You Searched For: stalk

Catalog Number: (10101-940)

Supplier: Prosci

Description: Vax1 is required for axon guidance and major tract formation in the developing forebrain. Vax1 may contribute to the differentiation of the neuroretina, pigmented epithelium and optic stalk.

Catalog Number: (10093-922)

Supplier: Proteintech

Description: RPLP0 is first identified as a cytosolic protein which takes a part in the ribosomal stalk and interacts with RPLP1 and RPLP2. It also has potential roles in molecular transport from outside into the cells. It generally presents in multiple copies on the ribosome and have isoelectric points in the range of pH 3 to 5, in contrast to most ribosomal proteins, which are single copy and basic

Catalog Number: (77440-542)

Supplier: Bioss

Description: This gene encodes a protein which is similar to the Drosophila crumbs protein and localizes to the inner segment of mammalian photoreceptors. In Drosophila crumbs localizes to the stalk of the fly photoreceptor and may be a component of the molecular scaffold that controls proper development of polarity in the eye. Mutations in this gene are associated with a severe form of retinitis pigmentosa, RP12, and with Leber congenital amaurosis. Alternate splicing results in multiple transcript variants, some protein coding and some non-protein coding.[provided by RefSeq, Apr 2012]

New Product

Catalog Number: (89358-050)

Supplier: Genetex

Description: KIFC3 belongs to the large superfamily of kinesins, molecular motors that use the energy of ATP hydrolysis to translocate cargoes along microtubules. Members share extensive homology within a globular domain containing the microtubule- and ATP-binding sites and have a coiled-coil stalk domain that mediates oligomerization. Different kinesin family members participate in specific and diverse motile processes, such as cell division, organelle transport, and nuclear movement (Hoang et al., 1998 [PubMed 9782090]).[supplied by OMIM]

Catalog Number: (10072-964)

Supplier: Prosci

Description: CXCL16 is a member of the CXC chemokine family and signals through the CXCR6 receptor. CXCL16 may play a role in attracting lymphocyte subsets during inflammation and may facilitate certain immune responses. The chemokine domain of CXCL16 contains six cysteine residues including the four highly conserved cysteine residues characteristic of CXC chemokines. The CXCL16 gene codes for a 273 amino acid polypeptide, which includes a 29 amino acid cytoplasmic domain and transmembrane sequence containing approximately 20 amino acids. The extracellular portion of CXCL16 contains a chemokines domain and an extended C-terminal ?mucin-like stalk? sequence. The extracellular domain contains 89 amino acid residues (86 a.a. residues for the murine homolog). Recombinant murine CXCL16 is a 9.9 kDa protein containing 88 amino acid residues.

Catalog Number: (10085-368)

Supplier: Proteintech

Description: Chemokines direct the trafficking of white blood cells in immune surveillance, playing a key role in inflammatory and infectious diseases such as AIDS. The human CX3C chemokine carries the chemokine domain on top of an extended mucin-like stalk. CX3CL1 is synthesized as a 50-75kDa precursor and undergoes glycosylation to yield two mature forms: a 100kDa cell membrane bound form and an 85kDa soluble form which is released from the cell surface.The soluble CX3C chemokine has potent chemoattractant activity for T cells and monocytes, and the cell-surface-bound protein, which is induced by primary proinflammatory signals in activated primary endothelial cells, promotes strong adhesion of those leukocytes.

Catalog Number: (75789-510)

Supplier: Prosci

Description: Human Fractalkine (CX3CL1) is a member of the CX3C family of chemokines. Human Fractalkine contains both chemokine and mucin domain. The soluble form of Fractalkine is chemotactic for T-cells and monocytes, but not for neutrophils. The membrane bound form of Fractalkine promotes leukocytes adhesion to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid). The mucin-like stalk permits it to bind to the cell surface.

Catalog Number: (77440-000)

Supplier: Bioss

Description: The natural cytotoxicity receptors (NCRs) are a recently characterized family of Ig-like activation receptors that appear to be major triggering receptors in tumor cell recognition. NCR1 is a glycoprotein that has two extracellular Ig-like domains followed by a ~40 amino acid residue stalk region, a type I transmembrane domain, and a short cytoplasmic tail. NCR1 has been shown to represent a novel NK cell-specific molecule involved in human NK cell activation. NCR1 has been implicated in NK cell-mediated lysis of several autologous tumor cells and pathogen-infected cell lines.

New Product

Catalog Number: (10665-566)

Supplier: Bioss

Description: DPP6 is a Type-II serine proteinase of the clan SC. The clan SC proteinases have a catalytic triad of Ser-Asp-His, and like other Serine proteinases, the active site serine is in a Gly-Xaa-Ser-Xaa -Gly orientation. DPP6 has an Asp instead of Ser in the catalytic site. DPP6 is a member of a broader family of dipeptidyl peptidases including DPP4, FAP/Seprase, DPP2, DPP8, DPP9, DPP10, which have differing substrate specificity and tissue localizations. The surface-bound DPP6 is a homodimer, and cleavage of in the stalk region releases a shed form of DPP6. The shed is the form found in serum. DPP6 has been found in highest abundance in the brain, but also in the kidney, liver and lung.

