Analysis Note

ControlNeuro2A cell lysate

Application

Detect TMEM132A using this rabbit polyclonal antibody, Anti-TMEM132A Antibody validated for use in western blotting & IHC (Paraffin).

Research CategoryApoptosis & Cancer

Research Sub CategoryApoptosis - Additional

Immunohistochemistry Analysis: A 1:500 dilution from a representative lot detected Neuro2A in human cerebellum and thalamus tissues.

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.

General description

Transmembrane protein 132A (TMEM132A), or HSPA5-binding protein 1 (HSPA5BP1), is thought to be involved in embryonic and postnatal development of the brain, and the increased cell death resistance induced by serum starvation in cultured cells. TMEM132A is known to regulate cAMP-induced GFAP gene expression through phosphorylation of STAT3.

Immunogen

Epitope: Cytoplasmic domain

KLH-conjugated linear peptide corresponding to the cytoplasmic domain of human TMEM132A.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Physical form

Affinity purified

Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Quality

Evaluated by Western Bloting in Neuro2A cell lysate.

Western Blotting Analysis: 0.1 µg/mL of this antibody detected TMEM132A in 10 µg of Neuro2A cell lysate.

Specificity

This antibody recognizes the cytoplasmic domain of TMEM132A.

Storage and Stability

Stable for 1 year at 2-8°C from date of receipt.

Target description

~140 kDa observed. The calculated molecular weight of this protein is 110kDa This protein has been observed at ~135 and ~170 kDa due to glycosylation, myristoylation, and phosphorylation (Kentaro, O. H., et al. (2003). J Biol Chem. 278(12): 10531-10537.). Uncharacterized band(s) may be observed in some cell lysates.