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3\\\'-Amino-2\\\'-hydroxybiphenyl-3-carboxylic+acid


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Supplier:  Bioss
Description:   ADRM1 is a 407 amino acid protein that localizes to both the nucleus and the cytoplasm and is thought to be involved in protein recruitment and cell adhesion. An integral membrane protein, ADRM1 functions to recruit UCH-L5, a deubiquitinating enzyme, to the 26S proteasome, and once at the proteasome it promotes the activity of UCH-L5. Additionally, ADRM1 is thought to mediate lymphocyte adhesion in endothelial cells and may thus play a role in lymphocyte homing. ADRM1 expression is induced by IFN-g in some cancer cell lines and its expression is upregulated in other metastatic cells, suggesting a role in carcinogenesis. Two isoforms of ADRM1 exist due to alternative splicing events.

Supplier:  Bioss
Description:   BMP2 belongs to the transforming growth factor-beta (TGFB) superfamily of secreted growth factors. It is a disulfide-linked homodimer and induces bone and cartilage formation. In addition to its osteogenic activity, BMP2 plays an important role in cardiac morphogenesis and is expressed in a variety of tissues including lung, spleen, brain, liver, prostate ovary and small intestine. The functional form of BMP2 is a 26 kDa protein composed of two identical 114 amino acid polypeptide chains linked by a single disulfide bond. BMPs control fundamental events in early embryonic development, organogenesis and adult tissue homeostasis.
Catalog Number: (10362-706)

Supplier:  Bioss
Description:   BMP2 belongs to the transforming growth factor-beta (TGFB) superfamily of secreted growth factors. It is a disulfide-linked homodimer and induces bone and cartilage formation. In addition to its osteogenic activity, BMP2 plays an important role in cardiac morphogenesis and is expressed in a variety of tissues including lung, spleen, brain, liver, prostate ovary and small intestine. The functional form of BMP2 is a 26 kDa protein composed of two identical 114 amino acid polypeptide chains linked by a single disulfide bond. BMPs control fundamental events in early embryonic development, organogenesis and adult tissue homeostasis.
Supplier:  Bioss
Description:   BMP2 belongs to the transforming growth factor-beta (TGFB) superfamily of secreted growth factors. It is a disulfide-linked homodimer and induces bone and cartilage formation. In addition to its osteogenic activity, BMP2 plays an important role in cardiac morphogenesis and is expressed in a variety of tissues including lung, spleen, brain, liver, prostate ovary and small intestine. The functional form of BMP2 is a 26 kDa protein composed of two identical 114 amino acid polypeptide chains linked by a single disulfide bond. BMPs control fundamental events in early embryonic development, organogenesis and adult tissue homeostasis.