Catalog Number: (10103-832)

Supplier: Prosci

Description: Cytoplasmic dyneins are large enzyme complexes with a molecular mass of about 1,200 kD. They contain two force-producing heads formed primarily from dynein heavy chains, and stalks linking the heads to a basal domain, which contains a varying number of accessory intermediate chains. The complex is involved in intracellular transport and motility. DYNLL1 is a light chain and exists as part of this complex but also physically interacts with and inhibits the activity of neuronal nitric oxide synthase. Binding of this protein destabilizes the neuronal nitric oxide synthase dimer, a conformation necessary for activity, and it may regulate numerous biologic processes through its effects on nitric oxide synthase activity.Cytoplasmic dyneins are large enzyme complexes with a molecular mass of about 1,200 kD. They contain two force-producing heads formed primarily from dynein heavy chains, and stalks linking the heads to a basal domain, which contains a varying number of accessory intermediate chains. The complex is involved in intracellular transport and motility. The protein described in this record is a light chain and exists as part of this complex but also physically interacts with and inhibits the activity of neuronal nitric oxide synthase. Binding of this protein destabilizes the neuronal nitric oxide synthase dimer, a conformation necessary for activity, and it may regulate numerous biologic processes through its effects on nitric oxide synthase activity. Alternate transcriptional splice variants have been characterized.

Catalog Number: (10090-422)

Supplier: Proteintech

Description: Mammalian MRPL12 was the first mitochondrial ribosomal protein to be characterized, and is encoded by a nuclear gene. The protein forms a homodimer, localizes predominantly to mitochondria and binds to the large mitochondrial ribosomal subunit . It is required for CycD/Cdk4-induced cell growth. In addition, forming a ribosomal stalk with MRPL7, MRPL12 is required for the recruitment of translation elongation factors Tu and G to the large ribosomal subunit . It also a part of a novel regulatory mechanism that coordinates mitochondrial transcription with translation and/or ribosome biogenesis during human mitochondrial gene expression.

Catalog Number: (10106-590)

Supplier: Prosci

Description: Vax1 is required for axon guidance and major tract formation in the developing forebrain. It may contribute to the differentiation of the neuroretina, pigmented epithelium and optic stalk.

Catalog Number: (10072-378)

Supplier: Prosci

Description: CXCL16 is a member of the CXC chemokine family and signals through the CXCR6 receptor. CXCL16 may play a role in attracting lymphocyte subsets during inflammation and may facilitate certain immune responses. The chemokine domain of CXCL16 contains six cysteine residues including the four highly conserved cysteine residues characteristic of CXC chemokines. The CXCL16 gene codes for a 273 amino acid polypeptide, which includes a 29 amino acid cytoplasmic domain and transmembrane sequence containing approximately 20 amino acids. The extracellular portion of CXCL16 contains a chemokines domain and an extended C-terminal mucin-like stalk sequence. The extracellular domain contains 89 amino acid residues (86 a.a. residues for the murine homolog). Recombinant human CXCL16 is a 10.1 kDa protein containing 89 amino acid residues.

Supplier: FUJIFILM IRVINE SCIENTIFIC, INC

Description: Fractalkine, also known as CX3CL1, is a cytokine protein containing a CX3C chemokine motif atop a mucin stalk. Fractalkine is produced by non-hemopoietic cells, including neurons and astrocytes. Soluble fractalkine functions as a chemoattractant for T cells and monocytes. Cell-membrane-bound fractalkine, which is induced on activated endothelial cells, promotes leukocyte adhesion. The transmembrane chemokine receptor CX3CR1 mediates the adhesive and chemoattractant functions of fractalkine.

Catalog Number: (10671-384)

Supplier: Bioss

Description: DPP6 is a Type-II serine proteinase of the clan SC. The clan SC proteinases have a catalytic triad of Ser-Asp-His, and like other Serine proteinases, the active site serine is in a Gly-Xaa-Ser-Xaa -Gly orientation. DPP6 has an Asp instead of Ser in the catalytic site. DPP6 is a member of a broader family of dipeptidyl peptidases including DPP4, FAP/Seprase, DPP2, DPP8, DPP9, DPP10, which have differing substrate specificity and tissue localizations. The surface-bound DPP6 is a homodimer, and cleavage of in the stalk region releases a shed form of DPP6. The shed is the form found in serum. DPP6 has been found in highest abundance in the brain, but also in the kidney, liver and lung.

Catalog Number: (10671-382)

Supplier: Bioss

Description: DPP6 is a Type-II serine proteinase of the clan SC. The clan SC proteinases have a catalytic triad of Ser-Asp-His, and like other Serine proteinases, the active site serine is in a Gly-Xaa-Ser-Xaa -Gly orientation. DPP6 has an Asp instead of Ser in the catalytic site. DPP6 is a member of a broader family of dipeptidyl peptidases including DPP4, FAP/Seprase, DPP2, DPP8, DPP9, DPP10, which have differing substrate specificity and tissue localizations. The surface-bound DPP6 is a homodimer, and cleavage of in the stalk region releases a shed form of DPP6. The shed is the form found in serum. DPP6 has been found in highest abundance in the brain, but also in the kidney, liver and lung.