate the proliferation and survival of various cell types, including muscle, bone and cartilage tissue in vitro. They are predominantly produced in the liver. IGFs belong to the Insulin gene family and are similar by structure and function to insulin, but have a much higher growth-promoting activity. IGF1 expression is regulated by growth hormone, while IGF2 expression is influenced by placenta lactogen. Both IGF1 and IGF2 signal through the tyrosine kinase type I receptor (IGF IR). Mature IGFs are generated through proteolytic processing of inactive precursor proteins. Recombinant human IGF1 is a globular protein containing 70 amino acids, and 3 intra-molecular disulfide bonds.

Sterile Filtered White lyophilized powder. Purified and tested for use in cell culture.

Insulin-like Growth Factor-Binding Protein 3 (IGFBP3) belongs to the IGFBP family, which are all proteins with conserved cysteine residues, an IGFBP domain, and a thyroglobulin type-I domain. IGFBP3 is expressed by most tissues and is the most abundant IGFBP protein. It has higher levels of expression during postnatal life, which peak during puberty. The expression of IGFBP3 in fibroblasts is stimulated by a number of mitogenic growth factors. The protein forms a ternary complex with IGFI or IGFII, and an acid-labile subunit, causing it to circulate in the plasma. As this complex, it prolongs the half-life of IGFs and alters their interaction with cell surface receptors. Decreased plasma levels of IGFBP3 often happen during the progression of prostate cancer from benign to metastatic disease.

IGFBP7 belongs to the superfamily of insulin-like growth factor (IGF) binding proteins and is encoded by the IGFBP7 gene in human. It is expressed in a wide range of normal human tissues and it generally shows reduced expression in cancer cell lines of prostate, breast, colon, and lung origin. IGFBP7 includes conserved cysteine residues. IGFBP7 modulates the biological activities of IGF proteins. It also suppresses growth and colony formation of prostate and breast cancer cell lines. Above all, IGFBP7 is a very important factor in skeletal myogenesis. Human IGFBP7 cDNA encodes a 282 amino acid (a.a.) residue precursor protein with a putative 26 a.a. signal peptide.

Interleukin-10 (IL10), also known as cytokine synthesis inhibitory factor (CSIF), is the charter member of the IL10 family of F-helical cytokines that also includes IL19, IL20, IL22, IL24, and IL26/AK155. While the gene which encodes IL10 is comprised of 178 amino acids, the active protein only contains 160 amino acids. IL10 contains two intrachain disulfide bridges and is expressed as a 36 kDa noncovalently associated homodimer. The IL10 dimer binds to two IL10 RF/IL10R1 chains, resulting in the recruitment of two IL10 RH/IL10R2 chains and the activation of a signaling cascade involving JAK1, TYK2, and STAT3. IL10RH does not bind IL10 directly, but is required for signal transduction. IL10 is also a critical molecule in the control of viral infections, allergic reactions and autoimmune inflammation. IL10 promotes phagocytic uptake and Th2 responses, but suppresses antigen presentation and Th1 pro-inflammatory responses. IL10 is secreted by many activated hematopoietic cell types, as well as hepatic stellate cells, keratinocytes and placental cytotrophoblasts. Human IL10 is active on mouse cells; however mouse IL10 does not act on human cells.