Lambda Ig light chain IHC Antibody
- Known as:
- Lambda Ig light epitope Immunohistochemistry Antibody
- Catalog number:
- c10141
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- IHC World
- Gene target:
- Lambda light chain IHC Antibody
Ask about this productRelated genes to: Lambda Ig light chain IHC Antibody
- Gene:
- FCGRT NIH gene
- Name:
- Fc fragment of IgG receptor and transporter
- Previous symbol:
- -
- Synonyms:
- FCRN, alpha-chain
- Chromosome:
- 19q13.33
- Locus Type:
- gene with protein product
- Date approved:
- 1995-08-23
- Date modifiied:
- 2016-10-05
Related products to: Lambda Ig light chain IHC Antibody
Related articles to: Lambda Ig light chain IHC Antibody
- Late gestation heat stress in dairy cows reduces offspring's capacity to absorb colostrum immunoglobulin G (IgG). This study evaluated small intestine histomorphology, cellular turnover, and gene expression profiles of in utero heat stressed versus in utero cooled heifers at birth. For the last 54 ± 5 d of gestation, pregnant dams were housed in a free stall barn and were either heat stressed (shade of the barn) or cooled (shade, fans, and water soakers) during a subtropical summer. Heat stressed pregnant cows responded physiologically by elevating respiration rate and skin temperature relative to their cooled counterparts (+25 breaths per minute and +1.7°C) and gave birth to heifers who were in utero heat stressed (IUHS) or in utero cooled (IUCL), respectively (n = 8/group). Heifers were euthanized at birth (before colostrum feeding) to harvest gastrointestinal tract (GIT) tissues. Histomorphology (villi length, width, and crypt depth) was assessed from duodenum, jejunum, and ileum tissue portions of the GIT, via H&E staining. Cellular turnover (death/proliferation) was quantified in crypt and villi regions of the jejunum and ileum via immunohistochemistry. The fluorescence intensity of tight junction proteins (occludin and zona occludens-1) and the neonatal Fc receptor were assessed in the jejunum and ileum. Jejunum and ileum tissue samples were snap-frozen for gene expression analysis of endosomal (FCGRT, DAB2, MAMDC4), tight junction (TJP1, TJP2, TJP3, OCLN, CLDN1), heat shock (HSP90AA1, HSF1), and autophagy (ATG3, ATG5) related genes by qPCR. Data were analyzed using PROC MIXED or PROC GLIMMIX. There were no differences in villi length or width across intestinal sections, nor crypt depth in the duodenum and jejunum; however, ileal crypts were shorter in IUHS heifers. No differences between treatments were detected in the rate of proliferation within either tissue section. Apoptosis was increased crypts of the jejunum and villi of the ileum in IUHS heifers, but unchanged in ileal crypts and jejunal villi. Occludin abundance tended to be reduced in the jejunum of IUHS heifers only, whereas other tight junction proteins were largely unchanged. Abundance of the neonatal Fc receptor was decreased in the jejunum of IUHS heifers and not different between treatments in the ileum. Gene expression analysis indicated a tendency for upregulation of CLDN1 and significant downregulation of TJP2 in the jejunum, and a significant upregulation of MAMDC4, ATG5, and HSF1 in the ileum of IUHS heifers. Additionally, expression of tight junction genes OCLN, TJP1, TJP2, and TJP3 were upregulated in the ileum of IUHS heifers. Overall, IUHS had minimal effects on histomorphology but disrupted cellular turnover and tight junction regulation, with reduced neonatal Fc receptor abundance in the jejunum, providing insight to mechanisms that may be responsible for impaired colostrum IgG absorption. These findings suggest that impaired passive immunity in IUHS calves may be attributed to disruptions in intestinal cellular and molecular function rather than gross structural changes. - Source: PubMed
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Xu YueLi XiaoleiNan Guangxian - Broadly neutralising antibodies (bNAbs) represent a promising long-acting modality for HIV prevention. However, substantial interindividual pharmacokinetic variability poses a threat to real-world efficacy. This review investigates the impact of systemic inflammation, driven by the high prevalence of sexually transmitted infections (STIs), co-endemic pathogens, and metabolic activation, on bNAb persistence, particularly within the vulnerable demographic of women in sub-Saharan Africa. We aim to bridge the gap between neonatal fragment crystallisable receptor (FcRn) biology and clinical pharmacokinetic observations to identify why certain individuals clear bNAbs faster than others. - Source: PubMed
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Khumalo AndilePillay SanjaliMohan JivankaMahomed SharanaArchary Derseree - Elucidating the quaternary structures of protein complexes under physiological conditions remains a central challenge for structural biology. Here, we introduce an integrative analytical pipeline that combines size exclusion chromatography (SEC), Taylor dispersion analysis (TDA), native mass spectrometry (nMS), and artificial intelligence to resolve macromolecular architectures under near-native solution conditions. The workflow begins with the SEC-based separation of heterogeneous mixtures, followed by online TDA in a PEEK capillary to probe hydrodynamic behavior via laminar-flow-induced dispersion. By deconvolving pre- and postdispersion chromatograms, a system transfer function is derived and subjected to Gaussian fitting to yield precise measurements of hydrodynamic radii. These experimentally derived radii are subsequently applied as biophysical constraints in an AlphaFold 3-based structural selection process. We validated this method using a six-protein model mixture, demonstrating its ability to simultaneously determine the hydrodynamic radii of individual components within complex mixtures. The methodology was further applied to three protein complexes (FCGRT-B2M, streptavidin, and concanavalin A), allowing for the precise measurement of their oligomeric hydrodynamic radii and the determination of their quaternary structures. By bridging high-resolution analytical chemistry with AI-driven structural prediction, this strategy offers a robust experimentally grounded framework for characterizing macromolecular assemblies. - Source: PubMed
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