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 Size AVAILABILITY Price Qty
EMD005
Alpha-Crystallin Homolog (Mb sHSP) Hexadecamer Protein, 25ug
25ug In stock
Price: $256.00
Specifications
Name: alpha crystallin homolog Mb SHSP
Accession ID: MBUR_RS10265
Molecular Weight: 20 kDa
Amino Acid Sequence: MKFGLVRRGSSDVSRWDPFDEIRQTQEHLNQLLREVSPFGGLFEGKSRAPLMDIKEEDNN VIVTTDLPGIDKEDVEISVNNNILEIHAEFKKESESEKEGYVQKERTYSSFSRSAVLPSV VSDEGVKAKLEAGVLTITLPKTKAEEKTKIKIE
Buffer: HEPES 50 mM, pH7.5
Source: E. coli BL21
Purity: 100
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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