You Searched For: gamma-Methyl-L-leucine


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Catalog Number: (10493-360)
Supplier: Bioss
Description: PIBF is synthesized during pregnancy in response to progesterone by progesterone receptor-positive T lymphocytes (mostly gamma-delta T cells). In the presence of PIBF, natural killer (NK) cells inhibit the release of perforin from storage granules and therefore fail to lyse target cells. In humans, the amount of cells that express PIBF is significantly higher in healthy pregnant women than in women at risk for premature pregnancy termination. Full-length PIBF is associated with the nucleus, whereas secretion of shorter forms is induced by activation of the cell. Research suggests that PIBF functions as a transcription factor in its full-length form, while smaller forms may act as cytokines. The PIBF gene encodes a deduced hydrophilic 757-amino acid alpha-helical protein with an N-terminal signal sequence, a leucine zipper motif, a basic zipper sequence, a PEST sequence, a nuclear localization signal, an endoplasmic reticulum membrane retention signal, and many presumeed N-glycosylation and phosphorylation sites.


Catalog Number: (10493-368)
Supplier: Bioss
Description: PIBF is synthesized during pregnancy in response to progesterone by progesterone receptor-positive T lymphocytes (mostly gamma-delta T cells). In the presence of PIBF, natural killer (NK) cells inhibit the release of perforin from storage granules and therefore fail to lyse target cells. In humans, the amount of cells that express PIBF is significantly higher in healthy pregnant women than in women at risk for premature pregnancy termination. Full-length PIBF is associated with the nucleus, whereas secretion of shorter forms is induced by activation of the cell. Research suggests that PIBF functions as a transcription factor in its full-length form, while smaller forms may act as cytokines. The PIBF gene encodes a deduced hydrophilic 757-amino acid alpha-helical protein with an N-terminal signal sequence, a leucine zipper motif, a basic zipper sequence, a PEST sequence, a nuclear localization signal, an endoplasmic reticulum membrane retention signal, and many presumeed N-glycosylation and phosphorylation sites.


Catalog Number: (89361-134)
Supplier: Genetex
Description: Apoptosis is mediated by death domain containing adapter molecules and a caspase family of proteases. Certain serine/threonine protein kinases, such as ASK-1 and RIP, are mediators of apoptosis. A novel serine/threonine kinas that mediates apoptosis was recently identified and designated ZIP kinase (1). ZIP kinase contains an N-terminal kinase domain and a C-terminal leucine zipper structure and binds to ATF4 that is a member of ATF/CREB family. ZIP kinase has high sequence homology to DAP kinase (death-associated protein kinase), which is a mediator of apoptosis induced by gamma interferon. Overexpression of ZIP kinase induces apoptosis. ZIP and DAP kinases represent a novel kinase family, which mediates apoptosis through their catalytic activities. The messenger RNA was ubiquitously expressed in various tissues (1).


Catalog Number: (10749-274)
Supplier: Prosci
Description: ZIPK Antibody: Apoptosis is mediated by death domain containing adapter molecules and a caspase family of proteases. Certain serine/threonine protein kinases, such as ASK-1 and RIP, are mediators of apoptosis. A novel serine/threonine kinase that mediates apoptosis was recently identified and designated ZIP kinase. ZIP kinase contains an N-terminal kinase domain and a C-terminal leucine zipper structure and binds to ATF4 that is a member of ATF/CREB family. ZIP kinase has high sequence homology to DAP kinase (death-associated protein kinase), which is a mediator of apoptosis induced by gamma interferon. Overexpression of ZIP kinase induces apoptosis. ZIP and DAP kinases represent a novel kinase family, which mediates apoptosis through their catalytic activities. The messenger RNA was ubiquitously expressed in various tissues.


Catalog Number: (10493-358)
Supplier: Bioss
Description: PIBF is synthesized during pregnancy in response to progesterone by progesterone receptor-positive T lymphocytes (mostly gamma-delta T cells). In the presence of PIBF, natural killer (NK) cells inhibit the release of perforin from storage granules and therefore fail to lyse target cells. In humans, the amount of cells that express PIBF is significantly higher in healthy pregnant women than in women at risk for premature pregnancy termination. Full-length PIBF is associated with the nucleus, whereas secretion of shorter forms is induced by activation of the cell. Research suggests that PIBF functions as a transcription factor in its full-length form, while smaller forms may act as cytokines. The PIBF gene encodes a deduced hydrophilic 757-amino acid alpha-helical protein with an N-terminal signal sequence, a leucine zipper motif, a basic zipper sequence, a PEST sequence, a nuclear localization signal, an endoplasmic reticulum membrane retention signal, and many presumeed N-glycosylation and phosphorylation sites.


