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Merck
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Documenti fondamentali

SAB1403949

Sigma-Aldrich

Monoclonal Anti-HSPA1B antibody produced in mouse

clone 2D11, purified immunoglobulin, buffered aqueous solution

Sinonimo/i:

FLJ54328, HSP70-1B, HSP70-2, HSPA1A

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About This Item

Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

mouse

Livello qualitativo

Coniugato

unconjugated

Forma dell’anticorpo

purified immunoglobulin

Tipo di anticorpo

primary antibodies

Clone

2D11, monoclonal

Stato

buffered aqueous solution

PM

antigen ~35.02 kDa

Reattività contro le specie

rat, human, mouse

tecniche

capture ELISA: suitable
immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable
indirect ELISA: suitable
proximity ligation assay: suitable
western blot: 1-5 μg/mL

Isotipo

IgG2aκ

N° accesso NCBI

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... HSPA1B(3304)

Descrizione generale

This intronless gene encodes a 70kDa heat shock protein which is a member of the heat shock protein 70 family. In conjuction with other heat shock proteins, this protein stabilizes existing proteins against aggregation and mediates the folding of newly translated proteins in the cytosol and in organelles. It is also involved in the ubiquitin-proteasome pathway through interaction with the AU-rich element RNA-binding protein 1. The gene is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which encode similar proteins. (provided by RefSeq)

Immunogeno

HSPA1B (NP_005336, 531 a.a. ~ 611 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.

Sequence
VQRERVSAKNALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGLY

Stato fisico

Solution in phosphate buffered saline, pH 7.4

Esclusione di responsabilità

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


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Ching-Chi Chiu et al.
Molecular neurobiology, 56(6), 3835-3853 (2018-08-09)
PARK14 patients with homozygous (D331Y) PLA2G6 mutation display motor deficits of pure early-onset Parkinson's disease (PD). The aim of this study is to investigate the pathogenic mechanism of mutant (D331Y) PLA2G6-induced PD. We generated knockin (KI) mouse model of PARK14
Sangita Maiti Dutta et al.
Environmental monitoring and assessment, 186(12), 8961-8967 (2014-09-23)
Expression of the stress biomarkers 70-kDa heat shock proteins (Hsp70) and manganese superoxide dismutase (MnSOD) was measured as the molecular basis of adaptive response against increased experimental temperatures (32-40 °C for a span of 24-72 h) on the fresh water molluscan species
Jianyue Wu et al.
Experimental and therapeutic medicine, 8(3), 893-898 (2014-08-15)
The present study aimed to investigate the effect of NVP-BEP800, a novel heat shock protein (Hsp) 90 inhibitor of the 2-aminothieno[2,3-d]pyrimidine class, in combination with radiation on glioblastoma cells. T98G human glioblastoma cells were treated with dimethyl sulfoxide (DMSO), NVP-BEP800
Uwe Paasch et al.
International journal of hyperthermia : the official journal of European Society for Hyperthermic Oncology, North American Hyperthermia Group, 30(4), 245-249 (2014-07-16)
Diode laser-based skin heating has been shown to minimise scars by interfering with wound healing responses through the induction of heat shock proteins (HSP). HSP are also induced after ablative fractional laser (AFXL) wound healing. AFXL itself is highly recommended
Silvia Carloni et al.
Journal of pineal research, 57(2), 192-199 (2014-07-02)
Conditions that interfere with the endoplasmic reticulum (ER) functions cause accumulation of unfolded proteins in the ER lumen, referred to as ER stress, and activate a homeostatic signaling network known as unfolded protein response (UPR). We have previously shown that

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