You Searched For: 2-Bromo-3-methoxyaniline

Catalog Number: (BOSSBS-1012R-A488)

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.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13357R-A750)

Supplier: Bioss

Description: ADRM1 is a 407 amino acid protein that localises 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.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-1012R-A350)

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.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-1012R-A647)

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.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-1012R-HRP)

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.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13357R-A647)

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.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13357R-HRP)

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.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-9609R)

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.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12406R)

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).

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12406R-CY5)

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).

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12406R-A488)

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).

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12406R-CY7)

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).

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12406R-A750)

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).

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12406R-CY3)

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).

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12406R-FITC)

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).

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12406R-A350)

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).

UOM: 1 * 100 µl