Catalog Number: (10493-346)
Supplier: Bioss
Description: PIBF is synthesized during pregnancy in response to progesterone by progesterone receptor-positive T lymphocytes (mostly gamma-delta T cells). In the presence of PIBF, natural killer (NK) cells inhibit the release of perforin from storage granules and therefore fail to lyse target cells. In humans, the amount of cells that express PIBF is significantly higher in healthy pregnant women than in women at risk for premature pregnancy termination. Full-length PIBF is associated with the nucleus, whereas secretion of shorter forms is induced by activation of the cell. Research suggests that PIBF functions as a transcription factor in its full-length form, while smaller forms may act as cytokines. The PIBF gene encodes a deduced hydrophilic 757-amino acid alpha-helical protein with an N-terminal signal sequence, a leucine zipper motif, a basic zipper sequence, a PEST sequence, a nuclear localization signal, an endoplasmic reticulum membrane retention signal, and many presumeed N-glycosylation and phosphorylation sites.


Catalog Number: (76110-892)
Supplier: Bioss
Description: PIBF is synthesized during pregnancy in response to progesterone by progesterone receptor-positive T lymphocytes (mostly gamma-delta T cells). In the presence of PIBF, natural killer (NK) cells inhibit the release of perforin from storage granules and therefore fail to lyse target cells. In humans, the amount of cells that express PIBF is significantly higher in healthy pregnant women than in women at risk for premature pregnancy termination. Full-length PIBF is associated with the nucleus, whereas secretion of shorter forms is induced by activation of the cell. Research suggests that PIBF functions as a transcription factor in its full-length form, while smaller forms may act as cytokines. The PIBF gene encodes a deduced hydrophilic 757-amino acid alpha-helical protein with an N-terminal signal sequence, a leucine zipper motif, a basic zipper sequence, a PEST sequence, a nuclear localization signal, an endoplasmic reticulum membrane retention signal, and many presumeed N-glycosylation and phosphorylation sites.


Catalog Number: (10493-362)
Supplier: Bioss
Description: PIBF is synthesized during pregnancy in response to progesterone by progesterone receptor-positive T lymphocytes (mostly gamma-delta T cells). In the presence of PIBF, natural killer (NK) cells inhibit the release of perforin from storage granules and therefore fail to lyse target cells. In humans, the amount of cells that express PIBF is significantly higher in healthy pregnant women than in women at risk for premature pregnancy termination. Full-length PIBF is associated with the nucleus, whereas secretion of shorter forms is induced by activation of the cell. Research suggests that PIBF functions as a transcription factor in its full-length form, while smaller forms may act as cytokines. The PIBF gene encodes a deduced hydrophilic 757-amino acid alpha-helical protein with an N-terminal signal sequence, a leucine zipper motif, a basic zipper sequence, a PEST sequence, a nuclear localization signal, an endoplasmic reticulum membrane retention signal, and many presumeed N-glycosylation and phosphorylation sites.


Catalog Number: (10493-366)
Supplier: Bioss
Description: PIBF is synthesized during pregnancy in response to progesterone by progesterone receptor-positive T lymphocytes (mostly gamma-delta T cells). In the presence of PIBF, natural killer (NK) cells inhibit the release of perforin from storage granules and therefore fail to lyse target cells. In humans, the amount of cells that express PIBF is significantly higher in healthy pregnant women than in women at risk for premature pregnancy termination. Full-length PIBF is associated with the nucleus, whereas secretion of shorter forms is induced by activation of the cell. Research suggests that PIBF functions as a transcription factor in its full-length form, while smaller forms may act as cytokines. The PIBF gene encodes a deduced hydrophilic 757-amino acid alpha-helical protein with an N-terminal signal sequence, a leucine zipper motif, a basic zipper sequence, a PEST sequence, a nuclear localization signal, an endoplasmic reticulum membrane retention signal, and many presumeed N-glycosylation and phosphorylation sites.


