NeuroMab™ Mouse Anti-ITGAM Monoclonal Antibody (CBP1560)

Product Overview

Description

It is a 20kDa water-soluble main structural protein and a member of the heat shock protein family, named HSPB5. It functions as a molecular chaperone and is believed to play a role in maintaining the transparency/refractive index of the lens. In addition to αA and αB lens proteins are involved in the prevention of protein precipitation in the eye and cataract formation, α lens protein has also been proven in other tissues including the heart, brain, kidney, spleen and thymus.

Immunogen

Human alpha B crystallin AA 1-175.

Species Reactivity

Human; Mouse

Clonality

Monoclonal

Host Species

Mouse

Isotype

IgG2b

Clone Number

CBP1560

Applications

WB; ELISA

Application Notes

WB (1/1000-1/2000)

Relevant Diseases

Alexander's Disease

Research Areas

Growth and Development

Conjugation

Unconjugated; APC; PE; HRP; Biotin; FITC; Alexa Fluor 488; Alexa Fluor 700; Alexa Fluor 647; Alexa Fluor 750; Alexa Fluor 594; Alexa Fluor 350; Alexa Fluor 1354

Product Properties

Form

Liquid

Formulation

PBS
0.02% Sodium Azide
10% Glycerol

Concentration

1 mg/ml

Purification

Purified IgG prepared by affinity chromatography on Protein G from ascites.

Endotoxin Level

Low Endotoxin

Shipping

The product is shipped at 4°C. Upon receipt, store it immediately at the temperature recommended below.

Storage

Store at +4°C or at -20°C if preferred. Storage in frost-free freezers is not recommended. This product should be stored undiluted. Avoid repeated freezing and thawing as this may denature the antibody. Should this product contain a precipitate we recommend micr°Centrifugation before use.

Target

CD11b

Official Name

ITGAM

Full Name

Integrin alpha M

Alternative Names

ITGAM; CD11B; CR3A; MAC-1; MAC1A; MO1A; SLEB6; integrin subunit alpha M

Gene ID

3684 (Human); 16409 (Mouse); 25021 (Rat)

Uniprot ID

P11215 (Human); P05555 (Mouse)

References

1. van Nierop, G.P. et al. (2015) Intrathecal CD8 T-cells of multiple sclerosis patients recognize lytic Epstein-Barr virus proteins. 2. Perng, M.D. et al. (1999) The cardiomyopathy and lens cataract mutation in alphaB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro.

Publications