Supplier: Bioss

The Ras superfamily of GTPases can be subdivided into the Ras, Rho/Rac, Sar, Rab, Arf, Rap and Ran subfamilies, all of which control multiple aspects of cell function, including cytoskeletal rearrangement, nuclear signaling and cell growth. The Ras superfamily of GTPases function as regulated switches that toggle between a biologically active GTP-bound and an inactive GDP-bound form. This activation is catalyzed by guanine nucleotide exchange factors (GEFs). RIC-8A (resistance to inhibitors of cholinesterase 8 homolog A), also known as RIC8 or Synembryn-A, is a 530 amino acid cytoplasmic protein that can activate several G-alpha proteins, including G?i-1, G?q and G?o. Functioning as a guanine nucleotide exchange factor, RIC-8A binds to GDP-associated substrates and exchanges bound GDP for free GTP. Via its ability to stimulate protein function, RIC-8A plays a role in regulating mitotic movement and may be involved in receptor-mediated ERK activation. RIC-8A is expressed as three isoforms due to alternative splicing events.

Supplier: Bioss

The Ras superfamily of GTPases can be subdivided into the Ras, Rho/Rac, Sar, Rab, Arf, Rap and Ran subfamilies, all of which control multiple aspects of cell function, including cytoskeletal rearrangement, nuclear signaling and cell growth. The Ras superfamily of GTPases function as regulated switches that toggle between a biologically active GTP-bound and an inactive GDP-bound form. This activation is catalyzed by guanine nucleotide exchange factors (GEFs). RIC-8A (resistance to inhibitors of cholinesterase 8 homolog A), also known as RIC8 or Synembryn-A, is a 530 amino acid cytoplasmic protein that can activate several G-alpha proteins, including G?i-1, G?q and G?o. Functioning as a guanine nucleotide exchange factor, RIC-8A binds to GDP-associated substrates and exchanges bound GDP for free GTP. Via its ability to stimulate protein function, RIC-8A plays a role in regulating mitotic movement and may be involved in receptor-mediated ERK activation. RIC-8A is expressed as three isoforms due to alternative splicing events.

Supplier: Bioss

The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, SUMO-2 and SUMO-3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2, and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1, SUMO-2 and SUMO-3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilizes Ubc9 for conjugation to several target proteins, which include IkBa, MDM2, p53, PML and Ran GAP1. SUMO-2 and SUMO-3 contribute to a greater percentage of protein modification than does SUMO-1, and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates b-Amyloid generation and may be critical in the onset or progression of Alzheimer’s disease.

Supplier: Bioss

The Ras superfamily of GTPases can be subdivided into the Ras, Rho/Rac, Sar, Rab, Arf, Rap and Ran subfamilies, all of which control multiple aspects of cell function, including cytoskeletal rearrangement, nuclear Signalling and cell growth. The Ras superfamily of GTPases function as regulated switches that toggle between a biologically active GTP-bound and an inactive GDP-bound form. This activation is catalysed by guanine nucleotide exchange factors (GEFs). RIC-8A (resistance to inhibitors of cholinesterase 8 homolog A), also known as RIC8 or Synembryn-A, is a 530 amino acid cytoplasmic protein that can activate several G-alpha proteins, including Gi-1, Gq and Go. Functioning as a guanine nucleotide exchange factor, RIC-8A binds to GDP-associated substrates and exchanges bound GDP for free GTP. Via its ability to stimulate protein function, RIC-8A plays a role in regulating mitotic movement and may be involved in receptor-mediated ERK activation. RIC-8A is expressed as three isoforms due to alternative splicing events.

Supplier: Bioss

The Ras superfamily of GTPases can be subdivided into the Ras, Rho/Rac, Sar, Rab, Arf, Rap and Ran subfamilies, all of which control multiple aspects of cell function, including cytoskeletal rearrangement, nuclear Signalling and cell growth. The Ras superfamily of GTPases function as regulated switches that toggle between a biologically active GTP-bound and an inactive GDP-bound form. This activation is catalysed by guanine nucleotide exchange factors (GEFs). RIC-8A (resistance to inhibitors of cholinesterase 8 homolog A), also known as RIC8 or Synembryn-A, is a 530 amino acid cytoplasmic protein that can activate several G-alpha proteins, including Gi-1, Gq and Go. Functioning as a guanine nucleotide exchange factor, RIC-8A binds to GDP-associated substrates and exchanges bound GDP for free GTP. Via its ability to stimulate protein function, RIC-8A plays a role in regulating mitotic movement and may be involved in receptor-mediated ERK activation. RIC-8A is expressed as three isoforms due to alternative splicing events.

