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Goat Anti-Mouse IgG, Human ads-HRP antibody


Antibody ID


Target Antigen

mouse IgG


SouthernBiotech Go To Vendor

Cat Num


Proper Citation

(SouthernBiotech Cat# 1030-05, RRID:AB_2619742)


polyclonal antibody

Host Organism


Publications that use this research resource

Influenza Infection in Humans Induces Broadly Cross-Reactive and Protective Neuraminidase-Reactive Antibodies.

  • Chen YQ
  • Cell
  • 2018 Apr 5

Literature context: Southern Biotech Cat# 2050-08; RRID:AB_2619742 Goat anti-human IgG-BIOT MABTEC


Antibodies to the hemagglutinin (HA) and neuraminidase (NA) glycoproteins are the major mediators of protection against influenza virus infection. Here, we report that current influenza vaccines poorly display key NA epitopes and rarely induce NA-reactive B cells. Conversely, influenza virus infection induces NA-reactive B cells at a frequency that approaches (H1N1) or exceeds (H3N2) that of HA-reactive B cells. NA-reactive antibodies display broad binding activity spanning the entire history of influenza A virus circulation in humans, including the original pandemic strains of both H1N1 and H3N2 subtypes. The antibodies robustly inhibit the enzymatic activity of NA, including oseltamivir-resistant variants, and provide robust prophylactic protection, including against avian H5N1 viruses, in vivo. When used therapeutically, NA-reactive antibodies protected mice from lethal influenza virus challenge even 48 hr post infection. These findings strongly suggest that influenza vaccines should be optimized to improve targeting of NA for durable and broad protection against divergent influenza strains.

Funding information:
  • NCRR NIH HHS - M01RR00046(United States)
  • NIAID NIH HHS - HHSN272201400005C()
  • NIAID NIH HHS - HHSN272201400008C()
  • NIAID NIH HHS - U19 AI057266()
  • NIAID NIH HHS - U19 AI082724()
  • NIAID NIH HHS - U19 AI109946()

α-synuclein Induces Mitochondrial Dysfunction through Spectrin and the Actin Cytoskeleton.

  • Ordonez DG
  • Neuron
  • 2018 Jan 3

Literature context: P SouthernBiotech Cat# 1030-05; RRID:AB_2619742 Goat anti-mouse Alexa Fluor 488


Genetics and neuropathology strongly link α-synuclein aggregation and neurotoxicity to the pathogenesis of Parkinson's disease and related α-synucleinopathies. Here we describe a new Drosophila model of α-synucleinopathy based on widespread expression of wild-type human α-synuclein, which shows robust neurodegeneration, early-onset locomotor deficits, and abundant α-synuclein aggregation. We use results of forward genetic screening and genetic analysis in our new model to demonstrate that α-synuclein expression promotes reorganization of the actin filament network and consequent mitochondrial dysfunction through altered Drp1 localization. Similar changes are present in a mouse α-synucleinopathy model and in postmortem brain tissue from patients with α-synucleinopathy. Importantly, we provide evidence that the interaction of α-synuclein with spectrin initiates pathological alteration of the actin cytoskeleton and downstream neurotoxicity. These findings suggest new therapeutic approaches for α-synuclein induced neurodegeneration.

Funding information:
  • NCI NIH HHS - U01 CA111275(United States)
  • NIA NIH HHS - R01 AG044113()
  • NICHD NIH HHS - U54 HD090255()
  • NIGMS NIH HHS - R01 GM084947()
  • NIH HHS - P40 OD018537()
  • NINDS NIH HHS - R01 NS083391()
  • NINDS NIH HHS - R01 NS086074()
  • NINDS NIH HHS - R01 NS092093()
  • NINDS NIH HHS - R01 NS098821()

Activation of Ras-ERK Signaling and GSK-3 by Amyloid Precursor Protein and Amyloid Beta Facilitates Neurodegeneration in Alzheimer's Disease.

  • Kirouac L
  • eNeuro
  • 2017 Oct 27

Literature context: IgG (Southern Biotech, 1030-05, RRID:AB_2619742), HRP-conjugated goat anti-rabb


It is widely accepted that amyloid β (Aβ) generated from amyloid precursor protein (APP) oligomerizes and fibrillizes to form neuritic plaques in Alzheimer's disease (AD), yet little is known about the contribution of APP to intracellular signaling events preceding AD pathogenesis. The data presented here demonstrate that APP expression and neuronal exposure to oligomeric Aβ42 enhance Ras/ERK signaling cascade and glycogen synthase kinase 3 (GSK-3) activation. We find that RNA interference (RNAi)-directed knockdown of APP in B103 rat neuroblastoma cells expressing APP inhibits Ras-ERK signaling and GSK-3 activation, indicating that APP acts upstream of these signal transduction events. Both ERK and GSK-3 are known to induce hyperphosphorylation of tau and APP at Thr668, and our findings suggest that aberrant signaling by APP facilitates these events. Supporting this notion, analysis of human AD brain samples showed increased expression of Ras, activation of GSK-3, and phosphorylation of APP and tau, which correlated with Aβ levels in the AD brains. Furthermore, treatment of primary rat neurons with Aβ recapitulated these events and showed enhanced Ras-ERK signaling, GSK-3 activation, upregulation of cyclin D1, and phosphorylation of APP and tau. The finding that Aβ induces Thr668 phosphorylation on APP, which enhances APP proteolysis and Aβ generation, denotes a vicious feedforward mechanism by which APP and Aβ promote tau hyperphosphorylation and neurodegeneration in AD. Based on these results, we hypothesize that aberrant proliferative signaling by APP plays a fundamental role in AD neurodegeneration and that inhibition of this would impede cell cycle deregulation and neurodegeneration observed in AD.

Activation of the unfolded protein response promotes axonal regeneration after peripheral nerve injury.

  • Oñate M
  • Sci Rep
  • 2016 Feb 24

Literature context: d -mouse IgG (RRID: AB_2687483, RRID: AB_2619742) (1:5,000, Southern Biotech, Bi


Although protein-folding stress at the endoplasmic reticulum (ER) is emerging as a driver of neuronal dysfunction in models of spinal cord injury and neurodegeneration, the contribution of this pathway to peripheral nerve damage remains poorly explored. Here we targeted the unfolded protein response (UPR), an adaptive reaction against ER stress, in mouse models of sciatic nerve injury and found that ablation of the transcription factor XBP1, but not ATF4, significantly delay locomotor recovery. XBP1 deficiency led to decreased macrophage recruitment, a reduction in myelin removal and axonal regeneration. Conversely, overexpression of XBP1s in the nervous system in transgenic mice enhanced locomotor recovery after sciatic nerve crush, associated to an improvement in key pro-regenerative events. To assess the therapeutic potential of UPR manipulation to axonal regeneration, we locally delivered XBP1s or an shRNA targeting this transcription factor to sensory neurons of the dorsal root ganglia using a gene therapy approach and found an enhancement or reduction of axonal regeneration in vivo, respectively. Our results demonstrate a functional role of specific components of the ER proteostasis network in the cellular changes associated to regeneration and functional recovery after peripheral nerve injury.