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SAB1403949

Sigma-Aldrich

Monoclonal Anti-HSPA1B antibody produced in mouse

clone 2D11, purified immunoglobulin, buffered aqueous solution

Synonym(s):

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

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

2D11, monoclonal

form

buffered aqueous solution

mol wt

antigen ~35.02 kDa

species reactivity

rat, human, mouse

technique(s)

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

isotype

IgG2aκ

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... HSPA1B(3304)

General description

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)

Immunogen

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

Physical form

Solution in phosphate buffered saline, pH 7.4

Disclaimer

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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Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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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