Supplier: Bioss

The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, SUMO-2 and SUMO-3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesised as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilise the E1, E2, and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1, SUMO-2 and SUMO-3 proteins localise to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilises Ubc9 for conjugation to several target proteins, which include IkBa, MDM2, p53, PML and Ran GAP1. SUMO-2 and SUMO-3 contribute to a greater percentage of protein modification than does SUMO-1, and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates b-Amyloid generation and may be critical in the onset or progression of Alzheimer?s disease.

Supplier: Bioss

The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, SUMO-2 and SUMO-3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesised as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilise the E1, E2, and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1, SUMO-2 and SUMO-3 proteins localise to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilises Ubc9 for conjugation to several target proteins, which include IkBa, MDM2, p53, PML and Ran GAP1. SUMO-2 and SUMO-3 contribute to a greater percentage of protein modification than does SUMO-1, and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates b-Amyloid generation and may be critical in the onset or progression of Alzheimer?s disease.

Supplier: Bioss

The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, SUMO-2 and SUMO-3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2, and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1, SUMO-2 and SUMO-3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilizes Ubc9 for conjugation to several target proteins, which include IkBa, MDM2, p53, PML and Ran GAP1. SUMO-2 and SUMO-3 contribute to a greater percentage of protein modification than does SUMO-1, and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates b-Amyloid generation and may be critical in the onset or progression of Alzheimer’s disease.

Supplier: Bioss

The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, SUMO-2 and SUMO-3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2, and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1, SUMO-2 and SUMO-3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilizes Ubc9 for conjugation to several target proteins, which include IkBa, MDM2, p53, PML and Ran GAP1. SUMO-2 and SUMO-3 contribute to a greater percentage of protein modification than does SUMO-1, and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates b-Amyloid generation and may be critical in the onset or progression of Alzheimer’s disease.

Supplier: Bioss

The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, SUMO-2 and SUMO-3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2, and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1, SUMO-2 and SUMO-3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilizes Ubc9 for conjugation to several target proteins, which include IkBa, MDM2, p53, PML and Ran GAP1. SUMO-2 and SUMO-3 contribute to a greater percentage of protein modification than does SUMO-1, and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates b-Amyloid generation and may be critical in the onset or progression of Alzheimer’s disease.

Supplier: Bioss

The Ras superfamily of GTPases can be subdivided into the Ras, Rho/Rac, Sar, Rab, Arf, Rap and Ran subfamilies, all of which control multiple aspects of cell function, including cytoskeletal rearrangement, nuclear signaling and cell growth. The Ras superfamily of GTPases function as regulated switches that toggle between a biologically active GTP-bound and an inactive GDP-bound form. This activation is catalyzed by guanine nucleotide exchange factors (GEFs). RIC-8A (resistance to inhibitors of cholinesterase 8 homolog A), also known as RIC8 or Synembryn-A, is a 530 amino acid cytoplasmic protein that can activate several G-alpha proteins, including G?i-1, G?q and G?o. Functioning as a guanine nucleotide exchange factor, RIC-8A binds to GDP-associated substrates and exchanges bound GDP for free GTP. Via its ability to stimulate protein function, RIC-8A plays a role in regulating mitotic movement and may be involved in receptor-mediated ERK activation. RIC-8A is expressed as three isoforms due to alternative splicing events.

Supplier: Bioss

The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, SUMO-2 and SUMO-3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2, and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1, SUMO-2 and SUMO-3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilizes Ubc9 for conjugation to several target proteins, which include IkBa, MDM2, p53, PML and Ran GAP1. SUMO-2 and SUMO-3 contribute to a greater percentage of protein modification than does SUMO-1, and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates b-Amyloid generation and may be critical in the onset or progression of Alzheimer’s disease.

Supplier: Bioss

The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, SUMO-2 and SUMO-3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2, and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1, SUMO-2 and SUMO-3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilizes Ubc9 for conjugation to several target proteins, which include IkBa, MDM2, p53, PML and Ran GAP1. SUMO-2 and SUMO-3 contribute to a greater percentage of protein modification than does SUMO-1, and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates b-Amyloid generation and may be critical in the onset or progression of Alzheimer’s disease.

Supplier: Bioss

The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, SUMO-2 and SUMO-3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2, and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1, SUMO-2 and SUMO-3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilizes Ubc9 for conjugation to several target proteins, which include IkBa, MDM2, p53, PML and Ran GAP1. SUMO-2 and SUMO-3 contribute to a greater percentage of protein modification than does SUMO-1, and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates b-Amyloid generation and may be critical in the onset or progression of Alzheimer’s disease.

