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Human Monoclonal GAPDHS Primary Antibody for IHC (p), ELISA - ABIN565269
Shchutskaya, Elkina, Kuravsky, Bragina, Schmalhausen: Investigation of glyceraldehyde-3-phosphate dehydrogenase from human sperms. in Biochemistry. Biokhimii?a 2008
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Human Polyclonal GAPDHS Primary Antibody for FACS, IHC (p) - ABIN6243346
Maselli, Hales, Chan, Robaire: Exposure to bleomycin, etoposide, and cis-platinum alters rat sperm chromatin integrity and sperm head protein profile. in Biology of reproduction 2012
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Human Polyclonal GAPDHS Primary Antibody for IF (p), IHC (p) - ABIN1714543
Zhang, Zhang, Zi: Overexpression of microRNA-141 relieves chronic constriction injury-induced neuropathic pain via targeting high-mobility group box 1. in International journal of molecular medicine 2015
Human Polyclonal GAPDHS Primary Antibody for IHC, IHC (p) - ABIN4313554
Djureinovic, Fagerberg, Hallström, Danielsson, Lindskog, Uhlén, Pontén: The human testis-specific proteome defined by transcriptomics and antibody-based profiling. in Molecular human reproduction 2014
GAPDS overexpression antagonize high glucose-induced apoptosis by controlling reactive oxygen species accumulation in TM3 cells.
It is assumed that the deficiency in GAPDS observed in most dysplasia of the fibrous sheath sperm samples is ascribable to a disorder in the regulation of GAPDS expression caused by the mutation in the intron region of GAPDS gene.
This result implies that GAPDHS participates in specific signal-transduction pathways.
Structural basis for the NAD binding cooperativity and catalytic characteristics of sperm-specific glyceraldehyde-3-phosphate dehydrogenase
GAPDS protein was expressed in both Sertoli cells and elongated sperms. The expression of GAPDS gradually increased with age in the epididymis.
Data indicate that the positive expression of studied genes fertilization rate for GAPDHS positive subset was 66%, ACR - 71%, SPATA22 - 68%, MND1 - 70%, pregnancy rates were 8%, 6%, 18% and 36% respectively.
the expression of GAPDS in melanoma cells may facilitate glycolysis and prevent the induction of apoptosis.
The chaperonin TRiC was shown to assist an ATP-dependent refolding of recombinant forms of GAPDS.
Structure and kinetic characterization of human sperm-specific glyceraldehyde-3-phosphate dehydrogenase, GAPDS.
Human his-GAPDHS expressed in baculovirus-infected insect cells is homotetrameric.
Data suggest that high stability of the sperm-specific GAPDS is of importance for the efficiency of fertilization.
We have concluded that a simple nuclear localization of GAPDH does not induce apoptosis, and that MPP+-induced apoptosis is not caused by nuclear translocation of GAPDH.
Comparative study of the amino acid sequences of mammalian GAPDs revealed conservative cysteine residues (C21, C94, and C150) that are specific for the sperm isoenzyme and absent in the somatic isoenzyme.
Characterization of the rat GAPDHS and comparison to the human and mouse enzymes.
GAPD2 enzymatic activity is present in human sperm. GAPD2 is tightly bound to sperm and most enzymatic activity is not released by permeabilization with CHAPS detergent. GAPD2 is restricted in location to the principal piece of the sperm flagellum.
These results identify multiple signaling and metabolic defects that are likely contributors to male infertility and the absence of progressive sperm motility seen in mice lacking GAPDHS.
TB-RBP is involved in the posttranscriptional regulation of Gapds gene expression during spermiogenesis.
Gapds(-/-) males were infertile and had profound defects in sperm motility, exhibiting sluggish movement without forward progression.
This gene encodes a protein belonging to the glyceraldehyde-3-phosphate dehydrogenase family of enzymes that play an important role in carbohydrate metabolism. Like its somatic cell counterpart, this sperm-specific enzyme functions in a nicotinamide adenine dinucleotide-dependent manner to remove hydrogen and add phosphate to glyceraldehyde 3-phosphate to form 1,3-diphosphoglycerate. During spermiogenesis, this enzyme may play an important role in regulating the switch between different energy-producing pathways, and it is required for sperm motility and male fertility.
glyceraldehyde-3-phosphate dehydrogenase, spermatogenic
, glyceraldehyde-3-phosphate dehydrogenase, testis-specific-like
, glyceraldehyde-3-phosphate dehydrogenase, testis-specific
, spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase 2
, spermatogenic glyceraldehyde-3-phosphate dehydrogenase
, glyceraldehyde-3-phosphate dehydrogenase type 2
, glyceraldehyde 3-phosphate dehydrogenase 2
, glyceraldehyde 3-phosphate dehydrogenase, testis-specific