Catalog Number: (76110-890)
Supplier: Bioss
Description: PIBF is synthesized during pregnancy in response to progesterone by progesterone receptor-positive T lymphocytes (mostly gamma-delta T cells). In the presence of PIBF, natural killer (NK) cells inhibit the release of perforin from storage granules and therefore fail to lyse target cells. In humans, the amount of cells that express PIBF is significantly higher in healthy pregnant women than in women at risk for premature pregnancy termination. Full-length PIBF is associated with the nucleus, whereas secretion of shorter forms is induced by activation of the cell. Research suggests that PIBF functions as a transcription factor in its full-length form, while smaller forms may act as cytokines. The PIBF gene encodes a deduced hydrophilic 757-amino acid alpha-helical protein with an N-terminal signal sequence, a leucine zipper motif, a basic zipper sequence, a PEST sequence, a nuclear localization signal, an endoplasmic reticulum membrane retention signal, and many presumeed N-glycosylation and phosphorylation sites.


Catalog Number: (10782-430)
Supplier: Biosensis
Description: FUNCTION: Receptor for brain-derived neurotrophic factor (BDNF), neurotrophin-3 and neurotrophin-4/5 but not nerve growth factor (NGF). Involved in the development and/or maintenance of the nervous system. This is a tyrosine-protein kinase receptor. Known substrates for the TRK receptors are SHC1, PI-3 kinase, and PLC-gamma-1. CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. SUBUNIT: Exists in a dynamic equilibrium between monomeric (low affinity) and dimeric (high affinity) structures (By similarity). Binds APS. Interacts with SQSTM1. SUBCELLULAR LOCATION: Membrane; single-pass type I membrane protein. ALTERNATIVE PRODUCTS: 3 named isoforms produced by alternative splicing. Additional isoforms seem to exist. TISSUE SPECIFICITY: The different forms are differentially expressed in various cell types. Isoform T2 is primarily expressed in neurons. PTM: Ligand-mediated auto-phosphorylation. SIMILARITY: Belongs to the Tyr protein kinase family. Insulin receptor subfamily. SIMILARITY: Contains 2 Ig-like C2-type (immunoglobulin-like) domains. SIMILARITY: Contains 2 LRR (leucine-rich) repeats. SIMILARITY: Contains 1 protein kinase domain.


Catalog Number: (10493-364)
Supplier: Bioss
Description: PIBF is synthesized during pregnancy in response to progesterone by progesterone receptor-positive T lymphocytes (mostly gamma-delta T cells). In the presence of PIBF, natural killer (NK) cells inhibit the release of perforin from storage granules and therefore fail to lyse target cells. In humans, the amount of cells that express PIBF is significantly higher in healthy pregnant women than in women at risk for premature pregnancy termination. Full-length PIBF is associated with the nucleus, whereas secretion of shorter forms is induced by activation of the cell. Research suggests that PIBF functions as a transcription factor in its full-length form, while smaller forms may act as cytokines. The PIBF gene encodes a deduced hydrophilic 757-amino acid alpha-helical protein with an N-terminal signal sequence, a leucine zipper motif, a basic zipper sequence, a PEST sequence, a nuclear localization signal, an endoplasmic reticulum membrane retention signal, and many presumeed N-glycosylation and phosphorylation sites.


Catalog Number: (TCF1028-1G)
Supplier: TCI America
Description: N-[(9H-Fluoren-9-ylmethoxy)carbonyl]-N-methyl-L-leucine, Purity: >98.0%(HPLC)(T), CAS number: 103478-62-2, Molecular Formula: C22H25NO4, Molecular Weight: 367.45, Synonym: Fmoc-N-Me-Leu-OH, N-Fmoc-N-methyl-L-leucine, Size: 1G


Supplier: Thermo Scientific Chemicals
Description: N-Fmoc-N-methyl-L-leucine, 98%
Catalog Number: (CAAAH59563-03)
Supplier: Thermo Scientific Chemicals

Supplier: Bachem Americas
Description: Sequence: Fmoc-N-Me-Leu-OH

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