Supplier: Bioss

The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, SUMO-2 and SUMO-3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2, and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1, SUMO-2 and SUMO-3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilizes Ubc9 for conjugation to several target proteins, which include IkBa, MDM2, p53, PML and Ran GAP1. SUMO-2 and SUMO-3 contribute to a greater percentage of protein modification than does SUMO-1, and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates b-Amyloid generation and may be critical in the onset or progression of Alzheimer’s disease.

Supplier: Bioss

The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, SUMO-2 and SUMO-3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2, and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1, SUMO-2 and SUMO-3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilizes Ubc9 for conjugation to several target proteins, which include IkBa, MDM2, p53, PML and Ran GAP1. SUMO-2 and SUMO-3 contribute to a greater percentage of protein modification than does SUMO-1, and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates b-Amyloid generation and may be critical in the onset or progression of Alzheimer’s disease.

Supplier: ProSci Inc.

KPNA2 Antibody: Karyopherin, a cytosolic and heterodimeric protein complex consisting of alpha and beta subunits, is responsible for targeting proteins with nuclear localization signals to the nuclear pore complex by an energy requiring, Ran-dependent mechanism. The alpha subunit and imported substrate enter the nucleus and accumulate in the nucleoplasm, while the beta subunit accumulates at the NPC. KPNA2 is the alpha subunit 2 of karyopherin, which forms a complex with importin subunit beta-1 and functions as a cargo carrier that transports various complexes from cytoplasm into nucleus. It is ubiquitously expressed and contains an IBB/importin beta domain, ten Armadillo repeats that bind "cargo" and three intervening nuclear localization sequences (NLSs). It has recently been reported to play an important role in tumorigenesis and tumor progression.

Supplier: Bioss

The Ras superfamily of GTPases can be subdivided into the Ras, Rho/Rac, Sar, Rab, Arf, Rap and Ran subfamilies, all of which control multiple aspects of cell function, including cytoskeletal rearrangement, nuclear signaling and cell growth. The Ras superfamily of GTPases function as regulated switches that toggle between a biologically active GTP-bound and an inactive GDP-bound form. This activation is catalyzed by guanine nucleotide exchange factors (GEFs). RIC-8A (resistance to inhibitors of cholinesterase 8 homolog A), also known as RIC8 or Synembryn-A, is a 530 amino acid cytoplasmic protein that can activate several G-alpha proteins, including G?i-1, G?q and G?o. Functioning as a guanine nucleotide exchange factor, RIC-8A binds to GDP-associated substrates and exchanges bound GDP for free GTP. Via its ability to stimulate protein function, RIC-8A plays a role in regulating mitotic movement and may be involved in receptor-mediated ERK activation. RIC-8A is expressed as three isoforms due to alternative splicing events.

Supplier: Bioss

The Ras superfamily of GTPases can be subdivided into the Ras, Rho/Rac, Sar, Rab, Arf, Rap and Ran subfamilies, all of which control multiple aspects of cell function, including cytoskeletal rearrangement, nuclear signaling and cell growth. The Ras superfamily of GTPases function as regulated switches that toggle between a biologically active GTP-bound and an inactive GDP-bound form. This activation is catalyzed by guanine nucleotide exchange factors (GEFs). RIC-8A (resistance to inhibitors of cholinesterase 8 homolog A), also known as RIC8 or Synembryn-A, is a 530 amino acid cytoplasmic protein that can activate several G-alpha proteins, including G?i-1, G?q and G?o. Functioning as a guanine nucleotide exchange factor, RIC-8A binds to GDP-associated substrates and exchanges bound GDP for free GTP. Via its ability to stimulate protein function, RIC-8A plays a role in regulating mitotic movement and may be involved in receptor-mediated ERK activation. RIC-8A is expressed as three isoforms due to alternative splicing events.

Supplier: Bioss

The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, SUMO-2 and SUMO-3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2, and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1, SUMO-2 and SUMO-3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilizes Ubc9 for conjugation to several target proteins, which include IkBa, MDM2, p53, PML and Ran GAP1. SUMO-2 and SUMO-3 contribute to a greater percentage of protein modification than does SUMO-1, and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates b-Amyloid generation and may be critical in the onset or progression of Alzheimer’s disease.

