You Searched For: myo-Inositol

Catalog Number: (ABCA_AB11083-50UL)

Supplier: Abcam

Description: Anti-Slow Skeletal Myosin Heavy chain Mouse Monoclonal Antibody [clone: NOQ7.5.4D]

New Product

Catalog Number: (10095-496)

Supplier: Proteintech

Description: SYNJ2(Synaptojanin-2) is also named as KIAA0348 and belongs to the synaptojanin family. SYNJ2 encodes an inositol polyphosphate phosphatase that functions in recycling neurotransmitter vesicles and is implicated in spermatogenesis. This protein has 3 isoforms produced by alternative splicing.

Catalog Number: (ABCA_AB300647-100U)

Supplier: Abcam

Description: Anti-non-muscle Myosin IIB/MYH10 Rat Monoclonal Antibody [clone: EPR22564-23]

New Product

Catalog Number: (76116-372)

Supplier: Bioss

Description: Inositol 1,4,5-triphosphate (IP3) functions as a second messenger for a myriad of extracellular stimuli including hormones, growth factors and neurotransmitters. Receptor tyrosine kinases indirectly increase the intracellular levels of IP3 through the activation of phospholipases such as phospholipase C (PLC), which convert phosphatidylinositol-4,5 bisphosphate into IP3 and diacylglycerol (DAG). The inositol 1,4,5-triphosphate receptor, IP3R, acts as an inositol triphosphate (IP3)-gated calcium release channel in a variety of cell types. Three IP3 receptor subtypes have been described and are designated IP3R-I, IP3R-II and IP3R-III. IP3R-I is the predominant IP3R subtype expressed in neuronal tissues and the central nervous system, but is also expressed at high levels in the liver.

Catalog Number: (10104-276)

Supplier: Prosci

Description: ITPK1 is the kinase that can phosphorylate various inositol polyphosphate such as Ins (3,4,5,6)P4 or Ins (1,3,4)P3. It may also act as an isomerase that interconverts the inositol tetraphosphate isomers Ins (1,3,4,5)P4 and Ins (1,3,4,6)P4 in the presence of ADP and magnesium. It probably acts as the rate-limiting enzyme of the InsP6 pathway. ITPK1 modifies TNF-alpha-induced apoptosis by interfering with the activation of TNFRSF1A-associated death domain.

Catalog Number: (10374-870)

Supplier: Bioss

Description: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. It is a crucial enzyme in transmembrane signaling.

Catalog Number: (10447-678)

Supplier: Bioss

Description: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes.

Catalog Number: (10447-676)

Supplier: Bioss

Description: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes.

Catalog Number: (ABCA_AB241068-100U)

Supplier: Abcam

Description: Anti-non-muscle Myosin IIA Rabbit Polyclonal Antibody

New Product

Catalog Number: (89330-526)

Supplier: Genetex

Description: Rabbit Polyclonal antibody to HISPPD1 (inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2)

Catalog Number: (10452-228)

Supplier: Bioss

Description: Members of the Id family of basic helix-loop-helix (bHLH) proteins include Id1 (1–3), Id2 (4), Id3 and Id4 (5). They are ubiquitously expressed and dimerize with members of the class A and B HLH proteins (1–5). Due to the absence of the basic region, the resulting heterodimers cannot bind DNA. The Id-type proteins thus appear to negatively regulate DNA binding of bHLH proteins. Since Id1 inhibits DNA binding of E12 and Myo D, it apparently functions to inhibit muscle-specific gene expression. Under conditions that facilitate muscle cell differentiation, the Id protein levels fall, allowing E12 and/or E47 to form heterodimers with Myo D and myogenin, which in turn activate myogenic differentiation. It has been shown that expression of each of the Id proteins is strongly dependent on growth factor activation and that reduction of Id mRNA levels by antisense oligonucleotides leads to a delayed reentry of arrested cells into the cell cycle following growth factor stimulation.

Catalog Number: (10452-232)

Supplier: Bioss

Description: Members of the Id family of basic helix-loop-helix (bHLH) proteins include Id1 (1–3), Id2 (4), Id3 and Id4 (5). They are ubiquitously expressed and dimerize with members of the class A and B HLH proteins (1–5). Due to the absence of the basic region, the resulting heterodimers cannot bind DNA. The Id-type proteins thus appear to negatively regulate DNA binding of bHLH proteins. Since Id1 inhibits DNA binding of E12 and Myo D, it apparently functions to inhibit muscle-specific gene expression. Under conditions that facilitate muscle cell differentiation, the Id protein levels fall, allowing E12 and/or E47 to form heterodimers with Myo D and myogenin, which in turn activate myogenic differentiation. It has been shown that expression of each of the Id proteins is strongly dependent on growth factor activation and that reduction of Id mRNA levels by antisense oligonucleotides leads to a delayed reentry of arrested cells into the cell cycle following growth factor stimulation.

