Alpha-Crystallin Homolog (Mb sHSP) Hexadecamer Protein

This soluble and active alpha crystallin homolog from Methanococcoides burtonii was recombinantly produced in E. coli, posesses non-native protein salvage activity, and forms polydisperse complexes with anti aggregation properties.

Methanococcoides burtonii is a methylotrophic methanogenic archaeon which has adapted to live in temperatures that are permanantly at 1-2C. While the alpha-Crystallin Homolog (Mb sHSP) gene originated from a cold-adapted microorganism, it encodes a sHsp with extremely efficient and versatile chaperone activity, preventing protein aggregation or loss of enzyme activity even at elevated temperatures.

From the laboratory of Frank T. Robb, PhD, University of Maryland, Baltimore, Institute of Marine and Environmental Technology (IMET).

Catalog Number Product DataSheet Size AVAILABILITY Price Qty
EMD005
Alpha-Crystallin Homolog (Mb sHSP) Hexadecamer Protein
25ug In stock
Regular Price:$300.00
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Specifications

Product Type: Protein
Name: alpha crystallin homolog Mb SHSP
Accession ID: P02489
Source: E. coli BL21
Molecular Weight: 20 kDa
Amino Acid Sequence: MKFGLVRRGSSDVSRWDPFDEIRQTQEHLNQLLREVSPFGGLFEGKSRAPLMDIKEEDNN VIVTTDLPGIDKEDVEISVNNNILEIHAEFKKESESEKEGYVQKERTYSSFSRSAVLPSV VSDEGVKAKLEAGVLTITLPKTKAEEKTKIKIE
Purity: 100
Buffer: HEPES 50 mM, pH7.5
Concentration: 1 mg/mL
Activity: Protection of Bovine glutamate dehydrogenase at 42C
Suggested Amount per Experiment: 50 ng
Comments: Stable to 60C
Storage: -80C
Shipped: Dry Ice

Provider
From the laboratory of Frank T. Robb, PhD, University of Maryland, Baltimore, Institute of Marine and Environmental Technology (IMET)
References
  1. Laksanalamai P, Narayan S, Luo H, Robb FT (2009) Chaperone action of a versatile small heat shock protein from Methanococcoides burtonii, a cold adapted archaeon. Proteins 75(2):275-81

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