Supplier:  PeproTech, Inc.
Description:   BMPs (Bone Morphogenetic Proteins) belong to the TGF-beta superfamily of structurally related signaling proteins. BMP-2 is a potent osteoinductive cytokine, capable of inducing bone and cartilage formation in association with an osteoconductive carrier such as collagen and synthetic hydroxyapatite. In addition to its osteogenic activity, BMP-2 appears to play an important role in cardiac morphogenesis, and is expressed in a variety of other tissues, including lung, liver, spleen, prostate, ovary, and small intestine. The functional form of BMP-2 is a 26 kDa protein composed of two identical 114 amino acid polypeptide chains (monomers) linked by a single disulfide bond. Each BMP-2 monomer is expressed as the C-terminal part of a precursor polypeptide, which also contains a 23 amino acid signal sequence for secretion, and a 259 amino acid propeptide. After dimerization of this precursor, the covalent bonds between the propeptide (which is also a disulfide-linked homodimer) and the mature BMP-2 ligand are cleaved by a furin-type protease. Recombinant Human/Murine/Rat BMP-2 derived from CHO cells is a homodimeric glycoprotein that consists of two 114 amino acid polypeptide chains linked by a single disulfide bond. Due to glycosylation, CHO cell-derived Human/Murine/Rat BMP-2 migrates at an apparent molecular weight of approximately 28-29 kDa by SDS-PAGE analysis under non-reducing conditions.
Supplier:  Bioss
Description:   ADRM1 is a 407 amino acid protein that localizes to both the nucleus and the cytoplasm and is thought to be involved in protein recruitment and cell adhesion. An integral membrane protein, ADRM1 functions to recruit UCH-L5, a deubiquitinating enzyme, to the 26S proteasome, and once at the proteasome it promotes the activity of UCH-L5. Additionally, ADRM1 is thought to mediate lymphocyte adhesion in endothelial cells and may thus play a role in lymphocyte homing. ADRM1 expression is induced by IFN-g in some cancer cell lines and its expression is upregulated in other metastatic cells, suggesting a role in carcinogenesis. Two isoforms of ADRM1 exist due to alternative splicing events.
Supplier:  Bioss
Description:   ADRM1 is a 407 amino acid protein that localizes to both the nucleus and the cytoplasm and is thought to be involved in protein recruitment and cell adhesion. An integral membrane protein, ADRM1 functions to recruit UCH-L5, a deubiquitinating enzyme, to the 26S proteasome, and once at the proteasome it promotes the activity of UCH-L5. Additionally, ADRM1 is thought to mediate lymphocyte adhesion in endothelial cells and may thus play a role in lymphocyte homing. ADRM1 expression is induced by IFN-g in some cancer cell lines and its expression is upregulated in other metastatic cells, suggesting a role in carcinogenesis. Two isoforms of ADRM1 exist due to alternative splicing events.
Supplier:  Enzo Life Sciences
Description:   S5a/Rpn10 is a major ubiquitin binding protein that binds preferentially to polyubiquitin chains. It is found as a non-ATPase subunit of the 19S regulatory complex of the 26S proteasome where it functions as a receptor for proteins destined for proteolytic degradation.In yeast, the homologue of S5a, Rpn10, is required for degradation of a subset of cellular proteins by the proteasome.  Unlike other proteasome subunits, S5a exists predominantly as a free protein in the cytosol (i.e. not incorporated into the proteasome), though its precise role in the cytosol has yet to be fully elucidated. S5a contains two approximately 15 amino acid ubiquitin interacting motifs (UIM) which are responsible for its binding to polyubiquitin chains.
Catalog Number: (10281-470)

Supplier:  Bioss
Description:   SNX2 and SNX4 share a high degree of amino acid similarity with SNX1, as they all contain a characteristic phox homology (PX) domain (4). These proteins are all partially associated with cellular membranes, and they, likewise, associate with EGF, PDGF and insulin receptor tyrosine kinases (2). These nexins are widely expressed and yet have various tissue distribution patterns. Additionally, the sorting nexins can associate with each other and with a variety of other cellular proteins, suggesting that they exist as part of multisubunit complexes (1,5). The related protein, SNX3, comprises a distinct subgroup of nexins that share less sequence similarity outside of the PX domain and have dramatically different binding affinities for the tyrosine kinase receptors (2,6).
Supplier:  Rockland Immunochemical
Description:   HEPES is a zwitterionic organic chemical buffering agent.
Supplier:  GE Healthcare - Life Sciences
Description:   Empty columns with high pressure stability (able to withstand up to 20 bar of pressure) and high flow rates are compatible for packing with modern BioProcessâ„¢ chromatography media, such as MabSelectâ„¢ and Captoâ„¢ for process development and preparative chromatography. The columns are designed to be used in aqueous solutions and nearly all organic solvents commonly used in liquid chromatography of biomolecules, with the following few exceptions: chlorinated hydrocarbons, acetone and other ketones, aliphatic esters and phenol. Solutions containing more than 2 M NaOH, 1 M HCl, other strong mineral acids or 75% acetic acid should not be used. The column hardware consists of borosilicate glass, PC, PA (reinforced glass fibre), EPDM, POM, PEEK, ETFE, Fluoro-rubber, PP and PA (nylon).
Product available on GSA Advantage®

Supplier:  Genetex
Description:   NCAM, as a member of the immunoglobulin superfamily of adhesion molecules is characterized by several immunoglobulin (Ig)-like domains. The extracellular part of NCAM consists of five of these Ig domains and two fibronectin type III homology regions. NCAM is encoded by a single copy gene composed of 26 exons. However, at least 20-30 distinct isoforms can be generated by alternative splicing and by posttranslational modifications, such as sialylation. During sialylation, polysialic acid (PSA) carbohydrates are attached to the extracellular part of NCAM. Through its extracellular region, NCAM mediates homophilic interactions. In addition, NCAM can also undergo heterophilic interactions by binding extracellular matrix components, such as laminin, or other cell adhesion molecules, such as integrins. NCAM is expressed on most neuroectodermal derived cell lines, tissues and neoplasm such as retinoblastoma, medulloblastoma, astrocytomas and neuroblastoma.
Catalog Number: (75791-712)