Catalog Number: (10452-226)

Supplier: Bioss

Description: Members of the Id family of basic helix-loop-helix (bHLH) proteins include Id1 (1–3), Id2 (4), Id3 and Id4 (5). They are ubiquitously expressed and dimerize with members of the class A and B HLH proteins (1–5). Due to the absence of the basic region, the resulting heterodimers cannot bind DNA. The Id-type proteins thus appear to negatively regulate DNA binding of bHLH proteins. Since Id1 inhibits DNA binding of E12 and Myo D, it apparently functions to inhibit muscle-specific gene expression. Under conditions that facilitate muscle cell differentiation, the Id protein levels fall, allowing E12 and/or E47 to form heterodimers with Myo D and myogenin, which in turn activate myogenic differentiation. It has been shown that expression of each of the Id proteins is strongly dependent on growth factor activation and that reduction of Id mRNA levels by antisense oligonucleotides leads to a delayed reentry of arrested cells into the cell cycle following growth factor stimulation.

Catalog Number: (10452-214)

Supplier: Bioss

Description: Members of the Id family of basic helix-loop-helix (bHLH) proteins include Id1 (1–3), Id2 (4), Id3 and Id4 (5). They are ubiquitously expressed and dimerize with members of the class A and B HLH proteins (1–5). Due to the absence of the basic region, the resulting heterodimers cannot bind DNA. The Id-type proteins thus appear to negatively regulate DNA binding of bHLH proteins. Since Id1 inhibits DNA binding of E12 and Myo D, it apparently functions to inhibit muscle-specific gene expression. Under conditions that facilitate muscle cell differentiation, the Id protein levels fall, allowing E12 and/or E47 to form heterodimers with Myo D and myogenin, which in turn activate myogenic differentiation. It has been shown that expression of each of the Id proteins is strongly dependent on growth factor activation and that reduction of Id mRNA levels by antisense oligonucleotides leads to a delayed reentry of arrested cells into the cell cycle following growth factor stimulation.

Catalog Number: (10452-236)

Supplier: Bioss

Description: Members of the Id family of basic helix-loop-helix (bHLH) proteins include Id1 (1–3), Id2 (4), Id3 and Id4 (5). They are ubiquitously expressed and dimerize with members of the class A and B HLH proteins (1–5). Due to the absence of the basic region, the resulting heterodimers cannot bind DNA. The Id-type proteins thus appear to negatively regulate DNA binding of bHLH proteins. Since Id1 inhibits DNA binding of E12 and Myo D, it apparently functions to inhibit muscle-specific gene expression. Under conditions that facilitate muscle cell differentiation, the Id protein levels fall, allowing E12 and/or E47 to form heterodimers with Myo D and myogenin, which in turn activate myogenic differentiation. It has been shown that expression of each of the Id proteins is strongly dependent on growth factor activation and that reduction of Id mRNA levels by antisense oligonucleotides leads to a delayed reentry of arrested cells into the cell cycle following growth factor stimulation.

Catalog Number: (76118-576)

Supplier: Bioss

Description: Members of the Id family of basic helix-loop-helix (bHLH) proteins include Id1 (13), Id2 (4), Id3 and Id4 (5). They are ubiquitously expressed and dimerize with members of the class A and B HLH proteins (15). Due to the absence of the basic region, the resulting heterodimers cannot bind DNA. The Id-type proteins thus appear to negatively regulate DNA binding of bHLH proteins. Since Id1 inhibits DNA binding of E12 and Myo D, it apparently functions to inhibit muscle-specific gene expression. Under conditions that facilitate muscle cell differentiation, the Id protein levels fall, allowing E12 and/or E47 to form heterodimers with Myo D and myogenin, which in turn activate myogenic differentiation. It has been shown that expression of each of the Id proteins is strongly dependent on growth factor activation and that reduction of Id mRNA levels by antisense oligonucleotides leads to a delayed reentry of arrested cells into the cell cycle following growth factor stimulation.