Supplier: Bioss

The Ras superfamily of GTPases can be subdivided into the Ras, Rho/Rac, Sar, Rab, Arf, Rap and Ran subfamilies, all of which control multiple aspects of cell function, including cytoskeletal rearrangement, nuclear signaling and cell growth. The Ras superfamily of GTPases function as regulated switches that toggle between a biologically active GTP-bound and an inactive GDP-bound form. This activation is catalyzed by guanine nucleotide exchange factors (GEFs). RIC-8A (resistance to inhibitors of cholinesterase 8 homolog A), also known as RIC8 or Synembryn-A, is a 530 amino acid cytoplasmic protein that can activate several G-alpha proteins, including G?i-1, G?q and G?o. Functioning as a guanine nucleotide exchange factor, RIC-8A binds to GDP-associated substrates and exchanges bound GDP for free GTP. Via its ability to stimulate protein function, RIC-8A plays a role in regulating mitotic movement and may be involved in receptor-mediated ERK activation. RIC-8A is expressed as three isoforms due to alternative splicing events.

Supplier: Bioss

The Ras superfamily of GTPases can be subdivided into the Ras, Rho/Rac, Sar, Rab, Arf, Rap and Ran subfamilies, all of which control multiple aspects of cell function, including cytoskeletal rearrangement, nuclear signaling and cell growth. The Ras superfamily of GTPases function as regulated switches that toggle between a biologically active GTP-bound and an inactive GDP-bound form. This activation is catalyzed by guanine nucleotide exchange factors (GEFs). RIC-8A (resistance to inhibitors of cholinesterase 8 homolog A), also known as RIC8 or Synembryn-A, is a 530 amino acid cytoplasmic protein that can activate several G-alpha proteins, including G?i-1, G?q and G?o. Functioning as a guanine nucleotide exchange factor, RIC-8A binds to GDP-associated substrates and exchanges bound GDP for free GTP. Via its ability to stimulate protein function, RIC-8A plays a role in regulating mitotic movement and may be involved in receptor-mediated ERK activation. RIC-8A is expressed as three isoforms due to alternative splicing events.

Supplier: Bioss

The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, SUMO-2 and SUMO-3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2, and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1, SUMO-2 and SUMO-3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilizes Ubc9 for conjugation to several target proteins, which include IkBa, MDM2, p53, PML and Ran GAP1. SUMO-2 and SUMO-3 contribute to a greater percentage of protein modification than does SUMO-1, and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates b-Amyloid generation and may be critical in the onset or progression of Alzheimer’s disease.

Supplier: ENZO LIFE SCIENCES

The Ras superfamily of small guanosine triphosphatases (GTPases) is traditionally subdivided into five families: Ras, Rho, Rab, Ran, and Arf. Rap1/Krev1 is a member of the Ras family of low molecular weight GTP-binding proteins1. Ras-like GTPases are ubiquitously expressed, evolutionarily conserved molecular switches that couple extracellular signals to various cellular responses. Rap1 is primarily found at the cytosolic side of intracellular membranes and has two isoforms: Rap1a and 1b2. Both isoforms have a molecular mass of 21 kDa and are isoprenylated at the carboxyl-terminal and phosphorylated by the cAMP-dependent protein kinase A (PKA)3. Rap1 cycles between a GTP-bound active form and a GDP-bound inactive form that is mediated by GTPase activating protein (GAP) and GDP dissociation stimulator (GDS)4,5. Activation occurs by a variety of extracellular stimuli through several conserved guanine nucleotide exchange factors (GEFs) and GTPase activating proteins (GAPs). Rap1 is proposed to regulate Ras mediated signaling and may also be involved in the regulation of integrinmediated cell adhesion, although the mechanism of regulation is not known. Overexpression of Rap reverses the transformed phenotype induced by Ras, possibly by competing with Ras for interaction with Ras-GAP. Rap has been shown to participate in MAP kinase cascade activated by growth factor and maintaining human T cell anergic state by blocking IL-2 expression.

Supplier: Merck

2'-DESOXYADENOSIN-5'-PHOSPHORSAEURE HYDR 1 * 1 g

Supplier: Merck

ANTI-RAN 1 * 100 µG

Supplier: Abcam

Rabbit monoclonal [EPR3295] to RanGAP1 - BSA and Azide free.

Supplier: Abcam

Human monoclonal [B1-8] to hapten 4-hydroxy-3-nitrophenyl acetyl (NP).

Supplier: Abcam

Mouse monoclonal [B1-8] to hapten 4-hydroxy-3-nitrophenyl acetyl (NP).

Supplier: Abcam

Mouse monoclonal [B1-8] to hapten 4-hydroxy-3-nitrophenyl acetyl (NP).