Supplier:  Prosci
Description:   ICAM-2 is a 55-65 kD transmembrane glycoprotein possessing 2 extracellular Ig domains, a single transmembrane domain, and a short 26-amino acid cytoplasmic domain. ICAM-2 is expressed on most leukocytes, and is strongly expressed on vascular endothelial cells. Interactions of ICAM-2 and the integrin receptors mediate cell adhesion in a wide range of lymphocyte, monocyte, natural killer cell, and granulocytewith other cells, and play important roles in many adhesion-dependent immune and inflammation responses, such as T cell aggregation, NK-cell cytotoxicity and migration, lymphocyte recirculation, etc. Serum levels of ICAM-2 correlated significantly with the inflammatory and course sequences of trichinosis in mice and had a similar relation with blood eosinophilia. So, estimation of ICAM-2 serum levels may prove useful in diagnosis of trichinosis recent infections, and in monitoring the prognosis and response to treatment.
Supplier:  Bioss
Description:   Proteins containing RNA recognition motifs, including various hnRNP proteins, are implicated in the regulation of alternative splicing and protein components of snRNPs. The RBM (RNA-binding motif) gene family encodes proteins with an RNA binding motif that have been suggested to play a role in the modulation of apoptosis. RBM26 (RNA binding motif protein 26), whose alternative names include CTCL tumor antigen se70-2, C13orf10, ARRS2, SE70-2, ZC3H17, PRO1777, FLJ20957, RP11-255E21.1, MGC133295 or MGC133296, is a 1,007 amino acid protein with six isoforms which result due to alternative splicing. RBM26 also contains one C3H1-type zinc finger and two RRM (RNA recognition motif) domains. The gene encoding RBM26 maps to human chromosome 13q31.1.
Supplier:  Bioss
Description:   Proteins containing RNA recognition motifs, including various hnRNP proteins, are implicated in the regulation of alternative splicing and protein components of snRNPs. The RBM (RNA-binding motif) gene family encodes proteins with an RNA binding motif that have been suggested to play a role in the modulation of apoptosis. RBM26 (RNA binding motif protein 26), whose alternative names include CTCL tumor antigen se70-2, C13orf10, ARRS2, SE70-2, ZC3H17, PRO1777, FLJ20957, RP11-255E21.1, MGC133295 or MGC133296, is a 1,007 amino acid protein with six isoforms which result due to alternative splicing. RBM26 also contains one C3H1-type zinc finger and two RRM (RNA recognition motif) domains. The gene encoding RBM26 maps to human chromosome 13q31.1.
Catalog Number: (RL009-001-C23)

Supplier:  Rockland Immunochemical
Description:   Vascular endothelial growth factor-A was originally isolated from tumor cells and referred to as Tumor Angiogenesis Factor. Although expressed at high levels in certain tumor-derived cells it is produced by a wide variety of cell types. In addition to stimulating vascular growth, vascular permeability, cell migration, and endothelial cell proliferation and growth, it may play a role in stimulating vasolidation via nitric oxide-dependent pathways and in inhibition of apoptosis. VEGF binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. Alternative splicing of the mRNA for VEGF-A results in several isoforms of the protein being produced. Rat and bovine VEGF are one amino acid shorter than the human factor, and the bovine and human sequences show a homology of 95 percent. In contrast to other factors mitogenic for endothelial cells such as FGF-1, FGF-2 and PDGF, VEGF is synthesized as a precursor containing a typical hydrophobic secretory signal sequence of 26 amino acids. Glycosylation is not required for efficient secretion of VEGF. VEGF121 is acidic, freely secreted, and widely expressed. This isoform is produced by alternative promoter usage and alternative initiation. It starts at an alternative upstream CUG codon and is post-translationally processed to produce the secreted VEGF peptide and a N-terminal peptide N-VEGF. The unprocessed protein and the N-VEGF peptide may localize to the nucleus, the endoplasmic reticulum and the Golgi or the extracellular matrix. Recombinant Human VEGF-121 produced in E.coli is a double, non-glycosylated, polypeptide chain containing 121 amino acids and having a molecular mass of 28423 Daltons.
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