Proteins & Peptides

c-Jun is a proto-oncogene that forms a complex with c-Fos which regulates transcription from promoters containing AP-1 activation elements (1). c-Jun has specific DNA binding activity and following in vitro translation, c-Jun binds as a homodimer to the AP-1 DNA site. The transactivating function of c-Jun is acutely regulated by a wide variety of cellular signals via modulation of phosphorylation of two serines (63 and 73). Jun N-terminal domain kinases (JNKs), are responsible for mediating S63/73 phosphorylation on c-Jun in response to a variety of cellular stimuli including TNF-a, heat stress and u.v. light (2). c-JUN Protein is ideal for investigators involved in Signaling Proteins, Transcription Proteins, Apoptosis/Autophagy, Cardiovascular Disease, Cellular Stress, Inflammation, JNK/SAPK Pathway, Neurobiology, and NfkB Pathway research.

Cofilin 1 (non-muscle), also known as CFL1, is a widely distributed intracellular actin-modulating protein that binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner (1). It is involved in the translocation of actin-cofilin complex from cytoplasm to nucleus (2). CFL1 processed proteins are most probably produced by HIV-1 protease digestion. Cofilin 1 Protein is ideal for investigators involved in Signaling Proteins, Microtubule/Actin Associated Proteins, Cancer, Cardiovascular Disease, Invasion/Metastasis, and Neurobiology research.

Cofilin 1 (non-muscle), also known as CFL1, is a widely distributed intracellular actin-modulating protein that binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner (1). It is involved in the translocation of actin-cofilin complex from cytoplasm to nucleus (2). CFL1 processed proteins are most probably produced by HIV-1 protease digestion. Cofilin 1 Protein is ideal for investigators involved in Signaling Proteins, Microtubule/Actin Associated Proteins, Cancer, Cardiovascular Disease, Invasion/Metastasis, and Neurobiology research.

CRKL or v-crk sarcoma virus CT10 oncogene homolog (avian)-like is a protein kinase containing SH2 and SH3 (src homology) domains that activate the RAS and JUN kinase signaling pathways and transform fibroblasts in a RAS-dependent fashion (1). It is a substrate of the BCR-ABL tyrosine kinase which plays a role in fibroblast transformation by BCR-ABL, and may be oncogenic (2). CRKL is also required for normal cellular responses to Fgf8, including survival and migration, Erk activation, and target gene expression. CRKL Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Apoptosis/Autophagy, Cancer, Cell Cycle, Receptor Tyrosine Kinases, and WNT Signaling research.

CRKL or v-crk sarcoma virus CT10 oncogene homolog (avian)-like is a protein kinase containing SH2 and SH3 (src homology) domains that activate the RAS and JUN kinase signaling pathways and transform fibroblasts in a RAS-dependent fashion (1). It is a substrate of the BCR-ABL tyrosine kinase which plays a role in fibroblast transformation by BCR-ABL, and may be oncogenic (2). CRKL is also required for normal cellular responses to Fgf8, including survival and migration, Erk activation, and target gene expression. CRKL Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Apoptosis/Autophagy, Cancer, Cell Cycle, Receptor Tyrosine Kinases, and WNT Signaling research.

CRYAA or crystallin alpha A is the major protein components of the vertebrate eye lens which is composed of 2 primary gene products--alpha-A and alpha-B. CRYAA can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family (1). CRYAA plays an important role in the normal embryologic development of the anterior segment of the eye. In the Elo mouse, a 1-bp deletion in the gamma-E-crystallin gene causes autosomal dominant cataract and microphthalmia (2). CRYAA Protein is ideal for investigators involved in Signaling Proteins, Cell Stress & Chaperone Proteins, Cancer, Metabolic Disorder, and Neurobiology research.

CRYAA or crystallin alpha A is the major protein components of the vertebrate eye lens which is composed of 2 primary gene products--alpha-A and alpha-B. CRYAA can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family (1). CRYAA plays an important role in the normal embryologic development of the anterior segment of the eye. In the Elo mouse, a 1-bp deletion in the gamma-E-crystallin gene causes autosomal dominant cataract and microphthalmia (2). CRYAA Protein is ideal for investigators involved in Signaling Proteins, Cell Stress & Chaperone Proteins, Cancer, Metabolic Disorder, and Neurobiology research.

CyclinA2 belongs to the highly conserved cyclin family whose members are characterized by a dramatic periodicity in protein abundance through the cell cycle and function as regulators of CDKs. CyclinA2 is an essential component of all embryonic and somatic cell cycles in mammals (1). CyclinA2 is highly expressed in the testis and certain myeloid leukemia cells (2). Cyclin A also plays a major role in the control of DNA replication (3). CyclinA2 binds and activates CDC2 or CDK2 and thus promotes both cell cycle G1/S and G2/M transitions. CyclinA2 Protein is ideal for investigators involved in Signaling Proteins, Cell Cycle Proteins, Cancer, and Cell Cycle research.

CyclinA2 belongs to the highly conserved cyclin family whose members are characterized by a dramatic periodicity in protein abundance through the cell cycle and function as regulators of CDKs. CyclinA2 is an essential component of all embryonic and somatic cell cycles in mammals (1). CyclinA2 is highly expressed in the testis and certain myeloid leukemia cells (2). Cyclin A also plays a major role in the control of DNA replication (3). CyclinA2 binds and activates CDC2 or CDK2 and thus promotes both cell cycle G1/S and G2/M transitions. CyclinA2 Protein is ideal for investigators involved in Signaling Proteins, Cell Cycle Proteins, Cancer, and Cell Cycle research.